U.S. patent application number 11/214372 was filed with the patent office on 2007-09-06 for trophic factor combinations for nervous system treatment.
Invention is credited to Francis J. Golder, Jonathan F. McAnulty, Gordon S. Mitchell, Christopher J. Murphy.
Application Number | 20070207209 11/214372 |
Document ID | / |
Family ID | 38471745 |
Filed Date | 2007-09-06 |
United States Patent
Application |
20070207209 |
Kind Code |
A1 |
Murphy; Christopher J. ; et
al. |
September 6, 2007 |
Trophic factor combinations for nervous system treatment
Abstract
The present invention relates to a composition including an
effective amount of at least one of an antimicrobial peptide and a
substance having an antimicrobial peptide effect and an effective
amount of a neurotrophin. The composition can also include an
effective amount of at least one of a growth factor and a
neuropeptide. The present invention also relates a method of
treating an injury to a nervous system of an animal that includes
the steps of identifying the injury to the nervous system and
applying to the injury an effective amount of at least one of
antimicrobial peptide and a substance having an antimicrobial
peptide effect. The method can also include applying an effective
amount of one or more trophic factors selected from the group
consisting of a growth factor, a neurotrophin, and a neuropeptide
to the injury.
Inventors: |
Murphy; Christopher J.;
(Madison, WI) ; McAnulty; Jonathan F.; (Oregon,
WI) ; Mitchell; Gordon S.; (Madison, WI) ;
Golder; Francis J.; (Stoughton, WI) |
Correspondence
Address: |
WHYTE HIRSCHBOECK DUDEK S C
555 EAST WELLS STREET
SUITE 1900
MILWAUKEE
WI
53202
US
|
Family ID: |
38471745 |
Appl. No.: |
11/214372 |
Filed: |
August 29, 2005 |
Related U.S. Patent Documents
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Application
Number |
Filing Date |
Patent Number |
|
|
60604912 |
Aug 27, 2004 |
|
|
|
Current U.S.
Class: |
424/484 ;
514/17.7; 514/4.8; 514/8.4; 514/8.6 |
Current CPC
Class: |
A61K 9/06 20130101; A61K
38/046 20130101; A61K 38/1709 20130101; A61K 38/185 20130101; A61K
38/30 20130101; A61K 38/1709 20130101; A61K 38/185 20130101; A61L
27/54 20130101; A61K 38/30 20130101; A61L 2300/252 20130101; A61L
2300/414 20130101; A61K 2300/00 20130101; A61L 27/52 20130101; A61L
2300/404 20130101; A61K 38/046 20130101; A61K 2300/00 20130101;
A61K 2300/00 20130101; A61K 2300/00 20130101 |
Class at
Publication: |
424/484 ;
514/012 |
International
Class: |
A61K 38/18 20060101
A61K038/18; A61K 38/17 20060101 A61K038/17; A61K 9/14 20060101
A61K009/14 |
Goverment Interests
REFERENCE TO GOVERNMENT GRANT
[0002] This invention was made with United States government
support awarded by the National Institutes of Health, Grant #
HL069064. The United States has certain rights in this invention.
Claims
1. A composition comprising: A. an effective amount of at least one
of an antimicrobial peptide and a substance having an antimicrobial
peptide effect; and B. an effective amount of a neurotrophin.
2. The composition of claim 1, further comprising an effective
amount of at least one of a growth factor and a neuropeptide.
3. The composition of claim 1, further comprising an effective
amount of a growth factor.
4. The composition of claim 3, wherein the antimicrobial peptide is
BNP-1, the neurotrophin is BDNF, and the growth factor is
IGF-1.
5. The composition of claim 1, further comprising an effective
amount of a neuropeptide.
6. The composition of claim 5, wherein the antimicrobial peptide is
BNP-1, the neurotrophin is BDNF, and the neuropeptide is Substance
P.
7. The composition of claim 1, further comprising an effective
amount of a growth factor and an effective amount of a
neuropeptide.
8. The composition of claim 7, wherein the antimicrobial peptide is
BNP-1, the neurotrophin is BDNF, the growth factor is IGF-1, and
the neuropeptide is Substance P.
9. The composition of claim 1, wherein the antimicrobial peptide is
BNP-1 and the neurotrophin is BDNF.
10. The composition of claim 9, further comprising an effective
amount of IGF-1 and an effective amount of Substance P.
11. The composition of claim 1, further comprising a viscous
substance.
12. The composition of claim 1, further comprising a matrix.
13. The composition of claim 10, wherein the matrix comprises a
hydrogel.
14. A method of treating an injury to a nervous system of an
animal, the method comprising: A. identifying the injury to the
nervous system; and B. applying to the injury an effective amount
of at least one of antimicrobial peptide and a substance having an
antimicrobial peptide effect.
15. The method of claim 14, wherein the at least one of an
antimicrobial peptide and a substance having an antimicrobial
peptide effect is combined with an effective amount of one or more
trophic factors selected from the group consisting of a growth
factor, a neurotrophin, and a neuropeptide.
16. The method of claim 14, wherein the injury to the nervous
system comprises a spinal cord injury.
17. The method of claim 14, wherein the applying step produces an
effect on the animal, the effect selected from the group consisting
of reduced pain, neuronal plasticity, a neuroprotective effect,
reduced body weight loss, increased motor recovery, increased
evoked potential amplitudes, and lowered threshold current.
18. A kit comprising: A. at least one of an antimicrobial peptide
and a substance having an antimicrobial peptide effect; and B. a
neurotrophin.
19. The kit of claim 18, further comprising a viscous
substance.
20. The kit of claim 18, further comprising at least one of a
growth factor and a neuropeptide.
Description
CROSS-REFERENCE TO RELATED APPLICATIONS
[0001] This application claims priority under 35 U.S.C.
.sctn.119(e) to U.S. Provisional Patent Application No. 60/604,912,
filed Aug. 27, 2004, the entirety of which is incorporated by
reference herein.
FIELD OF THE INVENTION
[0003] The invention relates to combinations of neurochemically
active agents for treating a nervous system and the methods of
treating a nervous system with the combinatorial treatments.
BACKGROUND OF THE INVENTION
[0004] The nervous system is comprised of two divisions: the
central nervous system (CNS) and the peripheral nervous system
(PNS). The CNS includes the brain and the spinal cord and controls
most functions of the body and mind. The remainder of the nervous
system is the PNS. Nerves of the PNS connect the CNS to sensory
organs (such as the eyes and ears), other organs of the body,
muscles, blood vessels, and glands. The peripheral nerves include
the cranial nerves, the spinal nerves, and roots.
[0005] The CNS controls all voluntary movement, such as movement of
the legs during walking, and all involuntary movement, such as
beating of the heart. The spinal cord connects the body and the
brain by transmitting information to and from the body and the
brain.
[0006] The nervous system can be injured in numerous ways, and
injuries can be traumatic. For instance, sudden physical assault on
a portion of the nervous system results in a traumatic injury. In
the case of a traumatic brain injury, the injury can be focal,
i.e., confined to a specific area of the brain, or diffuse, i.e.,
involving more than one area of the brain.
[0007] Injuries to the nervous system include contusions, which are
bruises of the nervous system, and blood clots. Blood clots can
form in or around the nervous system. For example, when bleeding
occurs between the skull and the brain, the blood forms a clot.
This puts pressure on the brain, which can lead to changes in brain
function.
[0008] Spinal cord injuries (SCI) are a particular type of injury
to the nervous system. As of the year 2000, approximately 450,000
people in the United States have sustained SCI, with more than
10,000 new cases reported in the United States every year. Motor
vehicle accidents are the leading cause of SCI (44 percent),
followed by acts of violence (24 percent), falls (22 percent),
sports injuries (8 percent), and other causes (2 percent). Of the
10,000 new cases of SCI in the United States each year, 51.7% have
tetraplegia, i.e., injuries to one of the eight cervical segments
of the spinal cord, and 56.7% have paraplegia, i.e., lesions in the
thoracic, lumbar, or sacral regions of the spinal cord. Since 1990,
the most frequent neurologic category is incomplete tetraplegia
(29.5%), followed by complete paraplegia (27.9%), incomplete
paraplegia (21.3%), and complete tetraplegia (18.5%).
[0009] With spinal cord injuries in the neck, significant
impairment of breathing may result. The most frequent site of
spinal injury is the neck or cervical region and, of these, the
major cause of death arises from respiratory complications. For
patients that survive a major spinal cord injury in the neck, they
may spend the rest of their lives depending on an artificial
ventilator or phrenic nerve pacemaker to sustain their lives. For
others with less severe respiratory impairment, they may be able to
breathe normally, but are unable to sigh or breathe deeply and
maintain the integrity of the lung. As a consequence, regions of
the lung will collapse in these patients, causing pneumonia and
allowing other respiratory infections to become established.
Clearly, restoration of normal breathing ability, including deep
breaths and sighs, is a major goal in the treatment of spinal cord
injury patients.
[0010] Injury to the spinal cord and other parts of the nervous
system may be particularly devastating to life and the quality of
life. In addition, injury to the nervous system can engender
serious economic losses to the individual and to society.
Currently, there are few effective treatment options available for
patients with spinal cord injuries, although there are a few
promising indications that physical therapy or chronic intermittent
hypoxia (CIH), may have beneficial effects. Exposure to
intermittent hypoxic episodes has been shown to initiate spinal
protein synthesis. However, studies have also shown that chronic
intermittent hypoxia has other drawbacks as a treatment for spinal
cord injuries. For example, certain CIH treatment methods can cause
systemic hypertension, altered sympathetic chemoreflexes, and
hippocampal cell death by the process of apoptosis.
[0011] Physical training and preconditioning have been used to
treat SCI. Almost all patients with spinal cord injuries can now
achieve a partial return of function with proper physical therapy
that maintains flexibility and function of the muscles and joints,
and strengthens the neural pathways that underlie movement.
Physical therapy can also help reduce the risk of blood clots and
boost the patient's morale. Physical training currently being
investigated includes body weight-supported treadmill training, in
which patients with partial spinal cord injury "walk" on a
treadmill while they are partially supported through the use of a
specially designed harness attached to an overhead lift.
Unfortunately, this type of therapy is very expensive, and efficacy
is far from complete.
SUMMARY OF THE INVENTION
[0012] The invention, which is defined by the claims set out at the
end of this disclosure, is intended to solve at least some of the
problems noted above. A composition is provided that includes an
effective amount of at least one of an antimicrobial peptide and a
substance having an antimicrobial peptide effect. The composition
also includes an effective amount of a neurotrophin.
[0013] In another embodiment, the composition also includes an
effective amount of at least one of a growth factor and a
neuropeptide.
[0014] Also provided is a method of treating an injury to a nervous
system of an animal. In one embodiment, the method includes the
steps of identifying the injury to the nervous system and applying
to the injury an effective amount of at least one of antimicrobial
peptide and a substance having an antimicrobial peptide effect.
[0015] In another embodiment, an injury to the nervous system is
identified. An effective amount of at least one of an antimicrobial
peptide and a substance having an antimicrobial peptide effect is
combined with an effective amount of one or more trophic factors
selected from the group consisting of a growth factor, a
neurotrophin, and a neuropeptide. The combination is applied to the
injury.
[0016] A kit is also provided. In an embodiment, the kit includes
at least one of an antimicrobial peptide and a substance having an
antimicrobial peptide effect. The kit also includes a neurotrophin.
In another embodiment, the kit also includes a viscous substance.
In some embodiments, the kit also includes at least one of a growth
factor and a neuropeptide.
BRIEF DESCRIPTION OF THE DRAWINGS
[0017] Preferred exemplary embodiments of the invention are
illustrated in the accompanying drawings in which:
[0018] FIG. 1 is a graph showing change in body weight at 2 weeks
after spinal cord injury (Y-axis) in two strains of rats, Sprague
Dawley and Lewis (X-axis). For each strain of rats, the body weight
is shown for spinal injury alone (black bar) and for spinal injury
and a trophic factor combination made in accordance with the
invention (grey bar). In addition, corresponding data are shown for
all rats combined.
[0019] FIG. 2 is a graph showing peak neurogram voltages from the
phrenic nerve during inspiration on the side of injury (Y-axis) at
2 weeks post-injury in two strains of rats, Sprague Dawley and
Lewis (X-axis). For each strain of rats, neurogram voltages are
shown for spinal injury alone (black bar) and for spinal injury and
the trophic factor combination (grey bar). In addition,
corresponding data are shown for all rats combined.
[0020] FIG. 3 is a graph showing evoked potential voltage (in
volts) from the phrenic neurogram on the side of injury at 2 weeks
post-injury (Y-axis) in two strains of rats, Sprague Dawley and
Lewis (X-axis). The stimulating current was 1000 uA. For each
strain of rats, evoked potential voltages are shown for spinal
injury alone (black bar) and for spinal injury and the trophic
factor combination (grey bar). In addition, corresponding data are
shown for all rats combined.
[0021] FIG. 4 is a graph showing the stimulating current (in uAmps)
required to evoke potentials in the phrenic nerve on the side of
injury at 2 weeks post-injury (Y-axis) in two strains of rats,
Sprague Dawley and Lewis (X-axis). For each strain of rats,
stimulating currents are shown for spinal injury alone (black bar)
and for spinal injury and the trophic factor combination (grey
bar). In addition, corresponding data are shown for all rats
combined.
[0022] FIG. 5 is a graph showing the change in body mass in grams
at 2 weeks post-injury (Y-axis) in different Lewis rats (X-axis).
The body weight is shown for spinal injury alone (SCI) and for
spinal injury and a trophic factor combination made in accordance
with the invention (SCI+NTs). FIG. 5 also shows change in phrenic
amplitude at 2 weeks post-injury (Y-axis) in the rats (X-axis) for
spinal injury alone (SCI) and for spinal injury and a trophic
factor combination made in accordance with the invention
(SCI+NTs).
[0023] Before explaining embodiments of the invention in detail, it
is to be understood that the invention is not limited in its
application to the details of construction and the arrangement of
the components set forth in the following description or
illustrated in the drawings. The invention is capable of other
embodiments or being practiced or carried out in various ways.
Also, it is to be understood that the phraseology and terminology
employed herein is for the purpose of description and should not be
regarded as limiting.
DETAILED DESCRIPTION
Definitions
[0024] To facilitate understanding of the invention, a number of
terms are defined below.
[0025] As used herein, the term "antimicrobial polypeptide" refers
to polypeptides that inhibit the growth of microbes (e.g.,
bacteria). Examples of antimicrobial polypeptides include, but are
not limited to, the polypeptides described in Tables 1 and 2 below.
Antimicrobial polypeptides include peptides synthesized from both
L-amino and D-amino acids.
[0026] As used herein, the term "pore forming agent" refers to any
agent (e.g., peptide or other organic compound) that forms pores in
a biological membrane. When the pore forming agent is a peptide,
the peptide can be synthesized from both L-amino and D-amino
acids.
[0027] As used herein, the term "growth factor" refers to any
compound that is involved in cell differentiation and growth.
Growth factors can be proteins (e.g., IGF-1 (insulin-like growth
factor 1), IGF-2 (insulin-like growth factor 2), NGF-.beta. (nerve
growth factor-.beta.), EGF (epidermal growth factor), CSGF
(colony-stimulating growth factor), FGF (fibroblast growth factor),
PDGF (platelet-derived growth factor), VEGF (vascular endothelial
growth factor), TGF-.beta. (transforming growth factor .beta., and
bone morphogenetic proteins)), either purified from natural sources
or genetically engineered, as well as fragments, mimetics, and
derivatives or modifications thereof. Further examples of growth
factors are provided in U.S. Pat. Nos. 5,183,805; 5,218,093;
5,130,298; 5,639,664; 5,457,034; 5,210,185; 5,470,828; 5,650,496;
5,998,376; and 5,410,019; all of which are incorporated herein by
reference.
[0028] The term "trophic factor" as used herein refers to a
substance that stimulates growth and development or stimulates
increased activity.
[0029] The term "hyaluronic acid" includes hyaluronic acid and its
derivatives, for instance, esters, salts such as the sodium,
potassium, magnesium, calcium, alkaline, alkaline earth metals, and
the like, and derivatives such as sulphated or polysulphated
hyaluronates, or hyaluronates that have been otherwise modified in
a manner way such that the function of hyaluronic acid is
retained.
[0030] The term "recombinant protein" or "recombinant polypeptide"
as used herein refers to a protein molecule expressed from a
recombinant DNA molecule. In contrast, the term "native protein" or
"native polypeptide" is used herein to indicate a protein isolated
from a naturally occurring (i.e., a nonrecombinant) source.
Molecular biological techniques may be used to produce a
recombinant form of a protein or polypeptide with similar or
identical properties as compared to the native form of the
protein.
[0031] Where an amino acid sequence is recited herein to refer to
an amino acid sequence of a naturally occurring protein molecule,
amino acid sequence and like terms, such as polypeptide or protein
are not meant to limit the amino acid sequence to the complete,
native amino acid sequence associated with the recited protein
molecule.
[0032] As used herein in reference to an amino acid sequence or a
protein, the term "portion" (as in "a portion of an amino acid
sequence") refers to fragments of that protein. The fragments may
range in size from four amino acid residues to the entire amino
acid sequence minus one amino acid (e.g., 5, 6, 7, 8, . . .
x-1).
[0033] As used herein, the term "variant," when used in reference
to a protein, refers to a protein encoded by partially homologous
nucleic acids so that the amino acid sequence of the protein
varies. As used herein, the term "variant" encompasses proteins
encoded by homologous genes having both conservative and
nonconservative amino acid substitutions that do not result in a
change in protein function, as well as proteins encoded by
homologous genes having amino acid substitutions that cause
decreased protein function or increased protein function.
[0034] As used herein, the term "fusion protein" refers to a
chimeric protein containing the protein of interest (e.g.,
defensins and fragments thereof) joined to a heterologous protein
fragment (e.g., the fusion partner which consists of a non-defensin
protein). The fusion partner may enhance the solubility of a
defensin as expressed in a host cell, may provide an affinity tag
to allow purification of the recombinant fusion protein from the
host cell or culture supernatant, or both. If desired, the fusion
protein may be removed from the protein of interest (e.g., defensin
or fragments thereof) by a variety of enzymatic or chemical
processes known to the art.
[0035] As used herein, the term "purified" refers to molecules,
either nucleic or amino acid sequences, that are removed from their
natural environment, isolated, or separated. The percent of a
purified component is thereby increased in the sample. For example,
an isolated defensin is therefore a purified defensin.
Substantially purified molecules are at least 60% free, preferably
at least 75% free, and more preferably at least 90% free from other
components with which they are naturally associated.
[0036] The term "gene" as used herein, refers to a DNA sequence
that comprises control and coding sequences necessary for the
production of a polypeptide or protein precursor. The polypeptide
can be encoded by a full length coding sequence or by any portion
of the coding sequence, as long as the desired protein activity is
retained.
[0037] The term "homology" refers to a degree of complementarity.
There may be partial homology or complete homology (i.e.,
identity). A "partially complementary sequence" is one that at
least partially inhibits a completely complementary sequence from
hybridizing to a target nucleic acid. This situation is referred to
using the functional term "substantially homologous." The
inhibition of hybridization of the completely complementary
sequence to the target sequence may be examined using a
hybridization assay (e.g., Southern or Northern blot, solution
hybridization, and the like) under conditions of low stringency. A
substantially homologous sequence or probe will compete for and
inhibit the binding (i.e., the hybridization) of a completely
homologous sequence or probe to a target under conditions of low
stringency. This is not to say that conditions of low stringency
are such that non-specific binding is permitted; low stringency
conditions require that the binding of two sequences to one another
be a specific (i.e., selective) interaction. The absence of
non-specific binding may be tested by the use of a second target
that lacks even a partial degree of complementarity (e.g., less
than about 30% identity). In this case, in the absence of
non-specific binding, the probe will not hybridize to the second
non-complementary target.
[0038] When used in reference to a double-stranded nucleic acid
sequence such as a cDNA or a genomic clone, the term "substantially
homologous" refers to any probe which can hybridize to either or
both strands of the double-stranded nucleic acid sequence under
conditions of low stringency as described herein.
[0039] As used herein, the term "hybridization" is used in
reference to the pairing of complementary nucleic acid strands.
Hybridization and the strength of hybridization (i.e., the strength
of the association between nucleic acid strands) is impacted by
many factors well known in the art including the degree of
complementarity between the nucleic acids, stringency of the
conditions involved affected by such conditions as the
concentration of salts, the T.sub.m (melting temperature) of the
formed hybrid, the presence of other components (e.g., the presence
or absence of polyethylene glycol), the molarity of the hybridizing
strands, and the G:C content of the nucleic acid strands.
[0040] As used herein, the term "stringency" is used in reference
to the conditions of temperature, ionic strength, and the presence
of other compounds, under which nucleic acid hybridizations are
conducted. With high stringency conditions, nucleic acid base
pairing will occur only between nucleic acid fragments that have a
high frequency of complementary base sequences. Thus, conditions of
medium or low stringency are often required when it is desired that
nucleic acids that are not completely complementary to one another
be hybridized or annealed together. It is well known in the art
that numerous equivalent conditions can be employed to comprise
medium or low stringency conditions. The choice of hybridization
conditions is generally evident to one skilled in the art and is
normally guided by the purpose of the hybridization, the type of
hybridization (DNA-DNA or DNA-RNA), and the level of desired
relatedness between the sequences (e.g., Sambrook et al., 1989,
Nucleic Acid Hybridization, A Practical Approach, IRL Press,
Washington D.C., 1985, for a general discussion of the state of the
art).
[0041] The stability of nucleic acid duplexes is known to decrease
with an increased number of mismatched bases, and further to be
decreased to a greater or lesser degree depending on the relative
positions of mismatches in the hybrid duplexes. Thus, the
stringency of hybridization can be used to maximize or minimize
stability of such duplexes. Hybridization stringency can be
altered, for example, by adjusting the temperature of
hybridization; adjusting the percentage of helix destabilizing
agents, such as formamide, in the hybridization mix; and adjusting
the temperature and/or salt concentration of the wash solutions.
For filter hybridizations, the final stringency of hybridizations
can be determined by the salt concentration and/or temperature used
for the post-hybridization washes.
[0042] "High stringency conditions" when used in reference to
nucleic acid hybridization comprise conditions equivalent to
binding or hybridization at 42.degree. C. in a solution consisting
of 5.times.SSPE (43.8 g/l NaCl, 6.9 g/l NaH.sub.2PO.sub.4.H.sub.2O
and 1.85 g/l EDTA, pH adjusted to 7.4 with NaOH), 0.5% SDS,
5.times. Denhardt's reagent and 100 .mu.g/ml denatured salmon sperm
DNA followed by washing in a solution comprising 0.1.times.SSPE,
1.0% SDS at 42.degree. C. when a probe of about 500 nucleotides in
length is employed.
[0043] "Medium stringency conditions" when used in reference to
nucleic acid hybridization comprise conditions equivalent to
binding or hybridization at 42.degree. C. in a solution consisting
of 5.times.SSPE (43.8 g/l NaCl, 6.9 g/l NaH.sub.2PO.sub.4.H.sub.2O
and 1.85 g/l EDTA, pH adjusted to 7.4 with NaOH), 0.5% SDS,
5.times. Denhardt's reagent and 100 .mu.g/ml denatured salmon sperm
DNA followed by washing in a solution comprising 1.0.times.SSPE,
1.0% SDS at 42.degree. C. when a probe of about 500 nucleotides in
length is employed.
[0044] "Low stringency conditions" comprise conditions equivalent
to binding or hybridization at 42.degree. C. in a solution
consisting of 5.times.SSPE (43.8 g/l NaCl, 6.9 g/l
NaH.sub.2PO.sub.4.H.sub.2O and 1.85 g/l EDTA, pH adjusted to 7.4
with NaOH), 0.1% SDS, 5.times. Denhardt's reagent [50.times.
Denhardt's contains per 500 ml: 5 g Ficoll (Type 400, Pharamcia), 5
g BSA (Fraction V; Sigma)] and 100 .mu.g/ml denatured salmon sperm
DNA followed by washing in a solution comprising 5.times.SSPE, 0.1%
SDS at 42.degree. C. when a probe of about 500 nucleotides in
length is employed.
[0045] As used herein, the term "T.sub.m" is used in reference to
the melting temperature, which is the temperature at which 50% of a
population of double-stranded nucleic acid molecules becomes
dissociated into single strands. The equation for calculating the
Tm of nucleic acids is well known in the art. The T.sub.m of a
hybrid nucleic acid can be estimated using a formula adopted from
hybridization assays in 1 M salt, and commonly used for calculating
T.sub.m for PCR primers: [(number of A+T).times.2.degree.
C.+(number of G+C).times.4.degree. C.]. (C. R. Newton et al., PCR,
2nd Ed., Springer-Verlag (New York, 1997), p. 24). This formula was
found to be inaccurate for primers longer than 20 nucleotides.
(Id.) Another simple estimate of the T.sub.m value can be
calculated by the equation: T.sub.m=81.5+0.41(% G+C), when a
nucleic acid is in aqueous solution at 1 M NaCl. (e.g., Anderson
and Young, Quantitative Filter Hybridization, in Nucleic Acid
Hybridization (1985). Other more sophisticated computations exist
in the art which take structural as well as sequence
characteristics into account for the calculation of T.sub.m. A
calculated T.sub.m is merely an estimate; the optimum temperature
is commonly determined empirically.
[0046] As used herein, the term "vector" is used in reference to
nucleic acid molecules that transfer DNA segment(s) from one cell
to another and capable of replication in a cell. Vectors may
include plasmids, bacteriophages, viruses, cosmids, and the
like.
[0047] The terms "recombinant vector" and "expression vector" as
used herein refer to DNA or RNA sequences containing a desired
coding sequence and appropriate DNA or RNA sequences necessary for
the expression of the operably linked coding sequence in a
particular host organism. Prokaryotic expression vectors include a
promoter, a ribosome binding site, an origin of replication for
autonomous replication in host cells and can also include other
sequences, e.g., an optional operator sequence. A "promoter" is
defined as a DNA sequence that directs RNA polymerase to bind to
DNA and to initiate RNA synthesis. Eukaryotic expression vectors
include a promoter, polyadenylation signal and optionally an
enhancer sequence.
[0048] As used herein the term "coding region" when used in
reference to structural gene refers to the nucleotide sequences
which encode the amino acids found in the nascent polypeptide as a
result of translation of a mRNA molecule. Typically, the coding
region is bounded on the 5' side by the nucleotide triplet ATG,
which encodes the initiator methionine, and on the 3' side by a
stop codon (e.g., TAA, TAG, TGA). In some cases, the coding region
is also known to initiate by a nucleotide triplet TTG.
[0049] The terms "buffer" or "buffering agents" refer to materials
that when added to a solution, cause the solution to resist changes
in pH.
[0050] The term "monovalent salt" refers to any salt in which the
metal (e.g., Na, K, or Li) has a net 1+ charge in solution (i.e.,
one more proton than electron).
[0051] The term "divalent salt" refers to any salt in which a metal
(e.g., Mg, Ca, or Sr) has a net 2+ charge in solution.
[0052] The term "solution" refers to an aqueous mixture.
[0053] The term "buffering solution" refers to a solution
containing a buffering reagent.
[0054] The present invention relates to neurochemically active
agents and combinations thereof. Neurochemically active agents
include one or more antimicrobial peptide and/or a substance having
an antimicrobial peptide effect. Antimicrobial peptides themselves
are known to have trophic effects. As such, an antimicrobial
peptide and/or a substance having an antimicrobial peptide effect
can be used by itself in the methods of the invention.
Neurochemically active agents also include one or more growth
factor, neurotrophin, and neuropeptide. Combinations of
neurochemically active agents are referred to herein as "trophic
factor combinations."
[0055] According to the invention, neurochemically active agents
can be used alone or in combination to treat injuries to the
nervous system, i.e., the central nervous system and the peripheral
nervous system. The one or more neurochemically active agents can
be used to treat nervous system injuries, including trauma induced
injuries, degenerative induced injuries, age induced injuries, and
infection induced injuries. Injuries that can be treated include,
but are not limited to, spinal cord injury, including severed
spinal cords; peripheral nerve damage, brain injuries, e.g., blood
clots, tumors, strokes, and ischemis and perfusion; and Parkinson's
disease, Alzheimer disease, muscular dystrophy, amyotrophic lateral
sclerosis, multiple sclerosis, Pick's disease, prion diseases,
Huntington disease, and related disorders.
[0056] When applied to a the nervous system, trophic factor
combinations of the invention result in at least one of the
following: lower loss in body weight after the injury when compared
to controls not receiving the trophic factor combinations,
strengthened motor recovery in injured animals treated with the
trophic factor combination when compared to animals not treated
with the trophic factor combination, larger evoked potentials in
nerves when compared to controls not receiving the trophic factor
combination, and a lower current required to evoke a response
(threshold current) when compared to controls not receiving the
trophic factor combination.
[0057] It is contemplated that the trophic factor combinations of
the present invention used to treat injuries of the nervous system
result in reduced inflammation, growth of new cells, increased
plasticity, among other beneficial effects.
I. Trophic Factor Combinations
[0058] The present invention contemplates the use of trophic factor
combinations and their individual components for treatment of
injuries to the nervous system. Trophic factor combinations
according to the invention can include one or more of the following
elements: antimicrobial polypeptides (e.g., defensins), a substance
having an effect of an antimicrobial peptide, a growth factor, a
neurotrophin, and a neuropeptide. Additional components can also be
included and are discussed below.
[0059] A. Antimicrobial Peptides
[0060] In some embodiments, one or more antimicrobial polypeptides
and/or one or more substances having an antimicrobial peptide
effect are used as a trophic factor to treat an injury to a nervous
system. For additional information on antimicrobial peptides, see,
for example, Antimicrobial Peptide Protocols, ed. W. M. Shafer,
Humana Press, Totowa, N.J., 1997; and databases including
http://aps.unmc.edu/AP/main.php (discussed in Wang Z, Wang G., APD:
the Antimicrobial Peptide Database, Nucleic Acids Res. 2004 Jan. 1;
32(Database issue):D590-2),
http://sdmc.lit.org.sg/Templar/DB/Antimic/, and
http://www.bbcm.units.it/.about.zelezetsky/hdpdb.html (database of
defense peptides) and Table 1 below.
[0061] In some embodiments, the antimicrobial peptide is a compound
or peptide selected from the following: bovine defensin peptide
(BNP-1, Romeo et al., J. Biol. Chem. 263(15):9573-9575 [1988]),
magainin (e.g., magainin I, magainin II, xenopsin, xenopsin
precursor fragment, caerulein precursor fragment), magainin I and
II analogs (PGLa, magainin A, magainin G, pexiganin, Z-12,
pexigainin acetate, D35, MSI-78A, MG0 [K10E, K11E, F12W-magainin
2], MG2+ [K10E, F12W-magainin-2], MG4+ [F12W-magainin 2], MG6+
[f12W, E19Q-magainin 2 amide], MSI-238, reversed magainin II
analogs [e.g., 53D, 87-ISM, and A87-ISM], Ala-magainin II amide,
magainin II amide), cecropin P1, cecropin A, cecropin B,
indolicidin, nisin, ranalexin, lactoferricin B, poly-L-lysine,
cecropin A (1-8)-magainin II (1-12), cecropin A (1-8)-melittin
(1-12), CA(1-13)-MA(1-13), CA(1-13)-ME(1-13), gramicidin,
gramicidin A, gramicidin D, gramicidin S, alamethicin, protegrin,
histatin, dermaseptin, lentivirus amphipathic peptide or analog,
parasin I, lycotoxin I or II, globomycin, gramicidin S, surfactin,
ralinomycin, valinomycin, polymyxin B, PM2 [(+/-)
1-(4-aminobutyl)-6-benzylindane], PM2c
[(+/-)-6-benzyl-1-(3-carboxypropyl)indane], PM3 [(+/-)
1-benzyl-6-(4-aminobutyl)indane], tachyplesin, buforin I or II,
misgurin, melittin, PR-39, PR-26, 9-phenylnonylamine, (KLAKKLA)n,
(KLAKLAK)n, where n=1, 2, or 3, (KALKALK)3, KLGKKLG)n, and
KAAKKAA)n, wherein N=1, 2, or 3, paradaxin, Bac 5, Bac 7,
ceratoxin, mdelin 1 and 5, bombin-like peptides, PGQ, cathelicidin,
HD-5, Oabac5alpha, ChBac5, SMAP-29, Bac7.5, lactoferrin,
granulysin, thionin, hevein and knottin-like peptides, MPG1, 1bAMP,
snakin, lipid transfer proteins, and plant defensins. Exemplary
sequences for the above listed compounds are provided in Table 1.
In some embodiments, the antimicrobial peptides or substances
having an antimicrobial peptide effect (where they are peptides)
are synthesized from L-amino acids, while in other embodiments, the
peptides are synthesized from or comprise D-amino acids.
[0062] The compounds listed above can be isolated and purified from
natural sources as appropriate. The compounds can also be produced
recombinantly or synthetically, as described below.
[0063] In preferred embodiments, the trophic factor combinations of
the present invention comprise one or more antimicrobial
polypeptides and/or one or more substance having an antimicrobial
peptide effect at a concentration of about 0.01 to about 1000 mg/L.
In preferred embodiments, the trophic factor combinations comprise
a solution comprising one or more antimicrobial polypeptides at a
concentration of about 0.1 to about 5 mg/L.
[0064] In some embodiments of the present invention, the
antimicrobial polypeptide is a defensin. In preferred embodiments,
the trophic factor combinations of the present invention comprise
one or more defensins. In further preferred embodiments, the
trophic factor combination comprises a solution comprising purified
defensins at a concentration of about 0.01 to 1000 mg/L. In
particularly preferred embodiments, the trophic factor combinations
comprise a solution comprising defensins at a concentration of
about 0.1 to 5 mg/L. In still further preferred embodiments, the
antimicrobial polypeptide is BNP1 (also known as bactanecin and
bovine dodecapeptide). In certain embodiments, the defensin
comprises the following consensus sequence:
X.sub.1CN.sub.1CRN.sub.2CN.sub.3ERN.sub.4CN.sub.5GN.sub.6CCX.sub.2,
wherein N and X represent conservatively or nonconservatively
substituted amino acids and N.sub.1=1, N.sub.2=3 or 4, N.sub.3=3 or
4, N.sub.4=1, 2, or 3, N.sub.6=5-9, X.sub.1 and X.sub.2 may be
present, absent, or equal from 1-2.
[0065] The present invention is not limited to any particular
defensin. Indeed, trophic factor combinations comprising a variety
of defensins are contemplated. Representative defensins are
provided in Tables 1 and 2 below. In general, defensins are a
family of highly cross-linked, structurally homologous
antimicrobial peptides that can be found in the azurophil granules
of polymorphonuclear leukocytes (PMNs) with homologous peptides
being present in macrophages (e.g., Selsted et al., Infect. Immun.
45:150-154 [1984]). Originally described as "Lysosomal Cationic
Peptides" in rabbit and guinea pig PMN (Zeya et al., Science
154:1049-1051 [1966]; Zeya et al., J. Exp. Med. 127:927-941 [1968];
Zeya et al., Lab. Invest. 24:229-236 [1971]; Selsted et al.,
[1984], supra.), this mixture was found to account for most of the
microbicidal activity of the crude rabbit PMN extract against
various microorganisms (Zeya et al., [1966], supra; Lehrer et al.,
J. Infect. Dis. 136:96-99 [1977]; Lehrer et al., Infect. Immun.
11:1226-1234 [1975]). Six rabbit neutrophil defensins have been
individually purified and are designated NP-1, NP-2, NP-3A, NP-3B,
NP-4, and NP-5. Their amino acid sequences were determined, and
their broad spectra of activity were demonstrated against a number
of bacteria (Selsted et al., Infect. Immun. 45:150-154 [1984]),
viruses (Lehrer et al., J. Virol. 54:467 [1985]), and fungi
(Selsted et al., Infect. Immun. 49:202-206 [1985]; Segal et al.,
151:890-894 [1985]). Defensins have also been shown to possess
mitogenic activity (e.g., Murphy et al., J. Cell. Physiol.
155:408-13 [1993]).
[0066] Four peptides of the defensin family have been isolated from
human PMN's and are designated HNP-1, HNP-2, HNP-3, and HNP-4 (Ganz
et al., J. Clin. Invest. 76:1427-1435 [1985]; Wilde et al., J.
Biol. Chem. 264:11200-11203 [1989]). The amino acid sequences of
HNP-1, HNP-2, and HNP-3 differ from each other only in their amino
terminal residues, while each of the human defensins are identical
to the six rabbit peptides in 10 or 11 of their 29 to 30 residues.
These are the same 10 or 11 residues that are shared by all six
rabbit peptides. Human defensin peptides have been shown to share
with the rabbit defensins a broad spectrum of antimicrobial
activity against bacteria, fungi, and enveloped viruses (Ganz et
al., [1985], supra).
[0067] Three defensins designated RatNP-1, RatNP-2, and RatNP-4,
have been isolated from rat (Eisenhauer et al., Infection and
Immunity 57:2021-2027 [1989]). A guinea pig defensin (GPNP) has
also been isolated, purified, sequenced and its broad spectrum
antimicrobial properties verified (Selsted et al., Infect. Immun.
55:2281-2286 [1987]). Eight of its 31 residues were among those
invariant in six rabbit and three human defensin peptides. The
sequence of GPNP also included three nonconservative substitutions
in positions otherwise invariant in the human and rabbit peptides.
Of the defensins tested in a quantitative assay HNP-1, RatNP-1, and
rabbit NP-1 possess the most potent antimicrobial properties, while
NP-5 possesses the least amount of antimicrobial activity when
tested against a panel of organisms in stationary growth phase
(Selsted et al., Infect. Immun. 45:150-154 [1984]; Ganz et al., J.
Clin. Invest. 76:1427-1435 [1985]). Defensin peptides are further
described in U.S. Pat. Nos. 4,543,252; 4,659,692; and 4,705,777
(each of which is incorporated herein by reference).
[0068] Defensin peptides suitable for use alone in the methods
and/or in trophic factor combinations of the present invention
include natural defensin peptides isolated from known cellular
sources, synthetic peptides produced by solid phase or recombinant
DNA techniques, and defensin analogs which may be smaller peptides
or other molecules having similar binding and biological activity
as the natural defensin peptides (e.g., peptide mimetics). Methods
for the purification of defensin peptides are described in U.S.
Pat. Nos. 4,543,252; 4,659,692; and 4,705,777, the disclosures of
which are incorporated herein by reference.
[0069] In preferred embodiments, suitable synthetic peptides will
comprise all or part of the amino acid sequence of a known peptide,
more preferably incorporating at least some of the conserved
regions identified in Table 2. In particularly preferred
embodiments, the synthetic peptides incorporate at least one of the
conserved regions, more typically incorporating two of the
conserved regions, preferably conserving at least three of the
conserved regions, and more preferably conserving four or more of
the conserved regions. In preferred embodiments, the synthetic
peptides comprise fifty amino acids or fewer, although there may be
advantages in increasing the size of the peptide above that of the
natural peptides in certain instances. In certain embodiments, the
peptides have a length in the range from about 10 to 50 amino
acids, preferably being in the range from about 10 to 40 amino
acids, and most preferably being in the range from about 30 to 35
amino acids which corresponds generally to the length of the
natural defensin peptides.
[0070] In some cases, it may be desirable to incorporate one or
more non-natural amino acids in the synthetic defensin peptides of
the present invention. In preferred embodiments, non-natural amino
acids comprise at least an N-terminus and a C-terminus of the
peptide and have side chains that are either identical to or
chemically modified or substituted from a natural amino acid
counterpart. An example of a non-natural amino acid is an optical
isomer of a naturally-occurring L-amino acid, such as a peptide
containing all D-amino acids. Examples of the synthesis of peptides
containing all D-amino acids include Merrifield et al., Ciba Found
Symp. 186:5-26 (1994); Wade et al., Proc. Natl. Acad. Sci. USA
87(12):4761-5 (1990); and U.S. Pat. No. 5,792,831, which is herein
incorporated by reference. Examples of chemical modifications or
substitutions include hydroxylation or fluorination of C--H bonds
within natural amino acids. Such techniques are used in the
manufacture of drug analogs of biological compounds and are known
to one of ordinary skill in the art.
[0071] Synthetic peptides having biological and binding activity
the same or similar to that of natural defensin peptides can be
produced by either of two exemplary approaches. First, the
polypeptides can be produced by the well-known Merrifield
solid-phase chemical synthesis method wherein amino acids are
sequentially added to a growing chain (Merrifield, J. Am. Chem.
Soc. 85:2149-2156 [1963]). Automatic peptide synthesis equipment is
available from several commercial suppliers, including PE
Biosystems, Inc., Foster City, Calif.; Beckman Instruments, Inc.,
Waldwick, N.J.; and Biosearch, Inc., San Raphael, Calif. Using such
automatic synthesizers according to manufacturer's instructions,
peptides can be produced in gram quantities for use in the present
invention.
[0072] Second, the synthetic defensin peptides of the present
invention can be synthesized by recombinant techniques involving
the expression in cultured cells of recombinant DNA molecules
encoding a gene for a desired portion of a natural or analog
defensin molecule. The gene encoding the defensin peptide can
itself be natural or synthetic. Conveniently, polynucleotides can
be synthesized by well-known techniques based on the desired amino
acid sequence. For example, short single-stranded DNA fragments can
be prepared by the phosphoramidite method (Beaucage et al., Tetra.
Lett. 22:1859-1862 [1981]). A double-stranded fragment can then be
obtained either by synthesizing the complementary strand and
annealing the strands together under appropriate conditions, or by
adding the complementary strand using DNA polymerase under
appropriate conditions, or by adding the complementary strand using
DNA polymerase with an appropriate primer sequence. The natural or
synthetic DNA fragments coding for the desired defensin peptide can
then be incorporated in a suitable DNA construct capable of
introduction to and expression in an in vitro cell culture. The DNA
fragments can be portions or variants of wild-type nucleic acids
encoding defensins. Suitable variants include those both with
conservative and nonconservative amino acid substitutions.
[0073] The methods, compositions, and trophic factor combinations
of the present invention can also employ synthetic non-peptide
compositions that have biological activity functionally comparable
to that of known defensin peptides. By functionally comparable, it
is meant that the shape, size, flexibility, and electronic
configuration of the non-peptide molecule is such that the
biological activity of the molecule is similar to defensin
peptides. In particular, the non-peptide molecules should display
comparable mitogenic activity and/or antimicrobial activity or pore
forming ability, preferably possessing both activities. Such
non-peptide molecules will typically be small molecules having a
molecular weight in the range from about 100 to about 1000 daltons.
The use of such small molecules is frequently advantageous in the
preparation of trophic factor combinations. Candidate mimetics can
be screened in large numbers to identify those having the desired
activity.
[0074] The identification of such nonpeptide analog molecules can
be performed using techniques known in the art of drug design. Such
techniques include, but are not limited to, self-consistent field
(SCF) analysis, configuration interaction (CI) analysis, and normal
mode dynamics computer analysis, all of which are well described in
the scientific literature (e.g., Rein et al., Computer-Assisted
Modeling of Receptor-Ligand Interactions, Alan Liss, N.Y., [1989]).
Preparation of the identified compounds will depend on the desired
characteristics of the compounds and will involve standard chemical
synthetic techniques (e.g., Cary et al., Advanced Organic
Chemistry, part B, Plenum Press, New York [1983]).
[0075] In some embodiments of the present invention, one or more
substances having an effect that an antimicrobial peptide has can
be used. Effects that antimicrobial peptides have include, but are
not limited to, the following: form pores on the cell membrane;
enter cells without membrane lysis and, once in the cytoplasm, bind
to, and inhibit the activity of specific molecular targets
essential to bacterial growth, thereby causing cell death; induce
expression of syndecan, an integral membrane proteoglycan
associated largely with epithelial cells, in mesenchymal cells and
inhibit the NADPH oxidase activity of neutrophils, suggesting a
role of this peptide in wound repair and inflammation; exert a
protective effect in various animal models of ischemia-reperfusion
injury, preventing the post-ischemic oxidant production; induce
angiogenesis both in vitro and in vivo; inhibit membrane protein
synthesis; inhibit DNA synthesis; antitumor effect; stimulate cell
proliferation; interfere with signal pathways; chemoattractant for
immune cells; stimulate cytokine expression; stimulate adhesion
molecule expression; angiogenesis; and chloride secretion.
TABLE-US-00001 TABLE 1 Human Antimicrobial Peptides Organism
Protein Name Name Length Sequence Antibacterial 170
MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQV peptide LL-37
LSYKEAVLRAIDGINQRSSDANLYRLLDLDPR precursor
PTMDGDPDTPKPVSFTVKETVCPRTTQQSP EDCDFKKDGLVKRCMGTVNLNQARGSFDIS
CDKDNKRFALLGDFFRKSKEKIGKEFKRIVQR IKDFLRNLVPRTES Antibacterial Homo
170 MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQV protein FALL- sapiens
LSYKEAVLRAIDGINQRSSDANLYRLLDLDPR 39 precursor
PTMDGDPDTPKPVSFTVKETVCPRTTQQSP EDCDFKKDGLVKRCMGTVTLNQARGSFDISC
DKDNKRFALLGDFFRKSKEKIGKEFKRIVQRI KDFLRNLVPRTES Antimicrobial Homo
476 MQPVMLALWSLLLLWGLATPCQELLETVGTL peptide RYA3 sapiens
ARIDKDELGKAIQNSLVGEPILQNVLGSVTAV NRGLLGSGGLLGGGGLLGHGGVFGVVEELS
GLKIEELTLPKVLLKLLPGFGVQLSLHTKVGM HCSGPLGGLLQLAAEVNVTSRVALAVSSRGT
PILILKRCSTLLGHISLFSGLLPTPLFGVVEQM LFKVLPGLLCPVVDSVLGVVNELLGAVLGLVS
LGALGSVEFSLATLPLISNQYIELDINPIVKSVA GDIIDFPKSRAPAKVPPKKDHTSQVMVPLYLF
NTTFGLLQTNGALDMDITPELVPSDVPLTTTD LAALLPEALGKLPLHQQLLLFLRVREAPTVTL
HNKKALVSLPANIHVLFYVPKGTPESLFELNS VMTVRAQLAPSATKLHISLSLERLSVKVASSF
THAFDGSRLEEWLSHVVGAVYAPKLNVALDV GIPLPKVLNINFSNSVLEIVENAVVLTVAS
Azurocidin Homo 251 MTRLTVLALLAGLLASSRAGSSPLLDIVGGRK precursor
sapiens ARPRQFPFLASIQNQGRHFCGGALIHARFVM
TAASCFQSQNPGVSTVVLGAYDLRRRERQS RQTFSISSMSENGYDPQQNLNDLMLLQLDRE
ANLTSSVTILPLPLQNATVEAGTRCQVAGWG SQRSGGRLSRFPRFVNVTVTPEDQCRPNNV
CTGVLTRRGGICNGDGGTPLVCEGLAHGVA SFSLGPCGRGPDFFTRVALFRDWIDGVLNNP
GPGPA Bactericidal Homo 483 MARGPCNAPRWVSLMVLVAIGTAVTAAVNP
permeability- sapiens GVVVRISQKGLDYASQQGTAALQKELKRIKIP increasing
DYSDSFKIKHLGKGHYSFYSMDIREFQLPSS protein
QISMVPNVGLKFSISNANIKISGKWKAQKRFL precursor (BPI)
KMSGNFDLSIEGMSISADLKLGSNPTSGKPTI (CAP 57)
TCSSCSSHINSVHVHISKSKVGWLIQLFHKKIE SALRNKMNSQVCEKVTNSVSSKLQPYFQTLP
VMTKIDSVAGINYGLVAPPATTAETLDVQMK GEFYSENHHNPPPFAPPVMEFPAAHDRMVY
LGLSDYFFNTAGLVYQEAGVLKMTLRDDMIP KESKFRLTTKFFGTFLPEVAKKFPNMKIQIHV
SASTPPHLSVQPTGLTFYPAVDVQAFAVLPN SSLASLFLIGMHTTGSMEVSAESNRLVGELKL
DRLLLELKHSNIGPFPVELLQDIMNYIVPILVLP RVNEKLQKGFPLPTPARVQLYNVVLQPHQNF
LLFGADVVYK bactericidal/per- Homo 487
MRENMARGPCNAPRWVSLMVLVAIGTAVTA meability- sapiens
AVNPGVVVRISQKGLDYASQQGTAALQKELK increasing
RIKIPDYSDSFKIKHLGKGHYSFYSMDIREFQL protein
PSSQISMVPNVGLKFSISNANIKISGKWKAQK precursor
RFLKMSGNFDLSIEGMSISADLKLGSNPTSGK PTITCSSCSSHINSVHVHISKSKVGWLIQLFHK
KIESALRNKMNSQVCEKVTNSVSSKLQPYFQ TLPVMTKIDSVAGINYGLVAPPATTAETLDVQ
MKGEFYSENHHNPPPFAPPVMEFPAAHDRM VYLGLSDYFFNTAGLVYQEAGVLKMTLRDDM
IPKESKFRLTTKFFGTFLPEVAKKFPNMKIQIH VSASTPPHLSVQPTGLTFYPAVDVQAFAVLP
NSSLASLFLIGMHTTGSMEVSAESNRLVGEL KLDRLLLELKHSNIGPFPVELLQDIMNYIVPILV
LPRVNEKLQKGFPLPTPARVQLYNVVLQPHQ NFLLFGADVVYK beta defensin Homo 111
MKSLLFTLAVFMLLAQLVSGNWYVKKCLNDV 126 sapiens
GICKKKCKPEEMHVKNGWAMCGKQRDCCV preproprotein;
PADRRANYPVFCVQTKTTRISTVTATTATTTL epididymal MMTTASMSSMAPTPVSPTG
secretory protein ESP13.2; beta defensin 26; chromosome 20 open
reading frame 8 beta-defensin Homo 65
MRTFLFLFAVLFFLTPAKNAFFDEKCNKLKGT sapiens
CKNNCGKNEELIALCQKFLKCCRTIQPCGSII D Beta-defensin Homo 67
MRIHYLLFALLFLFLVPVPGHGGIINTLQKYYC 103 precursor sapiens
RVRGGRCAVLSCLPKEEQIGKCSTRGRKCC (Beta-defensin RRKK 3) (DEFB-3)
(BD-3) (hBD-3) (HBD3) (Defensin like protein) Beta-defensin Homo 72
MQRLVLLLAVSLLLYQDLPVRSEFELDRICGY 104 precursor sapiens
GTARCRKKCRSQEYRIGRCPNTYACCLRKW (Beta-defensin DESLLNRTKP 4)
(DEFB-4) (BD-4) (hBD-4) beta-defensin Homo 77
MALIRKTFYFLFAMFFILVQLPSGCQAGLDFS 105 sapiens
QPFPSGEFAVCESCKLGRGKCRKECLENEK PDGNCRLNFLCCRQR Beta-defensin Homo
78 MALIRKTFYFLFAMFFILVQLPSGCQAGLDFS 105 precursor sapiens
QPFPSGEFAVCESCKLGRGKCRKECLENEK (Beta-defensin PDGNCRLNFLCCRQRI 5)
(DEFB-5) (BD-5) beta-defensin Homo 57
MRTFLFLFAVLFFLTPAKNAFFDEKCNKLKGT 106 sapiens
CKNNCGKNEELIALCQKSLKCCRTI Beta-defensin Homo 65
MRTFLFLFAVLFFLTPAKNAFFDEKCNKLKGT 106 precursor sapiens
CKNNCGKNEELIALCQKSLKCCRTIQPCGSII (Beta-defensin D 6) (DEFB-6)
(BD-6) Beta-defensin Homo 63 MKIFVFILAALILLAQIFQARTAIHRALISKRME 107
precursor sapiens GHCEAECLTFEVKIGGCRAELAPFCCKNR (Beta-defensin 7)
(DEFB-7) (Fragment) beta-defensin Homo 59
MRIAVLFFTIFFFMSQVLPAKGKFKEICERPN 108 sapiens
GSCRDFCLETEIHVGRCLNSRPCCLPL Beta-defensin Homo 73
MRIAVLLFAIFFFMSQVLPARGKFKEICERPN 108 precursor sapiens
GSCRDFCLETEIHVGRCLNSQPCCLPLGHQP (Beta-defensin RIESTTPKKD 8)
(DEFB-8) Beta-defensin Homo 123 MKLLLLALPMLVLLPQVIPAYSGEKKCWNRS 118
precursor sapiens GHCRKQCKDGEAVKDTCKNLRACCIPSNED (Beta-defensin
HRRVPATSPTPLSDSTPGIIDDILTVRFTTDYF 18) (DEFB-18)
EVSSKKDMVEESEAGRGTETSLPNVHHSS (Epididymal secretory protein 13.6)
(ESP13.6) Beta-defensin Homo 84 MKLLYLFLAILLAIEEPXISGKRHILRCMGNSGI
119 precursor sapiens CRASCKKNEQPYLYCRNCQSCCLQSYMRISI
(Beta-defensin SGKEENTDWSYEKQWPRLP 19) (DEFB-19) Beta-defensin Homo
88 MKLLYLFLAILLAIEEPVISVECWMDGHCRLLC 120 precursor sapiens
KDGEDSIIRCRNRKRCCVPSRYLTIQPVTIHGI (Beta-defensin
LGWTTPQMSTTAPKMKTNITNR 20) (DEFB-20) Beta-defensin Homo 67
MKLLLLTLTVLLLLSQLTPGGTQRCWNLYGK 123 precursor sapiens
CRYRCSKKERVYVYCINNKMCCVKPKYQPK (Beta-defensin ERWWPF 23) (DEFB-23)
Beta-defensin Homo 43 EFKRCWKGQGACQTYCTRQETYMHLCPDA 124 (Beta-
sapiens SLCCLSYALKPPPV defensin 24) (DEFB-24) (Fragment)
Beta-defensin Homo 152 MLTFIICGLLTRVTKGSFEPQKCWKNNVGHC 125
precursor sapiens RRRCLDTERYILLCRNKLSCCISIISHEYTRRP (Beta-defensin
AFPVIHLEDITLDYSDVDSFTGSPVSMLNDLIT 25) (DEFB-25)
FDTTKFGETMTPETNTPETTMPPSEATTPET TMPPSETATSETMPPPSQTALTHN
Beta-defensin Homo 111 MKFLLFTLAVFMLLAQLVSGNWYVKKCLNDV 126
precursor sapiens GICKKKCKPEEMHVKNGWAMCGKQRDCCV (Beta-defensin
PADRRANYPVFCVQTKTTRISTVTATTATTTL 26) (DEFB-26) MMTTASMSSMAPTPVSPTG
(Epididymal secretory protein 13.2) (ESP13.2) Beta-defensin Homo 99
MGLFMIIAILLFQKPTVTEQLKKCWNNYVQGH 127 precursor sapiens
CRKICRVNEVPEALCENGRYCCLNIKELEACK (Beta-defensin
KITKPPRPKPATLALTLQDYVTIIENFPSLKTQ 27) (DEFB-27) ST Beta-defensin
Homo 183 MKLLFPIFASLMLQYQVNTEFIGLRRCLMGLG 129 precursor sapiens
RCRDHCNVDEKEIQKCKMKKCCVGPKVVKLI (Beta-defensin
KNYLQYGTPNVLNEDVQEMLKPAKNSSAVIQ 29) (DEFB-29)
RKHILSVLPQIKSTSFFANTNFVIIPNATPMNS ATISTMTPGQITYTATSTKSNTKESRDSATAS
PPPAPPPPNILPTPSLELEEAEEQ Beta-defensin Homo 70
MRVLFFVFGVLSLMFTVPPGRSFISNDECPS 131 precursor sapiens
EYYHCRLKCNADEHAIRYCADFSICCKLKIIEI (Beta-defensin DGQKKW 31)
(DEFB-31) Beta-Defensin Homo 37 PVTCLKSGAICHPVFCPRRYKQIGTCGLPGT 2
sapiens KCCKKP Beta-defensin Homo 64
MRVLYLLFSFLFIFLMPLPGVFGGIGDPVTCL 2 precursor sapiens
KSGAICHPVFCPRRYKQIGTCGLPGTKCCKK (BD-2) (hBD-2) P (Skin-
antimicrobial peptide 1) (SAP1) beta-defensin Homo 156
MNILMLTFIICGLLTRVTKGSFEPQKCWKNNV 25 precursor sapiens
GHCRRRCLDTERYILLCRNKLSCCISIISHEYT RRPAFPVIHLEDITLDYSDVDSFTGSPVSMLN
DLITFDTTKFGETMTPETNTPETTMPPSEATT PETTMPPSETATSETMPPPSQTALTHN
beta-defensin Homo 93 MKLFLVLIILLFEVLTDGARLKKCFNKVTGYCR 28
precursor sapiens KKCKVGERYEIGCLSGKLCCANDEEEKKHVS
FKKPHQHSGEKLSVLQDYIILPTITIFTV Beta-Defensin Homo 45
GIINTLQKYYCRVRGGRCAVLSCLPKEEQIGK 3 sapiens CSTRGRKCCRRKK
beta-defensin Homo 95 MKFLLLVLAALGFLTQVIPASAGGSKCVSNTP 32 precursor
sapiens GYCRTCCHWGETALFMCNASRKCCISYSFL
PKPDLPQLIGNHWQSRRRNTQRKDKKQQTT VTS Beta-defensin- Homo 47
GNFLTGLGHRSDHYNCISSGGQCLYSACPIF 1 (Fragment) sapiens
TKIQGTCYRGKAKCCK Beta-Defensin- Homo 41
GIGDPVTCLKSGAICHPVFCPRRYKQIGTCGL 2 sapiens PGTKCCKKP Beta-defensin-
Homo 67 MRIHYLLFALLFLFLVPVPGHGGIINTLQKYYC 3 sapiens
RVRGGRCAVLSRLPKEEQIGKCSTRGRKCC RRKK Calgranulin A Homo 93
MLTELEKALNSIIDVYHKYSLIKGNFHAVYRDD (Migration sapiens
LKKLLETECPQYIRKKGADVWFKELDINTDGA inhibitory
VNFQEFLILVIKMGVAAHKKSHEESHKE factor-related protein 8) (MRP-8)
(Cystic fibrosis antigen) (CFAG) (P8) (Leukocyte L1 complex light
chain) (S100 calcium-binding protein A8) (Calprotectin L1L subun
Calgranulin B Homo 114 MTCKMSQLERNIETIINTFHQYSVKLGHPDTL (Migration
sapiens NQGEFKELVRKDLQNFLKKENKNEKVIEHIME inhibitory
DLDTNADKQLSFEEFIMLMARLTWASHEKMH factor-related EGDEGPGHHHKPGLGEGTP
protein 14) (MRP-14) (P14) (Leukocyte L1 complex heavy chain) (S100
calcium- binding protein A9) (Calprotectin L1H subunit) Calgranulin
C Homo 92 MTKLEEHLEGIVNIFHQYSVRKGHFDTLSKGE (CAGC) sapiens
LKQLLTKELANTIKNIKDKAVIDEIFQGLDANQ (CGRP)
DEQVDFQEFISLVAIALKAAHYHTHKE (Neutrophil S100 protein) (Calcium-
binding protein in amniotic fluid 1) (CAAF1) (p6) [Contains:
Calcitermin] cathelicidin Homo 170 MKTQRNGHSLGRWSLVLLLLGLVMPLAIIAQV
antimicrobial sapiens LSYKEAVLRAIDGINQRSSDANLYRLLDLDPR peptide
PTMDGDPDTPKPVSFTVKETVCPRTTQQSP EDCDFKKDGLVKRCMGTVTLNQARGSFDISC
DKDNKRFALLGDFFRKSKEKIGKEFKRIVQRI KDFLRNLVPRTES Cathepsin G Homo 255
MQPLLLLLAFLLPTGAEAGEIIGGRESRPHSR precursor (EC sapiens
PYMAYLQIQSPAGQSRCGGFLVREDFVLTAA 3.4.21.20) (CG)
HCWGSNINVTLGAHNIQRRENTQQHITARRAI RHPQYNQRTIQNDIMLLQLSRRVRRNRNVNP
VALPRAQEGLRPGTLCTVAGWGRVSMRRGT DTLREVQLRVQRDRQCLRIFGSYDPRRQICV
GDRRERKAAFKGDSGGPLLCNNVAHGIVSY GKSSGVPPEVFTRVSSFLPWIRTTMRSFKLL
DQMETPL chromogranin Homo 457 MRSAAVLALLLCAGQVTALPVNSPMNKGDTE A;
parathyroid sapiens VMKCIVEVISDTLSKPSPMPVSQECFETLRGD secretory
ERILSILRHQNLLKELQDLALQGAKERAHQQK protein 1
KHSGFEDELSEVLENQSSQAELKEAVEEPSS KDVMEKREDSKEAEKSGEATDGARPQALPE
PMQESKAEGNNQAPGEEEEEEEEATNTHPP ASLPSQKYPGPQAEGDSEGLSQGLVDREKG
LSAEPGWQAKREEEEEEEEEAEAGEEAVPE EEGPTVVLNPHPSLGYKEIRKGESRSEALAV
DGAGKPGAEEAQDPEGKGEQEHSQQKEEE EEMAVVPQGLFRGGKSGELEQEEERLSKEW
EDSKRWSKMDQLAKELTAEKRLEGQEEEED NRDSSMKLSFRARAYGFRGPGPQLRRGWR
PSSREDSLEAGLPLQVRGYPEEKKEEEGSAN RRPEDQELESLSAIEAELEKVAHQLQALRRG
Defensin 5 Homo 94 MRTIAILAAILLVALQAQAESLQERADEATTQK precursor
sapiens QSGEDNQDLAISFAGNGLSALRTSGSQARAT (Defensin,
CYCRTGRCATRESLSGVCEISGRLYRLCCR alpha 5) Defensin 6 Homo 101
MRTLTILTAVLLVALQAKAEPLQAEDDPLQAK sapiens
AYEADAQEQRGANDQDFAVSFAEDASSSLR ALGGSTRAFTCHCRRSCYSTEYSYGTCTVM
GINHRFCCL Defensin 6 Homo 100 MRTLTILTAVLLVALQAKAEPLQAEDDPLQAK
precursor sapiens AYEADAQEQRGANDQDFAVSFAEDASSSLR (Defensin,
ALGSTRAFTCHCRRSCYSTEYSYGTCTVMGI alpha 6) NHRFCCL defensin alpha-
Homo 65 CCSPGADCSGHPRSGCFPCMGRKLGSKAS 3 precursor sapiens
RLKEKHGLLLQNTSVHCRRTSLWNLHLPGKT (mistranslated) LGILL defensin beta
Homo 60 MKIFFFILAALILLAQIFQARTAIHRALISKRME 107 sapiens
GHCEAECLTFEVKIGGCRAELAPFCC defensin beta Homo 52
GKFKEICERPNGSCRDFCLETEIHVGRCLNS 108 sapiens QPCCLPLGHQPRIESTTPKKD
Defensin beta Homo 21 SCTAIGGRCKNQCDDSEFRIS 112 (Fragment) sapiens
Defensin beta Homo 39 KRYGRCKRDCLESEKQIDICSLPGKICCTEKL 114
(Fragment) sapiens YEEDDMF defensin beta Homo 101
GEKKCWNRSGXCRKQCKDGEAVKDTCKNX 118 sapiens
RACCIPSNEDHRRVPATSPTPLSDSTPGIIDDI LTVRFTTDYFEVSSKKDMVEESEAGRGTETS
LPNVHHSS defensin beta Homo 94 SLLFTLAVFMLLAQLVSGNWYVKKCLNDVGI 126
sapiens CKKKCKPEEMHVKNGWAMCGKQRDCCVPA
DRRANYPVFCVQTKTTRISTVTATTATTTLMM TT defensin beta Homo 59
EQLKKCWNNYVQRHCRKICRVNEVPEALCE 127 sapiens
NGRYCCLNIKELEACKKITKPPSPKQHLH defensin beta Homo 155
MKLLFPIFASLMLQYQVNTEFIGLRRCLMGLG 129 sapiens
RCRDHCNVDEKEIQKCKMKKCCVGPKVVKLI KNYLQYGTPNVLNEDVQEMLKPAKNSSAVIQ
RKHILSVLPQIKSTSFFANTNFVIIPNATPMNS ATISTMTPGQITYTATSTKSNTKESRDS
defensin beta-1 Homo 36 DHYNCVSSGGQCLYSACPIFTKIQGTCYRGK sapiens
AKCCK Defensin HNP- Homo 30 DCYCRIPACIAGERRYGTCIYQGRLWAFCC 3 -
Chain B sapiens EP2E Homo 80 MKVFFLFAVLFCLVQTNSGDVPPGIRNTICRM
sapiens QQGICRLFFCHSGEKKRDICSDPWNRCCVS NTDEEGKEKPEMDGRSGI gene TAP1
Homo 33 GYDTEVGEAGSQLSGGQRQAVALARALIRKP protein sapiens CV Hepcidin
Homo 84 MALSSQIWAACLLLLLLLASLTSGSVFPQQTG precursor sapiens
QLAELQPQDRAGARASWMPMFQRRRRRDT (Liver- HFPICIFCCGCCHRSKCGMCCKT
expressed antimicrobial peptide) (LEAP-1) (Putative liver tumor
regressor) (PLTR) [Contains: Hepcidin 25 (Hepc25); Hepcidin 20
(Hepc20)] High mobility Homo 215 MGKGDPKKPRGKMSSYAFFVQTCREEHKKK
group protein 1 sapiens HPDASVNFSEFSKKCSERWKTMSAKEKGKF (HMG-1)
EDMAKADKARYEREMKTYIPPKGETKKKFKD PNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIG
DVAKKLGEMWNNTAADDKQPYEKKAAKLKE KYEKDIAAYRAKGKPDAAKKGVVKAEKSKKK
KEEEEDEEDEEDEEEEEDEEDEDEEEDDDD E liver-expressed Homo 81
MWHLKLCAVLMIFLLLLGQIDGSPIPEVSSAK antimicrobial sapiens
RRPRRMTPFWRGVSLRPIGASCRDDSECITR peptide 2 LCRKGQQSPPTMLRSMEY
isoform Liver- Homo 77 MWHLKLCAVLMIFLLLLGQIDGSPIPEVSSAK expressed
sapiens RRPRRMTPFWRGVSLRPIGASCRDDSECITR antimicrobial
LCRKRRCSLSVAQE peptide 2 precursor (LEAP-2) Lysozyme C Homo 148
MKALIVLGLVLLSVTVQGKVFERCELARTLKR precursor (EC sapiens
LGMDGYRGISLANWMCLAKWESGYNTRATN 3.2.1.17) (1,4-
YNAGDRSTDYGIFQINSRYWCNDGKTPGAV beta-N-
NACHLSCSALLQDNIADAVACAKRVVRDPQG acetylmurami-
IRAWVAWRNRCQNRDVRQYVQGCGV dase C) Neutrophil Homo 94
MRTLAILAAILLVALQAQAEPLQARADEVAAA defensin 1 sapiens
PEQIAADIPEVVVSLAWDESLAPKHPGSRKN precursor
MACYCRIPACIAGERRYGTCIYQGRLWAFCC (HNP-1) (HP-1) (HP1) (Defensin,
alpha 1) [Contains: HP 1-56; Neutrophil defensin 2 (HNP-2) (HP-2)
(HP2)] Neutrophil Homo 94 MRTLAILAAILLVALQAQAEPLQARADEVAAA defensin
3 sapiens PEQIAADIPEVVVSLAWDESLAPKHPGSRKN precursor
MDCYCRIPACIAGERRYGTCIYQGRLWAFCC (HNP-3) (HP-3) (HP3) (Defensin,
alpha 3) [Contains: HP 3-56; Neutrophil defensin 2 (HNP-2) (HP-2)
(HP2)] Neutrophil Homo 97 MRIIALLAAILLVALQVRAGPLQARGDEAPGQ defensin
4 sapiens EQRGPEDQDISISFAWDKSSALQVSGSTRG precursor
MVCSCRLVFCRRTELRVGNCLIGGVSFTYCC (HNP-4) (HP-4) TRVD (Defensin,
alpha 4) Retrocyclin Homo 56 MPCFSWWPCRLRRSHFRQELMKLQPRSSLE sapiens
QMIRKWLMPLHGMKVPLFRFQTQREA Ribonuclease 7 Homo 156
MAPARAGFCPLLLLLLLGLWVAEIPVSAKPKG precursor (EC sapiens
MTSSQWFKIQHMQPSPQACNSAMKNINKHT 3.1.27.-)
KRCKDLNTFLHEPFSSVAATCQTPKIACKNG (RNase 7)
DKNCHQSHGPVSLTMCKLTSGKYPNCRYKE (Skin-derived
KRQNKSYVVACKPPQKKDSQQFHLVPVHLD antimicrobial RVL protein 2) (SAP-2)
Salivary gland Homo 46 MHDFWVLWVLLEYIYNSACSVLSATSSVSSR
antimicrobial sapiens VLNRSLQVKVVKITN salvic Secretogranin I Homo
677 MQPTLLLSLLGAVGLAAVNSMPVDNRNHNE
precursor (SgI) sapiens GMVTRCIIEVLSNALSKSSAPPITPECRQVLKT
(Chromogranin SRKDVKDKETTENENTKFEVRLLRDPADASE B) (CgB)
AHESSSRGEAGAPGEEDIQGPTKADTEKWA [Contains:
EGGGHSRERADEPQWSLYPSDSQVSEEVKT GAWK peptide;
RHSEKSQREDEEEEEGENYQKGERGEDSSE CCB peptide]
EKHLEEPGETQNAFLNERKQASAIKKEELVA RSETHAAGHSQEKTHSREKSSQESGEEAGS
QENHPQESKGQPRSQEESEEGEEDATSEVD KRRTRPRHHHGRSRPDRSSQGGSLPSEEKG
HPQEESEESNVSMASLGEKRDHHSTHYRAS EEEPEYGEEIKGYPGVQAPEDLEWERYRGR
GSEEYRAPRPQSEESWDEEDKRNYPSLELD KMAHGYGEESEEERGLEPGKGRHHRGRGG
EPRAYFMSDTREEKRFLGEGHHRVQENQMD KARRHPQGAWKELDRNYLNYGEEGAPGKW
QQQGDLQDTKENREEARFQDKQYSSHHTAE KRKRLGELFNPYYDPLQWKSSHFERRDNMN
DNFLEGEEENELTLNEKNFFPEYNYDWWEK KPFSEDVNWGYEKRNLARVPKLDLKRQYDR
VAQLDQLLHYRKKSAEFPDFYDSEEPVSTHQ EAENEKDRADQTVLTEDEKKELENLAAMDLE
LQKIAEKFSQRG Similar to Homo 226 AEGKWGLAHGRAEAHVWPGQGGWRLGPP
azurocidin 1 sapiens QGRWTGSSPLLDIVGGRKARPRQFPFLASIQ (Cationic
NQGRHFCGGALIHARFVMTAASCFQSQNPG antimicrobial
VSTVVLGAYDLRRRERQSRQTFSISSMSENG protein 37)
YDPQQNLNDLMLLQLDREANLTSSVTILPLPL (Fragment)
QNATVEAGTRCQVAGWGSQRSGGRLSRFP RFVNVTVTPEDQCRPNNVCTGVLTRRGGICN
VSAPCGGRRGPERY
[0076] TABLE-US-00002 Nonhuman Animal Antimicrobial Peptides
Organism Protein Name Name Length Sequence 11.5 kDa Carcinus 84
NKDCKYWCKDNLGLNYCCGQPGVTYPPFTK antibacterial maenas
KHLGRCPAVRDTCTGVRTQLPTYCPHDGAC protein QFRSKCCYDTCLKHHVCKTAEYPY 27
kDa Cyprinus 19 GIGGKPVQTAFVDNDGIYD antibacterial carpio protein
(Fragment) 4 kDa defensin Androctonus 37
GFGCPFNQGACHRHCRSIRRRGGYCAGLFK australis QTCTCYR 4 kDa defensin
Leiurus 38 GFGCPLNQGACHRHCRSIRRRGGYCAGFFK (Antibacterial 4
quinquestriatus QTCTCYRN kDa peptide) 7.5 kDa Ovis aries 164
METQMASPSLGRCSLWLLLLGLLLPSASAQA bactinecin
LSYREAVLRAVGQLNEKSSEVNLYRLLELDP (Fragment)
PPKDAEDQGARKPVSFRVKETVCPRTSQQP PEQCDFKENGLVKQCVGTVSLDTSNDEFDL
NCNELQSVRRLRPRRPRLPRPRPRPRPRPR SLPLPRPQPRRI Abaecin Bombus 39
FVPYNPPRPGQSKPFPSFPGHGPFNPKIQW pascuorum PYPLPNPGH Abaecin Apis
mellifera 53 MKVVIFIFALLATICAAFAYVPLPNVPQPGRRP precursor
FPTFPGQGPFNPKIKWPQGY Acaloleptin A1 Acalolepta 71
SLQPGAPNVNNKDQPWQVSPHISRDDSGNT luxuriosa
RTDINVQRHGENNDFEAGWSKVVRGPNKAK PTWHIGGTHRW Achacin Achatina 531
MLLLNSALFILCLVCWLPGTSSSRVLTRREGP precursor fulica
QCSRSVDVAVVGAGPSGTYSAYKLRNKGQT VELFEYSNRIGGRLFTTHLPNVPDLNLESGG
MRYFKNHHKIFGVLVKELNLSNKEFTEGFGK PGRTRFFARGKSLTLEEMTSGDVPYNLSTEE
KANQANLAGYYLKKLTGFDGEVLTIPQANKLE VDDGRKLYQLTVDEALDKVGTPEGKEFLKAF
STGNTEFIEGVSAVNYFLVELGEREEEILTLTD GMSALPQALADAFLKSSTSHALTLNRKLQSL
SKTDNGLYLLEFLETNTHEGYTEESNITDLVC ARKVILAIPQSALIHLDWKPLRSETVNEAFNAV
KFIPTSKVFLTFPTAWWLSDAVKNPAFVVKST SPFNQMYDWKSSNVTGDAAMIASYADTSDT
KFQENLNSKGELIPGSAPGANRVTVALKEELL SQLSQAYGIERSDIPEPKSGTSQFWSSYPFE
GDWTVWKAGYHCEYTQYIIERPSLIDDVFVV GSDHVNCIENAWTESAFLSVENVFEKYF
Acyl-CoA- Sus scrofa 87 MSQAEFEKAAEEVKNLKTKPADDEMLFIYSH binding
protein YKQATVGDINTERPGILDLKGKAKWDAWNGL (ACBP)
KGTSKEDAMKAYINKVEELKKKYGI (Diazepam binding inhibitor) (DBI)
(Endozepine) (EP) [Contains: DBI(32-86)] Adenoregulin Phyllomedusa
81 MAFLKKSLFLVLFLGLVSLSICEEEKRENEDE precursor bicolor
EEQEDDEQSEMKRGLWSKIKEVGKEAAKAA (Dermaseptin AKAAGKAALGAVSEAVGEQ
BII) (Dermaseptin B2) Alpha-defensin Macaca 96
MRTLAILAAILLVALQAQAEPLQARTDEATAA 1 mulatta
QEQIPTDNPEVVVSLAWDESLAPKDSVPGLR KNMACYCRIPACLAGERRYGTCFYMGRVWA FCC
Alpha-defensin Macaca 96 MRTLAILAAILLVALQAQAEPLQARTDEATAA 1A
mulatta QEQIPTDNPEVVVSLAWDESLAPKDSVPGLR
KNMACYCRIPACLAGERRYGTCFYLGRVWA FCC Alpha-defensin Macaca 94
MRTLAILAAILLFALLAQAKSLQETADDAATQE 2 mulatta
QPGEDDQDLAVSFEENGLSTLRASGSQARR TCRCRFGRCFRRESYSGSCNINGRIFSLCCR
Alpha-S2 Bos taurus 222 MKFFIFTCLLAVALAKNTMEHVSSSEESIISQE casein
TYKQEKNMAINPSKENLCSTFCKEVVRNANE precursor
EEYSIGSSSEESAEVATEEVKITVDDKHYQKA [Contains:
LNEINQFYQKFPQYLQYLYQGPIVLNPWDQV Casocidin-I]
KRNAVPITPTLNREQLSTSEENSKKTVDMES TEVFTKKTKLTEEEKNRLNFLKKISQRYQKFA
LPQYLKTVYQHQKAMKPWIQPKTKVIPYVRY L Androctonin Androctonus 25
RSVCRQIKICRRRGGCYYKCTNRPY australis Andropin Drosophila 57
MKYFVVLVVLALILAITVGPSDAVFIDILDKME precursor mauritiana
NAIHKAAQAGIGIAKPIEKMILPK Andropin Drosophila 57
MKYFVVLVVLALILAISVGPSDAVFIDILDKVEN precursor melanogaster
AIHNAAQVGIGFAKPFEKLINPK Andropin Drosophila 67
MKYFLVLVVLTLILAISVGQSDALFVDIIDNVEN precursor orena
AIHKAAKTGIGMVKPIENIFIPNQQKKSTEASN Andropin Drosophila 57
MKYFVVLVVLALILAITVDPSDAVFIDILDKMEN precursor sechellia
AIHKAAQAGIGLAKPIENMILPK Andropin Drosophila 60
MKYFVVLVVALILAIAVGPSDAVFIDILDKME precursor simulans
NAIHKAAQAGIGIAKPIENMILPKLTK Andropin Drosophila 62
MKYFSVLVVLTLILAIVDQSDAFINLLDKVEDA precursor teissieri
LHTGAQAGFKLIRPVERGATPKKSEKPEK Andropin Drosophila 60
MKYFSVLVVLTLILAISVGQSNAIFVDVLDNVE precursor yakuba
TALHNAAKAGFKLIKPIEKMIMPSKEK Anionic Bombina 144
MNFKYIFAVSFLIASAYARSVQNDEQSLSQRD antimicrobial maxima
VLEEESLREIRGIGGKILSGLKTALKGAAKELA peptide
STYLHRKRTAEEHEEMKRLEAVMRDLDSLDY PEEASERETRGFNQDEIANLFTKKEKRILGPV
LGLVSDTLDDVLGILG Antibacterial Carcinus 30
XXVPYPRPFPRPPIGPRPLPFPGGGRPFQS 6.5 kDa protein maenas (Fragment)
Antibacterial Bos taurus 158 METQRASLSLGRWSLWLLLLGLALPSASAQA
peptide BMAP- LSYREAVLRAVDQFNERSSEANLYRLLELDP 27 precursor
PPKEDDENPNIPKPVSFRVKETVCPRTSQQP (Myeloid
AEQCDFKENGLVKQCVGTVTLDAVKGKINVT antibacterial
CEELQSVGRFKRFRKKFKKLFKKLSPVIPLLH peptide 27) LG Antibacterial Bos
taurus 159 METQRASLSLGRWSLWLLLLGLALPSASAQA peptide BMAP-
LSYREAVLRAVDQLNEKSSEANLYRLLELDP 28 precursor
PPKEDDENPNIPKPVSFRVKETVCPRTSQQS (Myeloid
PEQCDFKENGLLKECVGTVTLDQVGSNFDIT antibacterial
CAVPQSVGGLRSLGRKILRAWKKYGPIIVPIIR peptide 28) IG Antibacterial Bos
taurus 165 METQRASFSLGRSSLWLLLLGLVVPSASAQD peptide BMAP-
LSYREAVLRAVDQFNERSSEANLYRLLELDP 34 precursor
PPEQDVEHPGARKPVSFTVKETVCPRTTPQP PEQCDFKENGLVKQCVGTVTRYWIRGDFDIT
CNNIQSAGLFRRLRDSIRRGQQKILEKARRIG ERIKDIFRG Antibacterial Bombyx
mori 59 MNFTRIIFFLFVVVFATASGKPWNIFKEIERAV peptide
ARTRDAVISAGPAVRTVAAATSVASG enbocin precursor (Moricin)
Antibacterial Sus scrofa 153 METQRASLCLGRWSLWLLLLGLVVPSASAQ peptide
PMAP- ALSYREAVLRAVDRLNEQSSEANLYRLLELD 23 precursor
QPPKADEDPGTPKPVSFTVKETVCPRPTRQP (Myeloid
PELCDFKENGRVKQCVGTVTLKEIRGNFDITC antibacterial
NQLQSVRIIDLLWRVRRPQKPKFVTVWVR peptide 23) Antibacterial Sus scrofa
166 METQRASLCLGRWSLWLLLLGLVVPSASAQ peptide PMAP-
ALSYREAVLRAVDRLNEQSSEANLYRLLELD 36 precursor
QPPKADEDPGTPKPVSFTVKETVCPRPTWR (Myeloid
PPELCDFKENGRVKQCVGTVTLNPSNDPLDI antibacterial
NCDEIQSVGRFRRLRKKTRKRLKKIGKVLKWI peptide 36) PPIVGSIPLGCG
Antibacterial Sus scrofa 167 METQRASLCLGRWSLWLLLLALVVPSASAQA
peptide PMAP- LSYREAVLRAVDRLNEQSSEANLYRLLELDQ 37 precursor
PPKADEDPGTPKPVSFTVKETVCPRPTWRP (Myeloid
PELCDFKENGRVKQCVGTVTLDQIKDPLDITC antibacterial
NEIQSVGLLSRLRDFLSDRGRRLGEKIERIGQ peptide 37) KIKDLSEFFQS
Antibacterial Carcinus 88 GLFPNKDCKYWCKDNLGLNYCCGQPGVTYP protein
11.5 maenas PFTKKHLGRCPAVRDTCTGVRTQLPTYCPHD kDa
GACQFRSKCCYDTCLKHHVCKTAEYPY (Fragment) Antibacterial Sus scrofa 172
METQRASLCLGRWSLWLLLLGLVVPSASAQ protein PR-39
ALSYREAVLRAVDRLNEQSSEANLYRLLELD precursor
QPPKADEDPGTPKPVSFTVKETVCPRPTRQP PELCDFKENGRVKQCVGTVTLNPSIHSLDISC
NEIQSVRRRPRPPYLPRPRPPPFFPPRLPPRI PPGFPPRFPPRFPGKR antibacterial Sus
scrofa 172 METQRASLCLGRWSLWLLLLALVVPSASAQA protein
LSYREAVLRAVDRLNEQSSEANLYRLLELDQ precursor
PPKADEDPGTPKPVSFTVKETVCPRPTRQPP ELCDFKENGRVKQCVGTVTLNPSIHSLDISCN
EIQSVRRRPRPPYLPRPRPPPFFPPRLPPRIP PGFPPRFPPRFPGKR antibacterial
Cavia 42 GLRKKFRKTRKRIQKLGRKIGKTGRKVXKAW protein, 11 K porcellus
REYGQIPYPCR Antifungal Galleria 76
MKIAFIVAISLAFLAVTSCIEFEKSTESHDIQKR peptide mellonella
GVTITVKPPFPGCVFYECIANCRSRGYKNGG gallerimycin YCTINGCQCLR Antifungal
Sarcophaga 85 MVKLFVIVILALIAVAFGQHGHGGQDQHGYG protein peregrina
HGQQAVYGKGHEGHGVNNLGQDGHGQHG precursor YAHGHSDQHGHGGQHGQHDGYKNRGY
(AFP) Antimicrobial Xenopus 66 LKCVNLQANGIKMTQECAKEDTKCLTLRSLK
amphipathic laevis KTLKFCASGRTCTTMKIMSLPGEQITCCEGN helix-forming
MCNA peptide Antimicrobial Acrocinus 34
CIKNGNGCQPDGSQGNCCSRYCHKEPGWV peptide ALO1 longimanus AGYCR
Antimicrobial Acrocinus 34 CIANRNGCQPDGSQGNCCSGYCHKEPGWV peptide
ALO2 longimanus AGYCR Antimicrobial Acrocinus 36
CIKNGNGCQPNGSQGNCCSGYCHKQPGWV peptide ALO3 longimanus AGYCRRK
Antimicrobial Glossina 208 MQSFKICFFISCLSVVLVKGQFGGTVSSNPN peptide
attacin morsitans GGLDVNARLSKTIGDPNANVVGGVFAAGNTD AttA
GGPATRGAFLAANKDGHGLSLQHSKTDNFG SSLTSSAHAHLFNDKTHKLDANAFHSRTHLD
NGFKFDRVGGGLRYDHVTGHGASLTASRIP QLDMNTLGLTGKANLWSSPNRATTLDLTGG
VSKHFGGPFDGQTNKQIGLGLNSRF Antimicrobial Manduca 67
MKFSRVLFFVFACFAAFTVTAAKPWDFLKEL peptide sexta
EGAGQRIRDAIISAQPAVETIAQATAIFKGQSK cecropin 6 EED Antimicrobial
Gallus gallus 39 GRKSDCFRKSGFCAFLKCPSLTLISGKCSRF peptide CHP1
YLCCKRIR (Chicken heterophil peptide 1) Antimicrobial Gallus gallus
34 GRKSDCFRKNGFCAFLKCPYLTLISGLCSXF peptide CHP2 HLC (Chicken
heterophil peptide 2) (Fragment)
Antimicrobial Glossina 87 MKFYLVLAFLTLCAVAVTALPAGDETRIDLETL peptide
morsitans EEDLRLVDGAQVTGELKRDKRVTCNIGEWV defensin DefA
CVAHCNSKSKKSGYCSRGVCYCTN Antimicrobial Glossina 76
PQSPPAQIKDPKIYASGGGSPKDGYNVNVDV peptide morsitans
RKNVWVSQNGRHSIDATGGYSQHLGGPYG diptericin DipA NSRPDFRGGASYTYRF
(Fragment) Antimicrobial Equus 46 DVQCGEGHFCHDXQTCCRASQGGXACCPY
peptide eNAP- caballus SQGVCCADQRHCCPVGF 1 (Fragment) Antimicrobial
Equus 46 EVERKHPLGGSRPGRCPTVPPGTFGHCACL peptide eNAP- caballus
CTGDASEPKGQKCCSN 2 (Fragment) Antimicrobial Manduca 171
AILFAAIVACACAQVSMPPQYAQIYPEYYKYS peptide sexta
KQVRHPRDVTWDKQVGNNGKVFGTLGQND gloverin
QGLFGKGGYQHQFFDDHRGKLTGQGYGSR (Fragment)
VLGPYGDSTNFGGRLDWANKNANAALDVTK SIGGRTGLTASGSGVWQLGKNTDLSAGGTL
SQTLGHGKPDVGFQGLFQHRW Antimicrobial Sus scrofa 82
MALSVQIRAACLLLLLLVSLTAGSVLPSQTRQ peptide
LTDLRTQDTAGATAGLTPVAQRLRRDTHFPI hepcidin CIFCCGCCRKAICGMCCKT
Antimicrobial Lumbricus 76 MSLCISDYLYLTLTFSKYERQKDKRPYSERKN peptide
rubellus QYTGPQFLYPPERIPPQKVIKWNEEGLPIYEI lumbricin1 PGEGGHAEPAAA
Antimicrobial Mytilus 82 MKAVFVLLVVGLCIMMMDVATAGFGCPNNY peptide
galloprovincialis ACHQHCKSIRGYCGGYCASWFRLRCTCYRC MGD2b
GGRRDDVEDIFDIYDNVAVERF Antimicrobial Manduca 67
MKLTSLFIFVIVALSLLFSSTDAAPGKIPVKAIK peptide moricin sexta
QAGKVIGKGLRAINIAGTTHDWSFFRPKKKK H Antimicrobial Equus 160
MKKMGCGGRLSSCPTMTSRALLLLASALLGT peptide NK- caballus
PGLTFSGLNPESYDLATAHLSDGEQFCQGLT lysin
QEDLQGDLLTERERQGIACWSCRKILQKLED LVGEQPNEATINEAASRVCRNLGLLRGACKKI
MRTCLRLISRDILAGKKPQEVCVDIKLCKHKA GLI Antimicrobial Xenopus 24
GVLSNVIGYLKKLGTGALNAVLKQ peptide PGQ laevis Antimicrobial Meleagris
65 MRIVYLLFPFILLLAQGAAGSSLALGKREKCL peptide THP1 gallopavo
RRNGFCAFLKCPTLSVISGTCSRFQVCCKTLL precursor G (Turkey heterophil
peptide 1) Antimicrobial Meleagris 64
MRILYLLFSLLFLALQVSPGLSSPKRDMLFCK peptide THP2 gallopavo
RGTCHFGRCPSHLIKVGSCFGFRSCCKWPW precursor DA (Turkey heterophil
peptide 2) Antimicrobial Meleagris 25 LSCKRGTCHFGRCPSHLIKGSCSGG
peptide THP3 gallopavo (Turkey heterophil peptide 3) (Fragment)
Antimicrobial Manduca 207 KMFTKFVVLVCLLVGAKARPQLGALTFNSDG protein
attacin sexta TSGAAVKVPFGGNKNNIFSAIGGADFNANHK 2 (Fragment)
LSSATAGVALDNIRGHGLSLTDTHIPGFGDKL TAAGKLNLFHNNNHDLTANAFATRNMPNIPQ
VPNFNTVGGGLDYMFKNKVGASLGAAHTDFI NRNDYSVGGKLNLFRNPSTSLDFNAGFKKFD
TPFMRSGWEPNMGFSLSKFF Antimicrobial Oryctolagus 171
METHKHGPSLAWWSLLLLLLGLLMPPAIAQD protein CAP18 cuniculus
LTYREAVLRAVDAFNQQSSEANLYRLLSMDP precursor (18
QQLEDAKPYTPQPVSFTVKETECPRTTWKLP kDa EQCDFKEDGLVKRCVGTVTRYQAWOSFDIR
lipopolysacchar- CNRAQESPEPTGLRKRLRKFRNKIKEKLKKIG ide- binding
QKIQGFVPKLAPRTDY protein) (18 kDa cationic protein) (CAP18-A)
Antimicrobial- Pheretima 67 MYSKYERQKDKRPYSERKDQYTGPQFLYPP like
peptide tschiliensis DRIPPSKAIKWNEEGLPMYEVLPDGAGAKTA PP-1 VEAAAE
Apidaecin Bombus 17 GNRPVYIPPPRPPHPRL pascuorum apidaecin Ib Apis
mellifera 26 EAKPEAKPGNNRPVYIPQPRPPHPRL precursor Apidaecin Apis
mellifera 168 MKNFALAILVVTFVVAVFGNTNLDPPTRPARL precursor, type
RREAKPEAEPGNNRPIYIPQPRPPHPRLRRE 14 AEPKAEPGNNRPIYIPQPRPPHPRLRREAES
EAEPGNNRPVYIPQPRPPHPRLRREPEAEPG NNRPVYIPQPRPPHPRLRREPEAEPGNNRPV
YIPQPRPPHPRI Apidaecin Apis mellifera 144
MKNFALAILVVTFVVAVFGNTNLDPPTRPTRL precursor, type
RREAEPEAEPGNNRPVYIPQPRPPHPRLRRE 22 AEPEAEPGNNRPVYIPQPRPPHPRLRREAEP
EAEPGNNRPVYIPQPRPPHPRLRREAEPEAE PGNNRPVYIPQPRPPHPRI Apidaecin Apis
mellifera 283 KNFALAILVVTFVVAVFGNTNLDPPTRPTRLR precursor, type
REAKPEAEPGNNRPVYIPQPRPPHPRLRREA 73 (Fragment)
EPEAEPGNNRPVYIPQPRPPHPRLRREAELE AEPGNNRPVYISQPRPPHPRLRREAEPEAEP
GNNRPVYIPQPRPPHPRLRREAELEAEPGNN RPVYISQPRPPHPRLRREAEPEAEPGNNRPV
YIPQPRPPHPRLRREAEPEAEPGNNRPVYIP QPRPPHPRLRREAEPEAEPGNNRPVYIPQPR
PPHPRLRREAKPEAKPGNNRPVYIPQPRPPH PRI Apolipoprotein Bos taurus 76
QAEESNLQSLVSQYFQTVADYGKDLVEKAK A-II (Apo-AII)
GSELQTQAKAYFEKTQEELTPFFKKAGTDLL (Antimicrobial NFLSSFIDPKKQPAT
peptide BAMP- 1) ASABF Ascaris suum 93
MKTAIIVVLLVIFASTNAAVDFSSCARMDVPGL precursor
SKVAQGLCISSCKFQNCGTGHCEKRGGRPT (ASABF-alpha)
CVCDRCGRGGGEWPSVPMPKGRSSRGRR HS ASABF-epsilon Ascaris suum 65
MVTKGIVLFMLVILFASTDAATCGYDDAKLNR (ASABF-
PTIGCILSCKVQGCETGACYLRDSRPICVCKR epsilon2) C ASABF-zeta Ascaris
suum 94 MKAILIALLLTTFTVVNGGVVLTSCARMDTPVL
SKAAQGLCITSCKYQNCGTGFCQKVGGRPT CMCRRCANGGGSWPVIPLDTLVKLALKRGK R
ASABF-zeta2 Ascaris suum 35 TSCKYQNCGTGFCQKVGGRPTCMCRRCAN
(Fragment) GGGSWP Attacin A Drosophila 224
MQKTSILIVALVALFAITEALPSLPTTGPIRVRR precursor melanogaster
QVLGGSLTSNPAGGADARLDLTKGIGNPNHN VVGQVFAAGNTQSGPVTTGGTLAYNNAGHG
ASLTKTHTPGVKDVFQQEAHANLFNNGRHNL DAKVFASQNKLANGFEFQRNGAGLDYSHING
HGASLTHSNFPGIGQQLGLDGRANLWSSPN RATTLDLTGSASKWTSGPFANQKPNFGAGL
GLSHHFG Attacin A Trichoplusia 254 MFTYKLILGLVLVVSASARYLVFEDLEGESYL
precursor ni VPNQAEDEQVLEGEPFYENAVQLASPRVRR
QAQGSVTLNSDGSMGLGAKVPIVGNEKNVL SALGSVDLNDQLKPASRGMGLALDNVNGHG
LSVMKETVPGFGDRLTGAGRVNVFHNDNHDI SAKAFVTKNMPDFPNVPNFNTVGGGVDYMY
KNKVGASLGMANTPFLDRKDYSAMGNLNVF RSPTTSVDFNAGFKKFDTPVFKSNWEPNFGL
TFSRSFGNKW Attacin B Drosophila 218
MQKTSILILALFAIAEAVPTTGPIRVRRQVLGG precursor melanogaster
SLASNPAGGADARLNLSKGIGNPNHNVVGQ VFAAGNTQSGPVTTGGTLAYNNAGHGASLT
KTHTPGVKDVFQQEAHANLFNNGRHNLDAK VFASQNKLANGFEFQRNGAGLDYSHINGHG
ASLTHSNFPGIGQQLGLDGRANLWSSPNRAT TLDLTGSASKWTSGPFANQKPNFGAGLGLS HHFG
Attacin B Hyalophora 233 MFAKLFLVSVLLVGVNSRYVLVEEPGYYDKQ precursor
cecropia YEEQPQQWVNSRVRRQAGALTINSDGTSGA (Immune
VVKVPITGNENHKFSALGSVDLTNQMKLGAA protein P5)
TAGLAYDNVNGHGATLTKTHIPGFGDKMTAA GKVNLFHNDNHDFSAKAFATKNMPNIPQVPN
FNTVGAGVDYMFKDKIGASANAAHTDFINRN DYSLGGKLNLFKTPTTSLDFNAGWKKFDTPF
FKSSWEPSTSFSFSKYF Aftacin E and F Hyalophora 235
MFGKIVFLLLVALCAGVQSRYLIVSEPVYYIEH precursor cecropia
YEEPELLASSRVRRDAHGALTLNSDGTSGAV (Immune
VKVPFAGNDKNIVSAIGSVDLTDRQKLGAATA protein P5)
GVALDNINGHGLSLTDTHIPGFGDKMTAAGK VNVFHNDNHDITAKAFATRNMPDIANVPNFN
TVGGGIDYMFKDKIGASASAAHTDFINRNDYS LDGKLNLFKTPDTSIDFNAGFKKFDTPFMKSS
WEPNFGFSLSKYF Attacin Bombyx mori 214
MSKSVALLLLCACLASGRHVPTRARRQAGSF precursor
TVNSDGTSGAALKVPLTGNDKNVLSAIGSAD (Nuecin)
FNDRHKLSAASAGLALDNVNGHGLSLTGTRI PGFGEQLGVAGKVNLFHNNNHDLSAKAFAIR
NSPSAIPNAPNFNTLGGGVDYMFKQKVGASL SAAHSDVINRNDYSAGGKLNLFRSPSSSLDF
NAGFKKFDTPFYRSSWEPNVGFSFSKFF Attacin-A Drosophila 221
MQNTSILIVALVALFAITEALPTTGPIRVRRQVL CG10146-PA melanogaster
GGSLTSNPAGGADARLDLTKGIGNPNHNVV GQVFAAGNTQSGPVTTGGTLAYNNAGHGAS
LTKTHTPGVKDVFQQEAHANLFNNGRHNLD AKVFASQNKLANGFEFQRNGAGLDYSHINGH
GASLTHSNFPGIGQQLGLDGRANLWSSPNR ATTLDLTGSASKWTSGPFANQKPNFGAGLGL
SHHFG Attacin-B Drosophila 218 MQKTSILILALFAIAEAVPTTGPIRVRRQVLGG
CG18372-PA melanogaster SLASNPAGGADARLNLSKGIGNPNHNVVGQ
VFAAGNTQSGPVTTGGTLAYNNAGHGASLT KTHTPGVKDVFQQEAHANLFNNGRHNLDAK
VFASQNKLANGFEFQRNGAGLDYSHINGHG GSLTHSNFPGIGQQLGLDGRANLWSSPNRA
TTLDLTGSASKWTSGPFANQKPNFGAGLGLS HHFG Azurocidin Sus scrofa 219
IVGGRRAQPQEFPFLASIQKQGRPFCAGALV (Cationic
HPRFVLTAASCFRGKNSGSASVVLGAYDLRQ antimicrobial
QEQSRQTFSIRSISQNGYDPRQNLNDVLLLQ protein CAP37)
LDREARLTPSVALVPLPPQNATVEAGTNCQV (Heparin-
AGWGTQRLRRLFSRFPRVLNVTVTSNPCLP binding protein)
RDMCIGVFSRRGRISQGDRGTPLVCNGLAQ (HBP)
GVASFLRRRFRRSSGFFTRVALFRNWIDSVL NNPP bactenecin 5 Bos taurus 42
RFRPPIRRPPIRPPFYPPFRPPIRPPIFPPIRPP FRPPLRFP Bactenecin 5 Ovis aries
176 METQGASLSLGRWSLWLLLLGLVLPSASAQA precursor
LSYREAVLRAVGQLNERSSEANLYRLLELDP (BAC5)
APNDEVDPGTRKPVSFTVKETVCPRTTQQPP EECDFKENGLVKQCVGTVTLDPSNDQFDINC
NELQSVRFRPPIRRPPIRPPFRPPFRPPVRPP IRPPFRPPFRPPIGPFPGRR Bactenecin 5
Bos taurus 176 METQRASLSLGRCSLWLLLLGLVLPSASAQA precursor
LSYREAVLRAVDQFNERSSEANLYRLLELDP (BAC5) (PR-
TPNDDLDPGTRKPVSFRVKETDCPRTSQQPL 42) EQCDFKENGLVKQCVGTVTLDPSNDQFDINC
NELQSVRFRPPIRRPPIRPPFYPPFRPPIRPPI FPPIRPPFRPPLGPFPGRR Bactenecin 5
Capra hircus 176 METQGASLSLGRWSLWLLLLGLVVPLASAQA precursor
LSYREAVLRAVGQLNERSSEANLYRLLELDP (CHBAC5)
APNDEVDPGTRKPVSFTVKETVCPRTTQQPP EECDFKENGLVKQCVGTVTLDPSNDQFDINC
NELQSVRFRPPIRRPPIRPPFNPPFRPPVRPP FRPPFRPPFRPPIGPFPGRR
bactenecin 7 Bos taurus 59 RRIRPRPPRLPRPRPRPLPFPRPGPRPIPRPL
PFPRPGPRPIPRPLPFPRPGPRPIPRP Bactenecin 7 Ovis aries 190
METQMASPSLGRCSLWLLLLGLLLPSASAQA precursor
LSYREAVLRAVGQLNEKSSEVNLYRLLELDP (BAC7)
PPKDAEDQGARKPVSFRVKETVCPRMSQQP PEQCDFKENGLVKQCVGTVSLDTSNDEFDL
NCNELQSVRRLRPRRPRLPRPRPRPRPRPR SLPLPRPQPRRIPRPILLPWRPPRPIPRPQPQ
PIPRWL Bactenecin 7 Bos taurus 190 METQRASLSLGRWSLWLLLLGLVLPSASAQA
precursor LSYREAVLRAVDRINERSSEANLYRLLELDPP (BAC7) (PR-
PKDVEDRGARKPTSFTVKETVCPRTSPQPPE 59) QCDFKENGLVKQCVGTITLDQSDDLFDLNCN
ELQSVRRIRPRPPRLPRPRPRPLPFPRPGPR PIPRPLPFPRPGPRPIPRPLPFPRPGPRPIPR PL
beta defensin Mus 74 MKISYFLLLILSLGSSQINPVSGDDSIQCFQKN 39 musculus
NTCHTNQCPYFQDEIGTCYDRRGKCCQKRL LHIRVPRKKKV Beta defensin 9 Mus 78
MPVTKSYFMTVVVVLILVDETTGGLFGFRSSK precursor musculus
RQEPWIACELYQGLCRNACQKYEIQYLSCPK (Hypothetical TRKCCLKYPRKITSF
defensin-like structure containing protein) Beta defensin- Capra
hircus 64 MRLHHLLLALFFLVLSAGSGFTQGIINHRSCY 2 precursor
RNKGVCAPARCPRNMRQIGTCHGPPVKCCR KK Beta-defensin Bos taurus 38
DFASCHTNGGICLPNRCPGHMIQIGICFRPRV 1 (BNDB-1) KCCRSW (BNBD-1)
Beta-defensin Capra hircus 64 MRLHHLLLVLFFLVLSAGSGFTQGIRSRRSCH 1
precursor RNKGVCALTRCPRNMRQIGTCFGPPVKCCR (BD-1) KK Beta-defensin
Sus scrofa 64 MRLHRLLLVFLLMVLLPVPGLLKNIGNSVSCL 1 precursor
RNKGVCMPGKCAPKMKQIGTCGMPQVKCC (BD-1) KRK (Defensin, beta 1)
Beta-defensin Pan 68 MRTSYLLLFTLCLLLSEMASGGNFLTGLGHR 1 precursor
troglodytes SDHYNCVSSGGQCLYSACPIFTKIQGTCYRG (BD-1) (hBD-1) KAKCCK
(Defensin, beta 1) Beta-defensin Mus 69
MKTHYFLLVMICFLFSQMEPGVGILTSLGRRT 1 precursor musculus
DQYKCLQHGGFCLRSSCPSNTKLQGTCKPD (BD-1) (mBD- KPNCCKS 1)
Beta-defensin Rattus 69 MKTHYFLLVMLFFLFSQMELGAGILTSLGRRT 1
precursor norvegicus DQYRCLQNGGFCLRSSCPSHTKLQGTCKPD (BD-1) (RBD-1)
KPNCCRS Beta-defensin Macaca 68 MRTSYLLLFTLCLLLSEMASGDNFLTGLGHR 1
precursor mulatta SDHYNCVRSGGQCLYSACPIYTRIQGTCYHG (BD-1) (RhBD-
KAKCCK 1) (Defensin, beta 1) Beta-defensin Ovis aries 64
MRLHHLLLVLFFVVLSAGSGFTQGVRNRLSC 1 precursor
HRNKGVCVPSRCPRHMRQIGTCRGPPVKCC (BD-1) (sBD1) RKK Beta-defensin Bos
taurus 40 QGVRSYLSCWGNRGICLLNRCPGRMRQIGT 10 (BNDB-10) CLAPRVKCCR
(BNBD-10) Beta-defensin Bos taurus 38
GPLSCRRNGGVCIPIRCPGPMRQIGTCFGRP 11 (BNDB-11) VKCCRSW (BNBD-11)
Beta-defensin Macaca 123 MKLLLLALPILVLLPQVIPAYGGEKKCWNRSG 118
precursor mulatta HCRKQCKDGEAVKETCKNHRACCVPSNEDH (Epididymal
RRLPTTSPTPLSDSTPGIIDNILTIRFTTDYFEI secretory
SSKKDMVEESEAGQGTQTSPPNVHHTS protein 13.6) (ESP13.6) Beta-defensin
Bos taurus 38 GPLSCGRNGGVCIPIRCPVPMRQIGTCFGRP 12 (BNDB-12) VKCCRSW
(BNBD-12) Beta-defensin Macaca 123 MKSLLFTLAVFMLLAQLVSGNLYVKRCLNDIG
126 precursor fascicularis ICKKTCKPEEVRSEHGWVMCGKRKACCVPA
(Epididymal DKRSAYPSFCVHSKTTKTSTVTARATATTATT secretory
ATAATPLMISNGLISLMTTMAATPVSPTT protein 13.2) (ESP13.2) Beta-defensin
Bos taurus 42 SGISGPLSCGRNGGVCIPIRCPVPMRQIGTCF 13 (BNDB-13)
GRPVKCCRSW (BNBD-13) Beta-defensin Macaca 64
MRVLYLLFSFLFIFLMPLPGVFGGIGDPVTCL 2 mulatta
KNGAICHPVFCPRRYKQIGTCGLPGTKCCKK P Beta-defensin Bos taurus 40
VRNHVTCRINRGFCVPIRCPGRTRQIGTCFG 2 (BNDB-2) PRIKCCRSW (BNBD-2)
Beta-defensin Mus 71 MRTLCSLLLICCLLFSYTTPAVGSLKSIGYEAE 2 precursor
musculus LDHCHTNGGYCVRAICPPSARRPGSCFPEK (BD-2) (mBD- NPCCKYMK 2)
Beta-defensin Rattus 63 MRIHYLLFSFLLVLLSPLSAFTQSINNPITCLTK 2
precursor norvegicus GGVCWGPCTGGFRQIGTCGLPRVRCCKKK (BD-2) (RBD-2)
Beta-defensin Ovis aries 64 MRLHHLLLVLFFVVLSAGSGFTHGVTDSLSC 2
precursor RWKKGICVLTRCPGTMRQIGTCFGPPVKCC (BD-2) (sBD2) RLK
Beta-defensin Mus 63 MRIHYLLFAFLLVLLSPPAAFSKKINNPVSCLR 3 precursor
musculus KGGRCWNRCIGNTRQIGSCGVPFLKCCKRK (BD-3) (mBD- 3)
Beta-defensin Bos taurus 57 LALLFLVLSAGSGFTQGVRNHVTCRINRGFC 3
precursor VPIRCPGRTRQIGTCFGPRIKCCRSW (BNDB-3) (BNBD-3) (Fragment)
Beta-defensin Mus 63 MRIHYLLFTFLLVLLSPLAAFTQIINNPITCMTN 4 precursor
musculus GAICWGPCPTAFRQIGNCGHFKVRCCKIR (BD-4) (mBD- 4)
Beta-defensin Bos taurus 63 MRLHHLLLAVLFLVLSAGSGFTQRVRNPQSC 4
precursor RWNMGVCIPFLCRVGMRQIGTCFGPRVPCC (BNDB-4) RR (BNBD-4)
beta-defensin 4 Mus 63 MRIHYLLFTFLPVLLSPLAAFTQIINNPITCMTN variant
musculus GAICWGPCPTAFRQIGNCGHFKVRCCKIR Beta-defensin Bos taurus 64
MRLHHLLLVLLFLVLSAGSGFTQVVRNPQSC 5 precursor
RWNMGVCIPISCPGNMRQIGTCFGPRVPCC (BNDB-5) RRW (BNBD-5) Beta-defensin
Mus 63 MKIHYLLFAFILVMLSPLAAFSQLINSPVTCMS 6 musculus
YGGSCQRSCNGGFRLGGHCGHPKIRCCRR K Beta-defensin Bos taurus 42
QGVRNHVTCRIYGGFCVPIRCPGRTRQIGTC 6 (BNDB-6) FGRPVKCCRRW (BNBD-6)
Beta-Defensin Mus 37 NSKRACYREGGECLQRCIGLFHKIGTCNFRF 7 musculus
KCCKFQ Beta-defensin Bos taurus 40 QGVRNFVTCRINRGFCVPIRCPGHRRQIGTC
7 (BNDB-7) LGPRIKCCR (BNBD-7) Beta-defensin Mus 71
MRIHYVLFAFLLVLLSPFAAFSQDINSKRACY 7 precursor musculus
REGGECLQRCIGLFHKIGTCNFRFKCCKFQIP EKKTKIL Beta-Defensin Mus 35
NEPVSCIRNGGICQYRCIGLRHKIGTCGSPFK 8 musculus CCK Beta-defensin Mus
60 MRIHYLLFTFLLVLLSPLAAFSQKINEPVSCIR 8 (Beta- musculus
NGGICQYRCIGLRHKIGTCGSPFKCCK defensin 6) Beta-defensin Bos taurus 38
VRNFVTCRINRGFCVPIRCPGHRRQIGTCLG 8 (BNDB-8) PQIKCCR (BNBD-8)
Beta-defensin Bos taurus 55 LALLFLVLSAGSGFTQGVRNFVTCRINRGFCV 9
precursor PIRCPGHRRQIGTCLAPQIKCCR (BNDB-9) (BNBD-9) (Fragment)
Beta-defensin Bos taurus 53 LALLFLVLSAGSGISGPLSCRRKGGICILIRCP C7
precursor GPMRQIGTCFGRPVKCCRSW (BBD(C7)) (Fragment) Beta-defensin
Gallus gallus 80 MRIVYLLIPFFLLFLQGAAGTATQCRIRGGFC prepropeptide
RVGSCRFPHIAIGKCATFISCCGRAYEVDALN SVRTSPWLLAPGNNPH Beta-defensin
Meleagris 59 MRIVYLLFPFFLLFLQSAAGTPIQCRIRGGFCR prepropeptide
gallopavo FGSCRFPHIAIAKCATFIPCCGSIWG Beta-defensin- Equus 64
MRILHFLLAFLIVFLLPVPGFTAGIETSFSCSQ 1 caballus
NGGFCISPKCLPGSKQIGTCILPGSKCCRKK Beta-defensin- Mus 85
MKNLPSNMALSREVFYFGFALFFIVVELPSGS 12 musculus
WAGLEYSQSFPGGEIAVCETCRLGRGKCRR (Hypothetical
TCIESEKIAGWCKLNFFCCRERI defensin-like structure containing protein)
Beta-defensin- Pan 64 MRVLYLLFSFLFIELMPLPGVFGGISDPVTCLK 2
troglodytes SGAICHPVFCPRRYKQIGTCGLPGTKCCKKP beta-defensin-3 Bos
taurus 42 QGVRNHVTCRINRGFCVPIRCPGRTRQIGTC FGPRIKCCRSW
Beta-defensin- Pan 64 MRIHYLLFALLFLFLVPVPGHGGIINTLQKYYC 3
(Fragment) troglodytes RVRGGRCAVLTCLPKEEQIGKCSTRGRKCC R
beta-defensin-4 Bos taurus 41 QRVRNPQSCRWNMGVCIPFLCRVGMRQIGT
CFGPRVPCCRR beta-defensin-5 Bos taurus 40
QVVRNPQSCRWNMGVCIPISCPGNMRQIGT CFGPRVPCCR beta-defensin-9 Bos
taurus 40 QGVRNFVTCRINRGFCVPIRCPGHRRQIGTC LGPQIKCCR Beta-defensin-
Canis 65 MKAFLLTLAALVLLSQVTSGSAEKCWNLRGS like peptide 1 familiaris
CREKCIKNEKLYIFCTSGKLCCLKPKFQPNML QR Beta-defensin- Canis 69
MKAFLLTLAALVLLSQVTSGSAEECWNLRGS like peptide 2 familiaris
CREKCIKNEKLYIFCTSGKLCCLKPKFQPNML QRSVQF Beta-defensin- Canis 99
MKAFLLTLAALVLLSQVTSGSAEKCWNLRGS like peptide 3 familiaris
CREKCIKNEKLYIFCTSGKLCCLKPKFQPNML QRNRKDNPKICLELQKILNIQSNLDKEEQSWK
HCTS Big defensin Tachypleus 79 NPLIPAIYIGATVGPSVWAYLVALVGAAAVTA
tridentatus ANIRRASSDNHSCAGNRGWCRSKCFRHEYV DTYYSAVCGRYFCCRSR
bombinin H Bombina 20 IIGPVLGMVGSALGGLLKKI
Met-8 variegata Bombinin Bombina 21 IIGPVLGMVGSALGGLLKKIG H1/H3
variegata Bombinin H4 Bombina 21 LIGPVLGLVGSALGGLLKKIG variegata
Bombinin H5 Bombina 21 IIGPVLGLVGSALGGLLKKIG variegata
Bombinin-like Bombina 27 GIGSAILSAGKSALKGLAKGLAEHFAN peptide 2
(BLP- orientalis 2) Bombinin-like Bombina 25
GIGAAILSAGKSIIKGLANGLAEHF peptide 4 (BLP- orientalis 4)
Bombinin-like Bombina 144 MNFKYIVAVSFLIASTYARSVKNDEQSLSQRD peptide
7, BPL- orientalis VLEEESLREIRGIGGALLSAGKSALKGLAKGL 7 precursor
AEHFANGKRTAEEHEVMKRLEAVMRDLDSL DYPEEASEMETRSFNQEEIANLFTKKEKRILG
PVLDLVGRALRGLLKKIG Bombinin-like Bombina 204
MNFKYIVAVSILIASAYARSEENDIQSLSQRDV peptides 1 orientalis
LEEESLREIRGIGASILSAGKSALKGLAKGLAE precursor
HFANGKRTAEDHEVMKRLEAAIQSLSQRDVL [Contains:
EEESLREIRGIGASILSAGKSALKGLAKGLAEH Acidic peptide
FANGKRTAEEHEVMKRLEAVMRDLDSLDYP 1; Bombinin-
EEASEMETRSFNQEEIANLYTKKEKRILGPIL like peptide 1 GLVSNALGGLLG
(BLP-1); Octapeptide 1; Acidic peptide 2; Octapeptide 2; Acidic
peptide 3; GH- 1 peptide] Bombinin-like Bombina 137
MNFKYIVAVSILIASAYARSEENDIQSLSQRDV peptides 1 variegata
LEEESLREIRGIGGALLSAAKVGLKGLAKGLA precursor
EHFANGKRTAEEREVMKRLEAAMRDLDSFE [Contains:
HPEEASEKETRGFNQEEKEKRIIGPVLGLVGS Acidic peptide ALGGLLKKIG 1-1;
Bombinin- like peptide 1 (BLP-1); Octapeptide 1; Acidic peptide
1-2; Bombinin H] Bombinin-like Bombina 137
MNFKYIVAVSILIASAYARREENNIQSLSQRDV peptides 2 variegata
LEEESLREIRGIGASILSAGKSALKGFAKGLAE precursor
HFANGKRTAEDHEMMKRLEAAVRDLDSLEH [Contains:
PEEASEKETRGFNQEEKEKRIIGPVLGLVGSA Acidic peptide LGGLLKKIG 2-1;
Bombinin- like peptide 2 (BLP-2); Octapeptide 2; Acidic peptide
2-2; Bombinin H2] Bombinin-like Bombina 200
MNFKYIVAVSILIASAYARSEENDIQSLSQRDV peptides 3 orientalis
LEEESLREIRGIGAAILSAGKSALKGLAKGLAE precursor
HFGKRTAEDHEVMKRLEAAIHSLSQRDVLEE [Contains:
ESLREIRGIGAAILSAGKSALKGLAKGLAEHF Acidic peptide
GKRTAEEHEMMKRLEAVMRDLDSLDYPEEA 1; Bombinin-
SEMETRSFNQEEIANLYTKKEKRILGPILGLVS like peptide 3 NALGGLLG (BLP-3);
Octapeptide 1; Acidic peptide 2; Octapeptide 2; Acidic peptide 3;
GH- 1 peptide] Bovine Bos taurus 38 APLSCGRNGGVCIPIRCPVPMRQIGTCFGRP
Neutrophil VKCCRSW Beta-Defensin 12 Brevinin-1 Rana 24
FLPVLAGIAAKVVPALFCKITKKC brevipoda Brevinin-1BA Rana 24
FLPFIAGMAAKFLPKIFCAISKKC berlandieri Brevinin-1BB Rana 24
FLPAIAGMAAKFLPKIFCAISKKC berlandieri Brevinin-1BC Rana 24
FLPFIAGVAAKFLPKIFCAISKKC berlandieri Brevinin-1BD Rana 24
FLPAIAGVAAKFLPKIFCAISKKC berlandieri Brevinin-1BE Rana 24
FLPAIVGAAAKFLPKIFCVISKKC berlandieri Brevinin-1BF Rana 24
FLPFIAGMAANFLPKIFCAISKKC berlandieri Brevinin-1E Rana 71
MFTLKKSMLLLFFLGTINLSLCEEERDADEEE precursor esculenta
RRDNPDESEVEVEKRFLPLLAGLAANFLPKIF CKITRKC Brevinin-1Ea Rana 24
FLPAIFRMAAKVVPTIICSITKKC esculenta brevinin-1Eb Rana 24
VIPFVASVAAEMMQHVYCAASRKC esculenta Brevinin-1Eb Rana 23
VIPFVASVAAEMQHVYCAASRKC esculenta Brevinin-1LA Rana 24
FLPMLAGLAASMVPKLVCLITKKC luteiventris Brevinin-1LB Rana 24
FLPMLAGLAASMVPKFVCLITKKC luteiventris Brevinin-1PA Rana pipiens 24
ELPIIAGVAAKVFPKIFCAISKKC Brevinin-1PB Rana pipiens 24
FLPIIAGIAAKVFPKIFCAISKKC Brevinin-1PC Rana pipiens 24
FLPIIASVAAKVFSKIFCAISKKC Brevinin-1PD Rana pipiens 24
FLPIIASVAANVFSKIFCAISKKC Brevinin-1PE Rana pipiens 24
FLPIIASVAAKVFPKIFCAISKKC Brevinin-1Sa Rana 24
FLPAIVGAAGQFLPKIFCAISKKC sphenocephala Brevinin-1Sb Rana 24
FLPAIVGAAGKFLPKIFCAISKKC sphenocephala Brevinin-1Sc Rana 24
FFPIVAGVAGQVLKKIYCTISKKC sphenocephala Brevinin-1SY Rana 24
FLPVVAGLAAKVLPSIICAVTKKC sylvatica Brevinin-1T Rana 20
VNPIILGVLPKFVCLITKKC temporaria Brevinin-1TA Rana 17
FITLLLRKFICSITKKC temporaria Brevinin-2 Rana 33
GLLDSLKGFAATAGKGVLQSLLSTASCKLAKT brevipoda C Brevinin-2E Rana 33
GIMDTLKNLAKTAGKGALQSLLNKASCKLSG esculenta QC Brevinin-2Ea Rana 33
GILDTLKNLAISAAKGAAQGLVNKASCKLSGQ esculenta C Brevinin-2Eb Rana 33
GILDTLKNLAKTAGKGALQGLVKMASCKLSG esculenta QC Brevinin-2Ec Rana 34
GILLDKLKNFAKTAGKGVLQSLLNTASCKLSG esculenta QC Brevinin-2Ed Rana 29
GILDSLKNLAKNAGQILLNKASCKLSGQC esculenta Brevinin-2Ee Rana 29
GIFDKLKNFAKGVAQSLLNKASCKLSGQC esculenta Brevinin-2Ef Rana 74
MFTMKKSLLLIFFLGTISLSLCQEERNADDDD precursor esculenta
GEMTEEEKRGIMDTLKNLAKTAGKGALQSLV KMASCKLSGQC Brevinin-2T Rana 33
GLLSGLKKVGKHVAKNVAVSLMDSLKCKISG temporaria DC Brevinin-2Tb Rana 74
MFTMKKSLLLFFFLGTISLSLCQEERNADEDD precursor temporaria
GEMTEEEKRGILDTLKHLAKTAGKGALQSLL NHASCKLSGQC Brevinin-2TC Rana 29
GLWETIKNFGKKFTLNILHKLKCKIGGGC temporaria Brevinin-2TD Rana 29
GLWETIKNFGKKFTLNILHNLKCKIGGGC temporaria buforin I Bufo 129
MSGRGKQGGKVRAKAKTRSSRAGLQFPVG gargarizans
RVHRLLRKGNYAQRVGAGAPVYLAAVLEYLT AEILELAGNAARDNKKTRIIPRHLQLAVRNDE
ELNKLLGGVTIAQGGVLPNIQAVLLPKTESSK PAKSK Buthinin Androctonus 34
SIVPIRCRSNRDCRRFCGFRGGRCTYARQCL australis CGY Caeridin Litoria
chloris 13 MGLLDGLLGTLGL 1.1/1.2/1.3 Caeridin Litoria 12
GLLDGLLGTLGL 1.1/1.2/1.3 xanthomera Caeridin 1.4 Litoria chloris 13
MGLLDGLLGGLGL Caeridin 1.4 Litoria 12 GLLDGLLGGLGL xanthomera
Caerin 1.1 Litoria 26 MGLLSVLGSVAKHVLPHVVPVIAEHL caerulea Caerin
1.1 Litoria 25 GLLSVLGSVAKHVLPHVVPVIAEHL splendida Caerin 1.6
Litoria chloris 25 MGLFSVLGAVAKHVLPHVVPVIAEK Caerin 1.6 Litoria 24
GLFSVLGAVAKHVLPHVVPVIAEK xanthomera Caerin 1.7 Litoria chloris 25
MGLFKVLGSVAKHLLPHVAPVIAEK Caerin 1.7 Litoria 24
GLFKVLGSVAKHLLPHVAPVIAEK xanthomera Caerulein Litoria 10 QQDYTGWMDF
xanthomera cathelin related Mus 172 MQFQRDVPSLWLWRSLSLLLLLGLGFSQTPS
antimicrobial musculus YRDAVLRAVDDFNQQSLDTNLYRLLDLDPEP peptide
QGDEDPDTPKSVRFRVKETVCGKAERQLPE QCAFKEQGWKQCMGAVTLNPAADSFDISC
NEPGAQPFRFKKISRLAGLLRKGGEKIGEKLK KIGQKIKNFFQKLVPQPE Cathelin- Mus
173 MQFQRDVPSLWLWRSLSLLLLLGLGFSQTPS related musculus
YRDAVLRAVDDFNQQSLDTNLYRLLDLDPEP antimicrobial
QGDEDPDTPKSVRFRVKETVCGKAERQLPE peptide
QCAFKEQGWKQCMGAVTLNPAADSFDISC precursor
NEPGAQPFRFKKISRLAGLLRKGGEKIGEKLK (Cramp) KIGQKIKNFFQKLVPQPEQ
(Cathelin-like protein) (CLP) Cathelin- Ovis aries 160
METQRASLSLGRCSLWLLLLGLALPSASAQV related peptide
LSYREAVLRAADQLNEKSSEANLYRLLELDP SC5 precursor
PPKQDDENSNIPKPVSFRVKETVCPRTSQQP 1 (Antibacterial
AEQCDFKENGLLKECVGTVTLDQVRNNFDIT
peptide SMAP- CAEPQSVRGLRRLGRKIAHGVKKYGPTVLRII 29) (Myeloid RIAG
antibacterial peptide SMAP- 29) Cathelin- Ovis aries 160
METQRASLSLGRRSLWLLLLGLVLASASAQA related peptide
LSYREAVLRAVDQLNEKSSEANLYRLLELDP SC5 precursor
PPKQDDENSNIPKPVSFRVKETVCPRTSQQP 2 (Antibacterial
AEQCDFKENGLLKECVGTVTLDQVGNNFDIT peptide SMAP-
CAEPQSVRGLRRLGRKIAHGVKKYGPTVLRII 29) (Myeloid RIAG antibacterial
peptide SMAP 29) cathelin-related Ovis aries 160
METQRAGLSLGRRSLWLLLLGLVLASASAQA protein 1
LSYREAVLRAVDQLNEKSSEANLYRLLELDP precursor
PPKQDDENSNIPKPVSFRVKETVCPRTSQQP AEQCDFKENGLLKECVGTVTLDQVGNNFDIT
CAEPQSVRGLRRLGRKIAHGVKKYGPTVLRII RIAG cathelin-related Ovis aries
152 SLGRCSLWLLLLGLALPSASAQVLSYREAVL protein 2
RAADQLNEKSSEANLYRLLELDPPPKQDDEN precursor
SNIPKPVSFRVKETVCPRTSQQPAEQCDFKE NGLLKECVGTVTLDQVRNNFDITCAEPQSVR
GLRRLGRKIAHGVKKYGPTVLRIIRIAG Cecropin Bombyx mori 35
RWKIFKKIEKVGQNIRDGIVKAGPAVAVVGQA (Antibacterial ATI peptide CM-IV)
Cecropin 1 Ceratitis 63 MNFNKVFILVAIVIAIFAGQTEAGWLKKIGKKIE
precursor capitata RVGQHTRDATIQTIAVAQQAANVAATARG Cecropin 1
Drosophila 63 MNFYKVFIFVALILAISLGQSEAGWLKKIGKKI precursor virilis
ERIGQHTRDATIQGLGIAQQAANVAATARG Cecropin 2 Ceratitis 63
MNFNKVLVLLAVIFAVFAGQTEAGWLKKIGKK precursor capitata
IERVGQHTRDATIQTIGVAQQAANVAATLKG Cecropin 2 Drosophila 63
MNFYKVFIFVALILAISLGQSEAGWLKKIGKKI precursor virilis
ERVGQHTRDATIQGLGIAQQAANVAATARG Cecropin 3 Drosophila 63
MNFYKVFIFVALILAISLGQSEAGWLKKIGKKI precursor virilis
ERIGQHTRDATIQGVGIAQQAANVAATARG Cecropin A Aedes 59
MNFTKLFLLIAVAVLLLTGQSEAGGLKKLGKK precursor aegypti
LEGAGKRVFNAAEKALPVVAGAKALRK Cecropin A Bombyx mori 63
MNFVRILSFVFALVLALGAVSAAPEPRWKLFK precursor
KIEKVGRNVRDGLIKAGPAIAVIGQAKSLGK Cecropin A Trichoplusia 62
MNLVKILFCVFACLVFTVTAVPEPRWKFFKKI precursor ni
EKVGQNIRDGIIKAGPAVAWGQAASITGK Cecropin A Hyalophora 64
MNFSRIFFFVFACLTALAMVNAAPEPKWKLF precursor cecropia
KKIEKVGQNIRDGIIKAGPAVAWGQATQIAK (Cecropin C) G Cecropin A
Spodoptera 57 IFFFVFACLLALSAVSAAPEPRWKVFKKIEKV precursor litura
GRNVRDGIIKAGPAIGVLGQAKALG (Fragment) Cecropin Drosophila 63
MNFYNIFVFVALILAITIGQSEAGWLKKIGKKIE A1/A2 melanogaster
RVGQHTRDATIQGLGIAQQAANVAATARG precursor Cecropin B Antheraea 35
KWKIFKKIEKVGRNIRNGIIKAGPAVAVLGEAK pernyi AL Cecropin B Drosophila
63 MNFNKIFVFVALILAISLGNSEAGWLRKLGKKI precursor melanogaster
ERIGQHTRDASIQVLGIAQQAANVAATARG Cecropin B Spodoptera 58
ILSFVFACLLALSAVSAAPEPRWKVFKKIEKM precursor litura
GRNIRDGIVKAGPAIEVLGSAKALGK (Fragment) Cecropin B Hyalophora 62
MNFSRIFFFVFALVLALSTVSAAPEPKWKVFK precursor cecropia
KIEKMGRNIRNGIVKAGPAIAVLGEAKALG (Immune protein P9) Cecropin B
Bombyx mori 63 MNFAKILSFVFALVLALSMTSAAPEPRWKIFK precursor
KIEKMGRNIRDGIVKAGPAIEVLGSAKAIGK (Lepidopteran A and B) Cecropin C
Drosophila 63 MNENKIFVFVALILAISLGQSEAGWLKKLGKRI precursor erecta
ERIGQHTRDATIQGLGIAQQAANVAATARG Cecropin C Drosophila 63
MNFYKIFVFVALILAISIGQSEAGWLKKLGKRI precursor mauritiana
ERIGQHTRDATIQGLGIAQQAANVAATARG Cecropin D Bombyx mori 61
MKFSKIFVFVFAIVFATASVSAAPGNFFKDLE precursor
KMGQRVRDAVISAAPAVDTLAKAKALGQG Cecropin D Hyalophora 62
MNFTKILFFWACVFAMRTVSAAPWNPFKEL precursor cecropia
EKVGQRVRDAVISAGPAVATVAQATALAKGK Cecropin P1 Sus scrofa 31
SWLSKTAKKLENSAKKRISEGIAIAIQGGPR ceratotoxin A Ceratitis 29
SIGSALKKALPVAKKIGKIALPIAKAALP capitata Ceratotoxin A Ceratitis 71
MANLKAVFLICIVAFIALQCVVAEPAAEDSVVV precursor 1 capitata
KRSIGSALKKALPVAKKIGKIALPIAKAALPVAA GLVG Ceratotoxin A Ceratitis 71
MANLKAVFLICIVAFIAFQCVVAEPAAEDSIVV precursor 2 capitata
KRSIGSALKKALPVAKKIGKIALPIAKAALPVAA GLVG Ceratotoxin B Ceratitis 29
SIGSAFKKALPVAKKIGKAALPIAKAALP capitata Ceratotoxin C Ceratitis 67
MANIKAVFLICIVAFIAFHCVVAEPTAEDSVVV precursor capitata
KRSLGGVISGAKKVAKVAIPIGKAVLPVVAKLV G Ceratotoxin D Ceratitis 71
MANLKAVFLICILAFIAFHCWGAPTAEDSIVV precursor capitata
KRSIGTAVKKAVPIAKKVGKVAIPIAKAVLSVV GQLVG Chlamysin Chlamys 137
MMYFVLFCLLAAGTTYGSHNFATGIVPHSCL precursor islandica
ECICKTESGCRAIGCKFDVYSDSCGYFQLKQ AYWEDCGRPGGSLTSCADDIHCSSQCVQHY
MSRYIGHTSCSRTCESYARLHNGGPHGCEH GSTLGYWGHVQGHGC Chromogranin Bos
taurus 449 MRSAAVLALLLCAGQVIALPVNSPMNKGDTE A precursor
VMKCIVEVISDTLSKPSPMPVSKECFETLRGD (CgA) (Pituitary
ERILSILRHQNLLKELQDLALQGAKERTHQQK secretory
KHSSYEDELSEVLEKPNDQAEPKEVTEEVSS protein I) (SP-I)
KDAAEKRDDFKEVEKSDEDSDGDRPQASPG [Contains:
LGPGPKVEEDNQAPGEEEEAPSNAHPLASLP Vasostatin-1
SPKYPGPQAKEDSEGPSQGPASREKGLSAE Chromostatin;
QGRQTEREEEEEKWEEAEAREKAVPEEESP Chromacin;
PTAAFKPPPSLGNKETQRAAPGWPEDGAGK Pancreastatin;
MGAEEAKPPEGKGEWAHSRQEEEEMARAP WE-14; QVLFRGGKSGEPEQEEQLSKEWEDAKRWS
Catestatin] KMDQLAKELTAEKRLEGEEEEEEDPDRSMR
LSFRARGYGFRGPGLQLRRGWRPNSREDSV EAGLPLQVRGYPEEKKEEEGSANRRPEDQE
LESLSAIEAELEKVAHQLEELRRG chromogranin Bos taurus 170
MPVDIRNHNEEVVTHLRDPADTSEAPGLSAG B EPPGSQVAKEAKTRYSKSEGQNREEEMVKY
QKRERGEVGSEERLSEGPQRNQTPAKKSSQ EGNPPLEEESHVGTGALEEGAERLPGELRNY
LDYGEEKGEESAEFPDFYDSEEQMSPQHTA EDLELQKIAEKFSGTRRG Chrysophsin-1
Pagrus major 25 FFGWLIKGAIHAGKAIHGLIHRRRH Chrysophsin-2 Pagrus
major 25 FFGWLIRGAIHAGKAIHGLIHRRRH Chrysophsin-3 Pagrus major 20
FIGLLISAGKAIHDLIRRRH Cicadin Cicada 55
NEYHGFVDKANNENKRKKQQGRDDFWKPN (Fragment) flammata
NFANRRRKDDYNENYYDDVDAADVV Citropin 1.1 Litoria citropa 16
GLFDVIKKVASVIGGL [Contains: Citropin 1.1.1; Citropin 1.1.2]
Citropin 1.1.3 Litoria citropa 18 GLFDVIKKVASVIGLASP Citropin 1.1.4
Litoria citropa 18 GLFDVIKKVASVIGLASQ Citropin 1.2 Litoria citropa
16 GLFDIIKKVASVVGGL [Contains: Citropin 1.2.1; Citropin 1.2.2;
Citropin 1.2.3] Citropin 1.2.4 Litoria citropa 18
GLFDIIKKVASVVGLASP Citropin 1.2.5 Litoria citropa 18
GLFDIIKKVASVVGLASQ Citropin 1.3 Litoria citropa 16 GLFDIIKKVASVIGGL
Citropin 2.1.3 Litoria citropa 26 GLIGSIGKALGGLLVDVLKPKLQAAS
[Contains: Citropin 2.1.2; Citropin 2.1.1; Citropin 2.1] Citropin
3.1.2 Litoria citropa 24 DLFQVIKEKLKELTGGVIEGIQGV [Contains:
Citropin 3.1.1; Citropin 3.1] Clavanin A Styela clava 80
MKTTILILLILGLGINAKSLEERKSEEEKVFQFL precursor
GKIIHHVGNFVHGFSHVFGDDQQDNGKFYG HYAEDNGKHWYDTGDQ Clavanin B Styela
clava 23 VFQFLGRIIHHVGNFVHGFSHVF Clavanin C Styela clava 80
MKTTILILLILGLGINAKSLEERKSEEEKVFHLL precursor
GKIIHHVGNFVYGFSHVFGDDQQDNGKFYG HYAEDNGKHWYDTGDQ Clavanin D Styela
clava 80 MKTTILILLILGLGINAKSLEERKSEEEKAFKLL precursor
GRIIHHVGNFVYGFSHVFGDDQQDNGKFYG HYAEDNGKHWYDTGDQ Clavanin E Styela
clava 80 MKTTILILLILGLGINAKSLEERKSEEEKLFKLL precursor
GKIIHHVGNFVHGFSHVFGDDQQDNGKFYG YYAEDNGKHWYDTGDQ Coleoptericin
Zophobas 74 SLQGGAPNFPQPSQQNGGWQVSPDLGRDD atratus
KGNTRGQIEIQNKGKDHDFNAGWGKVIRGP NKAKPTWHVGGTYRR Corticostatin I
Oryctolagus 93 MRTLILLAAILLAALQAQAELFSVNVDEVLDQ precursor (CS-
cuniculus QQPGSDQDLVIHLTGEESSALQVPDTKGICA I) (Neutrophil
CRRRFCPNSERFSGYCRVNGARYVRCCSRR antibiotic peptide NP-3A)
(Microbicidal peptide NP-3A) (Antiadrenocort- icotropin peptide I)
Corticostatin II Oryctolagus 34 GRCVCRKQLLCSYRERRIGDCKIRGVRFPFC
(CS-II) cuniculus CPR (Neutrophil antibiotic peptide NP-3B)
(Microbicidal peptide NP-3B) (Antiadrenocort- icotropin peptide II)
Corticostatin III Oryctolagus 95 MRTLALLAAILLVALQAQAEHVSVSIDEVVDQ
precursor (CS- cuniculus QPPQAEDQDVAIYVKEHESSALEALGVKAGV III)
VCACRRALCLPRERRAGFCRIRGRIHPLCCR (Macrophage R antibiotic peptide
MCP- 1) (NP-1) (Antiadrenocort- icotropin peptide III)
Corticostatin IV Oryctolagus 95
MRTLALLAAILLVALQAQAEHISVSIDEVVDQQ
precursor (CS- cuniculus PPQAEDQDVAIYVKEHESSALEALGVKAGVV IV)
CACRRALCLPLERRAGFCRIRGRIHPLCCRR (Macrophage antibiotic peptide MCP-
2) (NP-2) (Antiadrenocort- icotropin peptide IV) Corticostatin VI
Oryctolagus 34 GICACRRRFCLNFEQFSGYCRVNGARYVRC (CS-VI) cuniculus
CSRR (Neutrophil antibiotic peptide NP-6) Corticostatin-
Oryctolagus 32 MPCSCKKYCDPWEVIDGSCGLFNSKYICCRE related peptide
cuniculus K RK-1 Crabrolin Vespa crabro 13 FLPLILRKIVTAL cryptdin
Mus 23 CKRRERMNGTCRKGHLLYTLCCR musculus cryptdin 12 Mus 35
LRDLVCYCRARGCKGRERMNGTCRKGHLLY musculus MLCCR Cryptdin-1 Mus 35
LRDLVCYCRTRGCKRRERMNXTCRKGHLMY (CR1) musculus TLCCX Cryptdin-1 Mus
93 MKKLVLLFALVLLGFQVQADSIQNTDEETKTE precursor musculus
EQPGEEDQAVSVSFGDPEGTSLQEESLRDL (DEFCR)
VCYCRSRGCKGRERMNGTCRKGHLLYTLCC R cryptdin-10 Mus 35
LRDLVCYCRKRGCKGRERMNGTCRKGHLLY musculus TLCCR Cryptdin-10 Mus 92
KTLVLLSALVLLAFQVQADPIQNTDEETKTEE precursor musculus
QPGEDDQAVSVSFGDPEGSSLQEESLRDLV (Fragment)
CYCRKRGCKGRERMNGTCRKGHLLYTMCC R cryptdin-11 Mus 35
LRDLVCYCRSRGCKGRERMNGTCRKGHLLY musculus MLCCR Cryptdin-11 Mus 85
ALVLLAFQVQADPIQNTDEETKTEEQPGEED precursor musculus
QAVSVSFGDPEGTSLQEESLRDLVCYCRSR (Fragment) GCKGRERMNGTCRKGHLLYMLCCR
cryptdin-13 Mus 35 LRDLVCYCRKRGCKRREHMNGTCRRGHLM musculus YTLCCR
Cryptdin-13 Mus 93 MKTLVLLSALVLLAFQVQADPIQNTDEETKTE precursor
musculus EQPGEEDQAVSVSFGDPEGTSLQEESLRDL
VCYCRKRGCKRREHMNGTCRRGHLMYTLC CR Cryptdin-14 Mus 85
ALVLLAFQVQADPIQNTDEETKTEEQPGEDD precursor musculus
QAVSVSFGDPEGSSLQEESLRDLVCYCRTR (Fragment) GCKRRERMNGTCRKGHLMHTLCCR
cryptdin-15 Mus 35 LRDLVCYCRKRGCKRREHINGTCRKGHLLY musculus MLCCR
Cryptdin-15 Mus 93 MKTLVLLSALVLLAFQVQADPIQNTDEETKTE precursor
musculus EQPGEDDQAVSVSFGDPEGSSLQEESLRDL
VCYCRKRGCKRREHINGTCRKGHLLYMLCC R cryptdin-16 Mus 35
LRDLVCYCRSRGCKGRERMNGTCRKGHLM musculus YTLCCR Cryptdin-16 Mus 93
MKTLILLSALVLLAFQVQADPIQNTDEETKTEE precursor musculus
QPGEEDQAVSVSFGDPEGTSLQEESLRDLV CYCRSRGCKGRERMNGTCRKGHLMYTLCC R
Cryptdin-17 Mus 82 LLAFQVQADPIQNTDEETKTEEQPGEEDQAV precursor
musculus SVSFGDPEGTSLQEESLRDLVCYCRKRGCK (CRYP17)
RREHMNGTCRKGHLLYTLCCR (Fragment) Cryptdin-2 Mus 35
LRDLVCYCRARGXKGRERMNGTXRKGHLLY (CR2) musculus MXXXX Cryptdin-2 Mus
93 MKPLVLLSALVLLSFQVQADPIQNTDEETKTE precursor musculus
EQSGEEDQAVSVSFGDREGASLQEESLRDL VCYCRTRGCKRRERMNGTCRKGHLMYTLC CR
Cryptdin-3 Mus 93 MKTLVLLSALVLLAFQVQADPIQNTDEETKTE precursor
musculus EQPGEDDQAVSVSFGDPEGSSLQEESLRDL
VCYCRKRGCKRRERMNGTCRKGHLMYTLC CR cryptdin-4 Mus 34
LRGLLCYCRKGHCKRGERVRGTCGIRFLYCC musculus PRR Cryptdin-4 Mus 92
MKTLVLLSALVLLAFQVQADPIQNTDEETKTE precursor musculus
EQPGEEDQAVSISFGGQEGSALHEKSLRGLL CYCRKGHCKRGERVRGTCGIRFLYCCPRR
Cryptdin-5 Mus 93 MKTFVLLSALVLLAFQVQADPIHKTDEETNTE precursor
musculus EQPGEEDQAVSISFGGQEGSALHEELSKKLI
CYCRIRGCKRRERVFGTCRNLFLTFVFCCS Cryptdin-6/12 Mus 93
MKTLILLSALVLLAFQVQADPIQNTDEETKTEE precursor musculus
QPGEEDQAVSVSFGDPEGTSLQEESLRDLV CYCRARGCKGRERMNGTCRKGHLLYMLCC R
cryptdin-7 Mus 35 LRDLVCYCRTRGCKRREHMNGTCRKGHLMY musculus TLCCR
Cryptdin-7 Mus 93 MKTLILLSALVLLAFQVQADPIQNTDEETKTEE precursor
musculus QPGEDDQAVSVSFGDPEGSSLQEESLRDLV
CYCRTRGCKRREHMNGTCRKGHLMYTLCC R cryptdin-8 Mus 35
LRDLVCYCRKRGCKRREHMNGTCRKGHLM musculus YTLCCR Cryptdin-8 Mus 81
LAFQVQADPIQNTDEETKTEEQPGEDDQAVS precursor musculus
VSFGDPEGSSLQEESLRDLVCYCRKRGCKR (Fragment) REHMNGTCRKGHLMYTLCCR
cryptdin-9 Mus 35 LRDLVCYCRKRGCKRREHMNGTCRKGHLLY musculus MLCCR
Cryptdin-9 Mus 93 MKTLVLLSALVLLAFQVQADPIQNTDEETKTE precursor
musculus EQPGEEDQAVSVSFGDPEGSSLQEESLRDL
VCYCRKRGCKRREHMNGTCRKGHLLYMLC CR Cryptdin- Mus 116
MKTLVLLSALVLPCFQVQADPIQNTDEETKTE related protein musculus
EQPEEEDQAVSVSFGGTEGSALQDVAQRRF 1C precursor
PWCRKCRVCQKCQVCQKCPVCPTCPQCPK (CRS1C) QPLCEERQNKTAITTQAPNTQHKGC
Cryptdin- Mus 91 MKKLVLLFALVLLAFQVQADSIQNTDEETKTE related protein
musculus EQPGEKDQAVSVSFGDPQGSALQDAALGW 4C-1 precursor
GRRCPQCPRCPSCPSCPRCPRCPRCKCNP (CRS4C) K Cryptdin- Mus 91
MKKLVLLFALVLLAFQVQADSIQNTDEETKTE related protein musculus
EQQGEEDQAVSVSFGDPQGSGLQDAALGW 4C-2 precursor
GRRCPRCPPCPRCSWCPRCPTCPRCNCNP (CRS4C) K Cryptdin- Mus 91
MKKLVLLSAFVLLAFQVQADSIQNTDEETKTE related protein musculus
EQPGEENQAMSVSFGDPEGSALQDAAVGM 4C-4 precursor
ARPCPPCPSCPSCPWCPMCPRCPSCKCNP (CRS4C) K Cryptdin- Mus 91
MKKLVLLSAFVLLAFQVQADSIQNTDEEIKTE related protein musculus
EQPGEENQAVSISFGDPEGYALQDAAIRRAR 4C-5 precursor
RCPPCPSCLSCPWCPRCLRCPMCKCNPK (CRS4C) Cyclic Bos taurus 155
METPRASLSLGRWSLWLLLLGLALPSASAQA dodecapeptide
LSYREAVLRAVDQLNEQSSEPNIYRLLELDQP precursor
PQDDEDPDSPKRVSFRVKETVCSRTTQQPP (Bactenecin 1)
EQCDFKENGLLKRCEGTVTLDQVRGNFDITC NNHQSIRITKQPWAPPQAARLCRIVVIRVCR
Cyclic Ovis aries 155 METQRASLSLGRCSLWLLLLGLALPSASAQV dodecapeptide
LSYREAVLRAVDQLNEQSSEPNIYRLLELDQP precursor
PQDDEDPDSPKRVSFRVKETVCPRTTQQPP (Bactenecin 1)
EQCDFKENGLLKRCEGTVTLDQVRGNFDITC NNHQSIRITKQPWAPPQAARICRIIFLRVCR
DEFB1-like Cercopithecus 68 MRTSYLLLFTLCLLLSEMASGDNFLTGLGHR protein
aethiops SDHYNCVRSGGQCLYSACPIYTKIQGTCYHG KAKCCK DEFB1-like
Cercopithecus 68 MRTSYLLLFTLCLLLSEMASGDNFLTGLGHR protein
erythrogaster SDHYICVRSGGQCLYSACPIYTKIQGTCYHG KAKCCK DEFB1-like
Gorilla gorilla 68 MRTSYLLLFTLCLLLSEIASGGNFLTGLGHRS protein
DHYNCVSSGGQCLYSACPIFTKIQGTCYGGK AKCCK DEFB1-like Hylobates 68
MRTSYLLLFTLCLLLSEMASGDNFLTGLGHR protein concolor
SDHYNCVRSGGQCLYSACPIYTKIQGTCYQG KAKCCK DEEBI-like Pan 68
MRTSYLLLFTLCLLLSEMASGGNFLTGLGHR protein troglodytes
SDHYNCVSSGGQCLYSACPIFTKIQGTCYGG KAKCCK DEFB1-like Presbytis 68
MRTSYLLLFTLCLLMSEMASGDNFLTGLGHR protein obscura
SDHYNCVRSGGQCLYSACPIYTKIQGTCYHG KAKCCK DEFB1-like Saguinus 68
MRTSYLLLFILCLVLCDMDSGDTFLTGLGHRS protein oedipus
DHYNCVKGGGQCLYSACPIYTKVQGTCYGG KAKCCK DEFB36 Mus 43
MKLLLLTLAALLLVSQLTPGDAQKCWNLHGK (Fragment) musculus CRHRCSRKESVY
Defensin Aeshna 38 GFGCPLDQMQCHRHCQTITGRSGGYCSGPL cyanea KLTCTCYR
Defensin Allomyrina 43 VTCDLLSFEAKGFAANHSLCAAHCLAIGRRG dichotoma
GSCERGVCICRR Defensin Anopheles 102
MKCATIVCTIAVVLAATLLNGSVQAAPQEEAA gambiae
LSGGANLNTLLDELPEETHHAALENYRAKRA TCDLASGFGVGNNLCAAHCIARRYRGGYCN
SKAVCVCRN defensin Anopheles 131 NSRVNGATPAKLKLVLLCLPRASSSPQLIMKC
gambiae ATIVCTIAWLAATLLNGSVQAAPQEEAALSG
GANLNTLLDELPEETHHAALENYRAKRATCD LASGFGVGSSLCAAHCIARRYRGGYCNSKAV
CVCRN Defensin Bombus 51 VTCDLLSIKGVAEHSACAANCLSMGKAGGRC pascuorum
ENGICLCRKTTFKELWDKRF Defensin Branchiostoma 117
MEKKTAYCLLFLVLLVPYTALGAVLKRAPAKK beicheri
EKRAVPLAVPLVYWGASVSPAVWNWLLVTF GAAAVAAAAVTVSDNDSHSCANNRGWCRS
RCFSHEYIDSWHSDVCGSYDCCRPRY Defensin Drosophila 92
MKFFVLVAIAFALLACMAQAQPVSDVDPIPED melanogaster
HVLVHEDAHQEVLQHSRQKRATCDLLSKWN WNHTACAGHCIAKGFKGGYCNDKAVCVCRN
Defensin Drosophila 92 MKFFVLVAIAFALLACMAQAQPVSDVDPIPED
melanogaster HVLVHEDANQEVLQHSRQKRATCDLLSKWN
WNHTACAGHCIAKGFKGGYCNDKAVCVCRN Defensin Drosophila 92
MKFFVLVAIAFALLTCMAQAQPVSDVDPIPED melanogaster
HVLVHEDAHQEVLQHSRQKRATCDLLSKWN WNHTACAGHCIAKGFKGGYCNDKAVCVCRN
Defensin Drosophila 92 MKFFVPVAIAFALLACVAQAQPVSDVDPIPED
melanogaster HVLVHDDAHQEVLQHSRQKRATCDLLSKWN
WNHTACAGHCIAKGFKGGYCNDKAVCVCRN Defensin Drosophila 92
MKFFVLVAIAFALLACMAQAQPVSDVDPIPED simulans
HALVHEDAHQEWQHSRQKRATCDLLSKWN WNHTACAGHCIAKGFKGGYCNDKAVCVCRN
Defensin Mamestra 98 MLCLADIRIVASCSAAIKSGYGQQPWLAHVA brassicae
GPYANSLFDDVPADSYHAAVEYLRLIPASCYL
LDGYAAGRDDGRAHCIAPRNRRLYCASYQV CVCRY Defensin Musca 92
MKYFTMFAFFFVAVCYISQSSASPAPKEEAN domestica
FVHGADALKQLEPELHGRYKRATCDLLSGTG VGHSACAAHCLLRGNRGGYCNGKGVCVCR N
Defensin Ornithodoros 73 MNKLFIVALVLALAVATMAHEVHDDIEEPSVP moubata
RVRRGFGCPFNQYECHAHCSGVPGYKGGY CKGLFKQTCNCY Defensin Ornithodoros 73
MNKLFIVALVLALAVATMAHEVYDDVEEPSVP moubata
RVRRGYGCPFNQYQCHSHCSGIRGYKGGY CKGLFKQTCNCY Defensin Palomena 43
ATCDALSFSSKWLTVNHSACAIHCLTKGYKG prasina GRCVNTICNCRN Defensin
Phlebotomus 40 ATCDLLSAFGVGHAACAAHCIGHGYRGGYC duboscqi NSKAVCTCRR
Defensin Pyrocoelia 55 MKLSVFVLVAVMLVLLCCAMQTEARRRCRS rufa
CVPFCGSNERMISTCFSGGVVCCPR Defensin Pyrrhocoris 43
ATCDILSFQSQWVTPNHAGCALHCVIKGYKG apterus GQCKITVCHCRR Defensin Aedes
57 DELPEETYQAAVENYRRKRATCDLLSGFGVG (Fragment) albopictus
DSACAAHCIARRNRGGYCNAKTVCVC Defensin Apis mellifera 57
FEPLEHFENEERADRHRRVTCDLLSFKGQVN (Fragment)
DSACAANCHSLGKAGGHCEKGVCICR Defensin 1 Stomoxys 39
ATCDLLSGMGVNHSACAAHCVLRGNRGGYC (Fragment) calcitrans NSKAVCVCR
Defensin 1 Acalolepta 83 MKFFITFTFVLSLWLTVYSAPREFAEPEEQD precursor
luxuriosa EGHFRVKRFTCDVLSVEAKGVKLNHAACGIH CLFRRRTGGYCNKKRVCICR
Defensin 1 Stomoxys 79 MKFLNVVAIALLVVACLAVYSNAAPHEGVKEV precursor
calcitrans AAAKPMGITCDLLSLWKVGHAACAAHCLVLG DVGGYCTKEGLCVCKE
Defensin 1A Stomoxys 79 MKFLNVVAIALLVVACLSVYSNAAPHEGVKEV precursor
calcitrans AAAKPMGITCDLLSLWKVGHAACAAHCLVLG NVGGYCTKEGLCVCKE
Defensin 2 Stomoxys 97 MKFFSLFPVIVVVVACLTMRANAAPSAGNEV precursor
calcitrans DHHPDYVDGVEALRQLEPELHGRYKRATCD
LLSMWNVNHSACAAHCLLLGKSGGRCNDDA VCVCRK Defensin 2A Stomoxys 97
MKFFSLFPVILVVVACLTMRANAAPSAGDEV precursor calcitrans
DHHPDYVDGVEALRQLEPELHGRYKRATCD LLSMWNVNHSACAAHCLLLGKSGGRCNDDA
VCVCRK Defensin 5 Rattus 93 MKKLVLLSALVLLALQVEAEPTPKTDEGTKTD
precursor (RD- norvegicus EQPGKEDQWSVSIEGQGDPAFQDAVLRDL 5) (Enteric
KCFCRRKSCNWGEGIMGICKKRYGSPILCCR defensin Defensin A Aedes 98
MQSLTVICFLALCTGAITSAYPQEPVLADEAR aegypti
PFANSLFDELPEETYQAAVENFRLKRATCDLL SGFGVGDSACAAHCIARGNRGGYCNSKKVC
VCRN Defensin A Mytilus edulis 37 GFGCPNDYPCHRHCKSIPGRXGGYCGGXHR
LRCTCYR Defensin A Ornithodoros 73 MNKLFIVALVVALAVATMAQEVHNDVEEQSV
moubata PRVRRGYGCPFNQYQCHSHCSGIRGYKGGY CKGTFKQTCKCY Defensin A
Rhodnius 94 MKCILSLVTLFLVAVLVHSHPAEWNTHQQLD prolixus
DALWEPAGEVTEEHVARLKRATCDLFSFRSK WVTPNHAACAAHCLLRGNRGGRCKGTICHC RK
defensin A Aedes 37 MKSLTVICFLALCTGAITSAYPQEPVLADEAR isoform 2;
aegypti PFANS AaDefA2 defensin A Aedes 37
MQSLTVICFLALCTGAITSAYPQEPVLADEAR isoform 3; aegypti PFANS AaDefA3
defensin A Aedes 37 MQPLTVICFLALCTGAITSAYPQEPVLADEAR isoform 4;
aegypti PFANS AaDefA4 Defensin A Aedes 98
MKSITVICFLALCTVAITSAYPQEPVLADEARP precursor aegypti
FANSLFDELPEETYQAAVENFRLKRATCDLLS (AADEF)
GFGVGDSACAAHCIARGNRGGYCNSKKVCV CRN defensin A Aedes 98
MQSITVICFLALCTGAITSAYPQEPVLADEARP protein isoform aegypti
FANSLFDELPEETYQAAVENFRLKRATCDLLS 5 GFGVGDSACAAHCIARGNRGGYCNSKKVCV
CRN defensin alpha- Macaca 30 ACYCRIPACLAGERRYGTCFYLGRVWAFCC 1
mulatta defensin alpha- Macaca 30 ACYCRIPACLAGERRYGTCFYRRRVWAFCC 3
mulatta defensin alpha- Macaca 33 RRTCRCRFGRCFRRESYSGSCNINGRIFSLC 4
mulatta CR defensin alpha- Macaca 32
RTCRCRFGRCFRRESYSGSCNINGRIFSLCC 5 mulatta R defensin alpha- Macaca
33 RRTCRCRFGRCFRRESYSGSCNINGRISSLC 6 mulatta CR defensin alpha-
Macaca 32 RTCRCRFGRCFRRESYSGSCNINGRISSLCC 7 mulatta R Defensin B
Aedes 40 ATCDLLSGFGVGDSACAAHCIARGNRGGYC aegypti NSQKVCVCRN Defensin
B Ornithodoros 73 MNKLFIVALVVALAVATMAQEVHDDVEEQSV moubata
PRVRRGYGCPFNQYQCHSHCRGIRGYKGG YCTGRFKQTCKCY Defensin B Rhodnius 94
MKCILSLVTLFLVAVLVHSHPAEWNTQQELD prolixus
DALWEPAGEVTEEHVARLKRATCDLLSFSSK WVTPNHAGCAAHCLLRGNRGGHCKGTICHC RK
Defensin B Mytilus edulis 35 GFGCPNDYPCHRHCKSIPGRYGGYCGGXHR
(Fragment) LRCTC defensin beta Mus 67
MRLHYLLFVFLILFLVPAPGDAFLPKTLRKFFC 14; beta musculus
RIRGGRCAVLNCLGKEEQIGRCSNSGRKCC defensin 14 RKKK defensin beta Mus
81 MKTFLFLFAVLFFWSQPRMHFFFFDEKCSRI 34; beta musculus
NGRCTASCLKNEELVALCWKNLKCCVTVQS defensin 34 CGRSKGNQSDEGSGHMGTRG
defensin beta Mus 62 MKFSYFLLLLLSLSNFQNNPVAMLDTIACIENK 37; beta
musculus DTCRLKNCPRLHNVVGTCYEGKGKCCHKN defensin 37 defensin beta
Mus 63 MKISCFLLLILSLYFFQINQAIGPDTKKCVQRK 38; beta musculus
NACHYFECPWLYYSVGTCYKGKGKCCQKRY defensin 38 defensin beta Mus 73
MKISCFLLMIFFLSCFQINPVAVLDTIKCLQGN 40; beta musculus
NNCHIQKCPWFLLQVSTCYKGKGRCCQKRR defensin 40 WFARNHVYHV Defensin beta
Mus 64 MRIHYLLFAFLLVLLCPLASDFSKTINNPVSCC 5 musculus
MIGGICRYLCKGNILQNGNCGVTSLNCCKRK Defensin C Rhodnius 94
MKCILSLFTLFLVATLVYSYPAEWNSQHQLDD prolixus
AQWEPAGELTEEHLSRMKRATCDLLSLTSK WFTPNHAGCAAHCIFLGNRGGRCVGTVCHC RK
defensin C Zophobas 43 FTCDVLGFEIAGTKLNSAACGAHCLALGRTG atratus
GYCNSKSVCVCR Defensin C Aedes 99 MRTLIWCFVALCLSAIFTTGSALPGELADDV
precursor aegypti RPYANSLFDELPEESYQAAVENFRLKRATCD
LLSGFGVGDSACAAHCIARRNRGGYCNAKK VCVCRN Defensin D Aedes 96
VPTVICFLAMCLVAITGAYPQEPVLADEAQSV precursor albopictus
ANSLFDELPEESYQAAVENLRLKRATCDLLS (AALDEFD)
GFGVGDSACAAHCIARGNRGGYCNSKKVCV (Fragment) CPI Defensin Heliothis 44
DKLIGSCVWGAVNYTSDCNGECKRRGYKGG heliomicin virescens HCGSFANVNCWCET
Defensin Heliothis 44 DKLIGSCVWGAVNYTSDCNGECLLRGYKGG Heliomicin
virescens HCGSFANVNCWCET defensin Aedes 98
MKSITVICFLALCTGSITSAYPQDPVLADEARP isoform A1 aegypti
FANSLFDELPEETYQAAVENFRLKRATCDLLS GFGVGDSACAAHCIARGNRGGYCNSKKVCV CRN
defensin Aedes 98 MKSITVICFLALCTVAITSAYPQEPVLADEARP isoform B1
aegypti FANSLFDELPEETYQAAVENFRLKRATCDLLS
GFGVGDSACAAHCIARGNRGGYCNSQKVCV CRN defensin Aedes 98
MKSITVICFLALCTGSITSAYPQEPVLADEARP isoform B2 aegypti
FANSLFDELPEETYQAAVENFRLKRATCDLLS GFGVGDSACAAHCIARGNRGGYCNSQKVCV CRN
defensin Aedes 99 MRTLIVVCFVALCLSAIFTTGSALPEELADDVR isoform C1
aegypti SYANSLFDELPEESYQAAVENFRLKRATCDL
LSGFGVGDSACAAHCIARRNRGGYCNAKKV CVCRN Defensin Mgd- Mytilus 39
GFGCPNNYQCHRHCKSIPGRCGGYCGGWH 1 galloprovincialis RLRCTCYRCG
Defensin MGD- Mytilus 38 GFGCPNNYQCHRHCKSIPGRCGGYCGGXH 1
galloprovincialis RLRCTCYRC Defensin MGD- Mytilus 81
MKAAFVLLWGLCIMTDVATAGFGCPNNYAC 2 precursor galloprovincialis
HQHCKSIRGYCGGYCAGWFRLRCTCYRCG GRRDDVEDIFDIYDNVAVERF defensin NP-1
Rattus 32 VTCYCRRTRCGFRERLSGACGYRGRIYRLC norvegicus CR defensin
NP-4 Rattus 31 ACYCRIGACVSGERLTGACGLNGRIYRLCCR norvegicus Defensin
Anopheles 102 MKCATIVCTIAVVLAATLLNGSVQAAPQEEAA precursor gambiae
LSGGANLNTLLDELPEETHHAALENYRAKRA TCDLASGFGVGSSLCAAHCIARRYRGGYCN
SKAVCVCRN Defensin Drosophila 92 MKFFVLVAIAFALLACVAQAQPVSDVDPIPED
precursor melanogaster HVLVHEDAHQEVLQHSRQKRATCDLLSKWN
WNHTACAGHCIAKGFKGGYCNDKAVCVCRN Defensin Oryctes 79
MSRFIVFAFIVAMCIAHSLAAPAPEALEASVIR precursor rhinoceros
QKRLTCDLLSFEAKGFAANHSLCAAHCLAIG RKGGACQNGVCVCRR defensin Spodoptera
102 MGVKVINVFLLIAVSACLIHAVAGKPNPRDSS precursor frugiperda
VVEEQSLGPIHNEDLEVKVKPETTTTPEPRIP GRVSCDFEEANEDAVCQEHCLPKGYTYGICV
SHTCSCI Defensin Culex pipiens 40 ATCDLLSGFGVNDSACAAHCILRGNRGGYC
precursor NGKKVCVCRN (Fragment) defensin R-2 Rattus 31
VTCSCRTSSCRFGERLSGACRLNGRIYRLCC norvegicus defensin R-5 Rattus 32
VTCYCRSTRCGFRERLSGACGYRGRIYRLC norvegicus CR defensin Mus 92
MKKLVLLSAFVLLAFQVQADSIQNTDEEIKTE related musculus
EQPGEENQAVSISFGDPEGYALQDAAAIRRA cryptdin,
RRCPPCPSCLSCPWCPRCLRCPMCKCNPK related
sequence 12 defensin Mus 92 MKKLVLLFALVLLAFQVQADSIQNTDEETKTE
related musculus EQQGEEDQAVSVSFGDPQGSGLQDAAALG cryptdin,
WGRRCPRCPPCPRCSWCPRCPTCPRCNCN related PK sequence 7 Defensin Mus 60
MRIHYLLFTFLLVLLSPLAAFSQKINDPVTYIR related peptide musculus
NGGICQYRCIGLRHKIGTCGSPFKCCK Defensin, Zophobas 43
FTCDVLGFEIAGTKLNSAACGAHCLALGRRG isoforms B and atratus GYCNSKSVCVCR
C defensin-3 Macaca 96 MRTLVILAAILLVALQAQAEPLQARTDEATAA mulatta
QEQIPTDNPEVVVSLAWDESLAPKDSVPGLR KNMACYCRIPACLAGERRYGTCFYRRRVWA FCC
defensin-8 Macaca 96 MRTLVILAAILLVALQAQAEPLQARTDEATAA mulatta
QEQIPTDNPEVWSLAWDESLAPKDSVPGLR KNMACYCRIPACLAGERRYGTCFYLRRVWA FCC
defensin-like Mus 5 ICSPK gene 1C-1 musculus Defensin-like
Ornithorhynchus 42 FVQHRPRDCESINGVCRHKDTVNCREIFLAD peptide 1
anatinus CYNDGQKCCRK (DLP-1) Defensin-like Ornithorhynchus 42
IMFFEMQACWSHSGVCRDKSERNCKPMAW peptide 2/4 anatinus TYCENRNQKCCEY
(DLP-2/DLP-4) Defensin-like Ornithorhynchus 38
FEMQYCWSHSGVCRDKSERNNKPMAWTYC peptide 3 anatinus ENRQKKCEF (DLP-3)
Defensin-like Mesobuthus 61 MTYAILIIVSLLPISDGISNVVDKYCSENPLDCN
protein TXKS2 martensii EHCLKTKNQIGICHGANGNEKCSCMES Demidefensin 2
Macaca 76 MRTFALLTAMLLLVALHAQAEARQARADEAA mulatta
AQQQPGADDQGMAHSFTWPENAALPLSESA KGLRCICTRGFCRLL Demidefensin 3
Macaca 76 MRTLALHTAMLLLVALHAQAEARQARADEAA mulatta
AQQQPGADDQGMAHSFTWPENAALPLSESE RGLRCICVLGICRLL Dermaseptin 1
Phyllomedusa 34 ALWKTMLKKLGTMALHAGKAALGAAADTISQ (DS I) sauvagei GTQ
Dermaseptin BI Phyllomedusa 78 MDILKKSLFLVLFLGLVSLSICEEEKRENEDEE
precursor bicolor KQDDEQSEMKRAMWKDVLKKIGTVALHAGK (Dermaseptin
AALGAVADTISQGEQ B1) Dermaseptin Phyllomedusa 77
MAFLKKSLFLVLFLGLVSLSVCEEEKRENEDE DRG3 bicolor
EEQEDDEQSEEKRALWKTIIKGAGKMIGSLA precursor KNLLGSQAQPESEQ
(Dermaseptin 3) Dermatoxin Phyllomedusa 77
MAFLKKSLFLVLFLGLVPLSLCESEKREGENE precursor bicolor
EEQEDDQSEEKRSLGSFLKGVGTTLASVGKV VSDQFGKLLQAGQG Diptericin A
Protophormia 82 DEKPKLILPTPAPPNLPQLVGGGGGNRKDGF terraenovae
GVSVDAHQKVWTSDNGGHSIGVSPGYSQHL PGPYGNSRPDYRIGAGYSYNF diptericin B
Protophormia 41 DEKPKLVLPSXAPPNLPQLVGGGGGNNKXG terraenovae
XXVSINAAQKV diptericin C Protophormia 39
DEKPKLIXPXXAPXNLXQLVGGGGGNNKKXX terraenovae GVXVXXAQ Diptericin D
Protophormia 101 MKLFYLLVICALSLAVMADEKPKLILPTPAPPN precursor
terraenovae LPQLVGGGGGNRKDGFGVSVDAHQKVWTS
DNGRHSIGVTPGYSQHLGGPYGNSRPDYRI GAGYSYNFG Dolabellanin Dolabella 33
SHQDCYEALHKCMASHSKPFSCSMKFHMCL B2 auricularia QQQ Drosocin
Drosophila 64 MKFTIVFLLLACVFAMAVATPGKPRPYSPRPT melanogaster
SHPRPIRVRREALAIEDHLTQAAIRPPPILPA Drosocin Drosophila 64
MKFTIVFLLLACVFAMAVATPGKPRPYSPRPT melanogaster
SHPRPIRVRREALAIEDHLTQAAIRPPPILPV Drosocin Drosophila 64
MKFTIVFLLLACVFAMGVATPGKPRPYSPRPT CG10816-PA melanogaster
SHPRPIRVRREALAIEDHLTQAAIRPPPILPA Drosocin Drosophila 64
MKFTIVFLLLACVFAMAVATPGKPRPYSPRPT precursor melanogaster
SHPRPIRVRREALAIEDHLAQAAIRPPPILPA Drosomycin Drosophila 44
DCLSGRYKGPCAVWDNETCRRVCKEEGRS melanogaster SGHCSPSLKCWCEGC
Drosomycin Drosophila 70 MMQIKYLFALFAVLMLVVLGANEADADCLSG precursor
melanogaster RYKGPCAVWDNETCRRVCKEEGRSSGHCS (Cysteine-rich
PSLKCWCEGC peptide) enbocin Bombyx mori 59
MNFTRIIFFLGVVVFATASGKPWNIFKEIERAV ARTRDAVISAGPAVATVAAATSVASG
Enhancer of Sus scrofa 32 RADTQTYQPYNKDWIKEKIYVLLRRQAQQAG
rudimentary K homolog [Contains: Antibacterial peptide 3910]
(Fragment) entenic beta Bubalus 64 MRLHHLLLALLFLVLSAGSGFTQGVRNPQSC
defensin bubalis HRNKGICVPIRCPGNMRQIGTCLGPPVKCCR preproprotein RK
Enteric beta- Bos taurus 64 MRLHHLLLTLLFLVLSAGSGFTQGISNPLSCR
defensin LNRGICVPIRCPGNLRQIGTCFTPSVKCCRW precursor R Eosinophil
Cavia 233 MKLLLLLALLLGAVSTRHLKVDTSSLQSLRGE granule major porcellus
ESLAQDGETAEGATREATAGALMPLPEEEE basic protein 1
MEGASGSEDDPEEEEEEEEEVEFSSELDVS precursor
PEDIQCPKEEDTVKFFSRPGYKTRGYVMVGS (MBP-1)
ARTFNEAQWVCQRCYRGNLASIHSFAFNYQ VQCTSAGLNVAQVWIGGQLRGKGRCRRFV
WVDRTVWNFAYWARGQPWGGRQRGRCVT LCARGGHWRRSHCGKRRPFVCTY EP2e (ANTI-
Mus 69 MKVLLLFAVFFCFVQGNSGDIPPGIRNTVCLM microbial-like musculus
QQGHCRLFMCRSGERKGDICSDPWNRCCV protein BIN-1B PYSVKDRR homolog)
Esculentin-1 Rana 46 GIFSKLGRKKIKNLLISGLKNVGKEVGMDVVR esculenta
TGIDIAGCKIKGEC Esculentin-1A Rana 46
GIFSKLAGKKIKNLLISGLKNVGKEVGMDVVR esculenta TGIDIAGCKIKGEC
Esculentin-1B Rana 84 MFTLKKPLLLIVLLGMISLSLCEQERNADEEE precursor
esculenta GSEIKRGIFSKLAGKKLKNLLISGLKNVGKEV GMDVVRTGIDIAGCKIKGEC
Esculentin-2A Rana 37 GILSLVKGVAKLAGKGLAKEGGKFGLELIACKI esculenta
AKQC Esculentin-2B Rana 37 GLFSILRGAAKFASKGLGKDLTKLGVDLVACK
berlandieri ISKQC Esculentin-2B Rana 37
GIFSLVKGAAKLAGKGLAKEGGKFGLELIACKI esculenta AKQC Esculentin-2L Rana
37 GILSLFTGGIKALGKTLFKMAGKAGAEHLACK luteiventris ATNQC
Esculentin-2P Rana pipiens 37 GFSSIFRGVAKFASKGLGKDLARLGVNLVAC
KISKQC Formaecin 1 Myrmecia 16 GRPNPVNNKPTPHPRL gulosa Formaecin 2
Myrmecia 16 GRPNPVNTKPTPYPRL gulosa Gaegurin-1 Rana rugosa 33
SLESLIKAGAKFLGKNLLKQGACYAACKASKQ C Gaegurin-2 Rana rugosa 33
GIMSIVKDVAKNAAKEAAKGALSTLSCKLAKT C Gaegurin-3 Rana rugosa 33
GIMSIVKDVAKTAAKEAAKGALSTLSCKLAKT C Gaegurin-4 Rana rugosa 80
MFTMKKSLLFLFFLGTISLSLCEEERSADEDD precursor
GGEMTEEEVKRGILDTLKQFAKGVGKDLVKG AAQGVLSTVSCKLAKTC Gaegurin-5 Rana
rugosa 65 MFTLKKSLLLLFFLGTISLSLCEEERNADEEEK precursor
RDVEVEKRFLGALFKVASKVLPSVFCAITKKC Gaegurin-6 Rana rugosa 24
FLPLLAGLAANFLPTIICKISYKC Gal-1 alpha Gallus gallus 65
MRIVYLLLPFILLLAQGAAGSSQALGRKSDCF RKNGFCAFLKCPYLTLISGKCSRFHLCCKRIW G
gallinacin Gallus gallus 39 GRKSDCFRKSGFCAFLKCPSLTLISGKCSRF
YLCCKRIW gallinacin Gallus gallus 36
LFCKGGSCHFGGCPSHLIKVGSCFGFRSCCK WPWNA Gallinacin 1 Gallus gallus 39
GRKSDCFRKNGFCAFLKCPYLTLISGKCSRF alpha HLCCKRIW Gallinacin 1 Gallus
gallus 65 MRIVYLLLPFILLLAQGAAGSSQALGRKSDCF precursor
RKSGFCAFLKCPSLTLISGKCSRFYLCCKRIW G Gallinacin 2 Gallus gallus 64
MRILYLLFSLLFLALQVSPGLSSPRRDMLFCK precursor
GGSCHFGGCPSHLIKVGSCFGFRSCCKWPW NA Gastric Sus scrofa 42
YAEGTFISDYSIAMDKIRQQDFVNWLLAQKG inhibitory KKSDWKHNITQ polypeptide
(GIP) (Glucose- dependent insulinotropic polypeptide) Gloverin
Hyalophora 130 DVTWDKNIGNGKVFGTLGQNDDGLFGKAGF cecropia
KQQFFNDDRGKFEGQAYGTRVLGPAGGTTN FGGRLDWSDKNANAALDISKQIGGRPNLSAS
GAGVWDFDKNTRLSAGGSLSTMGRGKPDV GVHAQFQHDF Gomesin Acanthoscurria 18
QCRRLCYKQRCVTYCRGR gomesiana GP- Cavia 31
RRCICTTRTCRFPYRRLGTCLFQNRVYTFCC CS2 = CORTIC OSTATIC peptide
(Fragment) Hadrurin Hadrurus 41 GILDTIKSIASKVWNSKTVQDLKRKGINWVAN
aztecus KLGVSPQAA Hemiptericin Pyrrhocoris 133
DVELKGKGGENEGFVGLKAQRNLYEDDRTS apterus
LSGTVKGQSQWKDPYPAQHAGMARLDGTR TLIENDRTKVTGSGFAQREVATGMRPHDSFG
VGVEATHNIYKGKNGEVDVFGGVQRQWNTP DRHQARGGIRWRF Hepcidin Mus 83
MALSTRTQAACLLLLLLASLSSTTYLQQQMR antimicrobial musculus
QTTELQPLHGEESRADIAIPMQKRRKRDINFP peptide 2 ICRFCCQCCNKPSCGICCEE
hepcidin Danio rerio 91 MKLSNVFLAAVVILTCVCVFQITAVPFIQQVQ
antimicrobial DEHHVESEELQENQHLTEAEHRLTDPLVLFR peptide
TKRQSHLSLCRFCCKCCRNKGCGYCCKF precursor
Hepcidin Morone 85 MKTFSVAVAVAVVLAFICLQESSAVPVTEVQE precursor
chrysops x LEEPMSNEYQEMPVESWKMPYNNRHKRHS Morone
SPGGCRFCCNCCPNMSGCGVCCRF saxatilis Hepcidin Mus 83
MALSTRTQAACLLLLLLASLSSTTYLHQQMR precursor musculus
QTTELQPLHGEESRADIAIPMQKRRKRDTNF PICIFCCKCCNNSQCGICCKT Hepcidin
Rattus 84 MALSTRIQAACLLLLLLASLSSGAYLRQQTRQ precursor norvegicus
TTALQPWHGAESKTDDSALLMLKRRKRDTN FPICLFCCKCCKNSSCGLCCIT Hepcidin
Oncorhynchus 61 LQVLTEEVGSIDSPVGEHQQPGGESMRLPE precursor mykiss
HFRFKRXSHLSLCRWCCNCCHNKGXGFCCK (Fragment) F Histone H2A Bufo 39
AGRGKQGGKVRAKAKTRSSRAGLQFPVGRV [Contains: gargarizans HRLLRKGNY
Buforin I; Buforin II] (Fragment) Histone H2A Hippoglossus 51
SGRGKTGGKARAKAKTRSSRAGLQFPVGRV [Contains: hippoglossus
HRLLRKGNYAHRVGAGAPVYL Hipposin] (Fragment) Histone H2B-1 Ictalurus
20 PDPAKTAPKKGSKKAVTKXA (Antibacterial punctatus histone-like
protein 1) (HLP-1) (Fragment) Histone H2B-3 Ictalurus 17
PDPAKTAPKKKSKKAVT (Antibacterial punctatus histone-like protein 3)
(HLP-3) (Fragment) holotricin 1 Holotrichia 43
VTCDLLSLQIKGIAINDSACAAHCLAMRRKGG diomphalia SCKQGVCVCRN Holotricin
2 Holotrichia 127 MMKLVIALCLIGISAAYVVPVYYEIYPEDATFD precursor
diomphalia EADIEPQLSPAELHHGSIRERRSLQPGAPSFP
MPGSQLPTSVSGNVEKQGRNTIATIDAQHKT DRYDVRGTWTKVVDGPGRSKPNFRIGGSYR W
holotricin 2 Holotrichia 127 MMKLVIALCLIGISAAYVVPVYYEIYPEDATFD
precursor diomphalia EADIEPQLSPAELHHGSIRERRSLQPGAPSLS
QLPTSVSGNVEKQGRPMPGNTIATIDAQHKT DRYDVRGTVDGPGRSKPNFRIGGSWTKVYR W
Holotricin 3 Holotrichia 104 MNKLIILGLACIIAVASAMPYGPGDGHGGGHG
precursor diomphalia GGHGGGHGNGQGGGHGHGPGGGFGGGH
GGGHGGGGRGGGGSGGGGSPGHGAGGG YPGGHGGGHHGGYQTHGY Hymenoptaecin Apis
mellifera 129 MKFIVLVLFCAVAYVSAQAELEPEDTMDYIPT precursor
RFRRQERGSIVIQGTKEGKSRPSLDIDYKQR VYDKNGMTGDAYGGLNIRPGQPSRQHAGFE
FGKEYKNGFIKGQSEVQRGPGGRLSPYFGIN GGFRF Indolicidin Bos taurus 14
ILPWKWPWWPWRRX Indolicidin Bos taurus 144
MQTQRASLSLGRWSLWLLLLGLVVPSASAQ precursor
ALSYREAVLRAVDQLNELSSEANLYRLLELDP PPKDNEDLGTRKPVSFTVKETVCPRTIQQPA
EQCDFKEKGRVKQCVGTVTLDPSNDQFDLN CNELQSVILPWKWPWWPWRRG Insect
Defensin Protophormia 40 ATCDLLSGTGINHSACAAHCLLRGNRGGYCN A (NMR, 10
terraenovae GKGVCVCRN Structures) - Chai Interferon- Mus sp. 15
SETAPAETPAPAKAE activated antimicrobial protein (Fragment)
Japonicin-1 Rana 14 FFPIGVFCKIFKTC japonica Japonicin-2 Rana 21
FGLPMLSILPKALCILLKRKC japonica Lactoferricin Bos taurus 25
FKCRRWQWRMKKLGAPSITCVRRAF lactoferrin Sus scrofa 703
MKLFIPALLFLGTLGLCLAAPKKGVRWCVIST precursor
AEYSKCRQWQSKIRRTNPMFCIRRASPTDCI RAIAAKRADAVTLDGGLVFEADQYKLRPVAA
EIYGTEENPQTYYYAVAWKKGFNFQNQLQG RKSCHTGLGRSAGWNIPIGLLRRFLDWAGPP
EPLQKAVAKFFSQSCVPCADGNAYPNLCQL CIGKGKDKCACSSQEPYFGYSGAFNCLHKGI
GDVAFVKESTVFENLPQKADRDKYELLCPDN TRKPVEAFRECHLARVPSHAWARSVNGKE
NSIWELLYQSQKKFGKSNPQEFQLFGSPGQ QKDLLFRDATIGFLKIPSKIDSKLYLGLPYLTAI
QGLRETAAEVEARQAKVVWCAVGPEELRKC RQWSSQSSQNLNCSLASTTEDCIVQVLKGEA
DAMSLDGGFIYTAGKCGLVPVLAENQKSRQS SSSDCVHRPTQGYFAVAWRKANGGITWNS
VRGTKSCHTAVDRTAGWNIPMGLLVNQTGS CKFDEFFSQSCAPGSQPGSNLCALCVGNDQ
GVDKCVPNSNERYYGYTGAFRCLAENAGDV AFVKDVTVLDNTNGQNTEEWARELRSDDFE
LLCLDGTRKPVTEAQNCHLAVAPSHAWSRK EKAAQVEQVLLTEQAQFGRYGKDCPDKFCL
FRSETKNLLFNDNTECLAQLQGKTTYEKYLG SEYVTAIANLKQCSVSPLLEACAFMMR
Lactotransferrin Bos taurus 708 MKLFVPALLSLGALGLCLAAPRKNVRWCTIS
precursor QPEWFKCRRWQWRMKKLGAPSITCVRRAF (Lactoferrin)
ALECIRAIAEKKADAVTLDGGMVFEAGRDPY [Contains:
KLRPVAAEIYGTKESPQTHYYAVAVVKKGSN Lactoferricin B
FQLDQLQGRKSCHTGLGRSAGWIIPMGILRP (LFCIN B)]
YLSWTESLEPLQGAVAKFFSASCVPCIDRQA YPNLCQLCKGEGENQCACSSREPYFGYSGA
FKCLQDGAGDVAFVKETTVFENLPEKADRDQ YELLCLNNSRAPVDAFKECHLAQVPSHAWA
RSVDGKEDLIWKLLSKAQEKFGKNKSRSFQL FGSPPGQRDLLFKDSALGFLRIPSKVDSALYL
GSRYLTTLKNLRETAEEVKARYTRVVWCAVG PEEQKKCQQWSQQSGQNVTCATASTTDDCI
VLVLKGEADALNLDGGYIYTAGKCGLVPVLAE NRKSSKHSSLDCVLRPTEGYLAVAWKKANE
GLTWNSLKDKKSCHTAVDRTAGWNIPMGLIV NQTGSCAFDEFFSQSCAPGADPKSRLCALC
AGDDQGLDKCVPNSKEKYYGYTGAFRCLAE DVGDVAFVKNDTVWENTNGESTADWAKNLN
REDFRLLCLDGTRKPVTEAQSCHLAVAPNHA VVSRSDRAAHVKQVLLHQQALFGKNGKNCP
DKFCLFKSETKNLLFNDNTECLAKLGGRPTY EEYLGTEYVTAIANLKKCSTSPLLEACAFLTR
Lebocin 1/2 Bombyx mori 179 MYKFLVFSSVLVLFFAQASCQRFIQPTFRPPP
precursor TQRPIIRTARQAGQEPLWLYQGDNVPRAPST
ADHPILPSKIDDVQLDPNRRYVRSVTNPENN EASIEHSHHTVDTGLDQPIESHRNTRDLRFLY
PRGKLPVPTPPPFNPKPIYIDMGNRYRRHAS DDQEELRQYNEHFLIPRDIFQE Lebocin 3
Bombyx mori 179 MYKFLVFSSVLVLFFAQASCQRFIQPTFRPPP precursor (LEB
TQRPITRTVRQAGQEPLWLYQGDNVPRAPS 3) TADHPILPSKIDDVQLDPNRRYVRSVTNPENN
EASIEHSHHTVDIGLDQPIESHRNTRDLRFLY PRGKLPVPTLPPFNPKPIYIDMGNRYRRHAS
EDQEELRQYNEHFLIPRDIFQE lectin-L6 Limulus 221
VQWHQIPGKLMHITATPHFLWGVNSNQQIYL polyphemus
CRQPCYDGQWTQISGSLKQVDADDHEVWG VNRNDDIYKRPVDGSGSVVVRVSGKLKHVSA
SGYGYIWGVNSNDQIYKCPKPCNGAWTQVN GRLKQIDGGQSMVYGVNSANAIYRRPVDGS
GSWQQISGSLKHITGSGLSEVFGVNSNDQIY RCTKPCSGQWSLIDGRLKQCDATGNTIVGVN
SVDNIYRSG Limulus factor Tachypleus 394
MKVLLLVAFLLGTTLAYPQDDDGPVWGGSS D tridentatus
NDNDDGGISSRVGNPQSGFGNCECVPYYLC KDNNIIIDGSGLLDPRKKPVASKEPKLSARLG
PEGPSGCGPFHVCCIAPETSTVKPYTHQCGF RNVNGINKRILSPNGKDLSEFGEWPWQGAVL
KVEGKVNIFQCGAVLIDSYHLLTVAHCVYKFT LENAFPLKVRLGEWDTQNTNEFLKHEDYEVE
KIYIHPKYDDERKNLWDDIAILKLKAEVSFGPH IDTICLPNNQEHFAGVQCVVTGWGKNAYKNG
SYSNVLREVHVPVITNDRCQELLRKTRLSEW YVLYENFICAGGESNADSCKGDGGGPLTCW
RKDGTYGLAGLVSWGINCGSPNVPGVYVRV SNYLDWITKITGRPISDYWPRS Lingual Bos
taurus 64 MRLHHLLLALLFLVLSAGSGFTQGVRNSQSC antimicrobial
RRNKGICVPIRCPGSMRQIGTCLGAQVKCCR peptide RK precursor Liver- Bos
taurus 77 MWHLKLFAVLMICLLLLAQVDGSPIPQQSSAK expressed
RRPRRMTPFWRAVSLRPIGASCRDDSECITR antimicrobial LCRKRRCSLSVAQE
peptide 2 precursor (LEAP-2) Liver- Macaca 77
MWHLKLCAVLMIFLLLLGQTDGSPIPEVSSAK expressed mulatta
RRPRRMTPFWRGVSLRPIGASCRDDSECITR antimicrobial LCRKRRCSLSVAQE
peptide 2 precursor (LEAP-2) Liver- Mus 76
MLQLKLFAVLLTCLLLLGQVNSSPVPEVSSAK expressed musculus
RSRRMTPFWRGVSLRPIGASCRDDSECITRL antimicrobial CRKRRCSLSVAQE peptide
2 precursor (LEAP-2) Liver- Sus scrofa 77
MWHLKLFAVLVICLLLAVQVHGSPIPELSSAK expressed
RRPRRMTPFWRAVSLRPIGASCRDDSECLT antimicrobial RLCRKRRCSLSVAQE
peptide 2 precursor (LEAP-2) Liver- Cavia 71
SVVLLICLLLLGQVDGSPVPEKSSVKKRLRRM expressed porcellus
TPFWRGVSLRPIGASCRDDSECITRLCKKRR antimicrobial CSLSVAQE peptide 2
precursor (LEAP-2) (Fragment) Liver- Sus scrofa 77
MWHLKLFAVLVICLLLAVQVHGSPIPELSSAK expressed
RRPRRITPFWRAVSLRPIGASCRDDSECLTR antimicrobial LCRKRRCSLSVAQE
protein 2 Lysozyme Heliothis 141 MQKLTLFVVALAAVVLHCEAKQFSRCGLVQE
virescens LRRQGFPEDKLGDWVCLVENESARKTDKVG
TVNKNGSRDYGLYQINDKYWCSNTSTPGKD CNVTCAEMLLDDITKASTCAKKIYKRHKFEAW
YGWKNHCKGKTLPDISNC lysozyme (EC Alopochen 129
KVYGRCELAAAMKRLGLDNYRGYSLGNWVC 3.2.1.17) aegyptiacus
AAKYESGFNTQATNRNTDGSTDYGILQINSR WWCNDGKTPRAKNVCGIPCSVLLRSDITEAV
KCAKRIVSDGNGMNAWVAWRNRCKGTDVS QWIRGCRL lysozyme (EC Chrysolophus
129 KVYGRCELAAAMKRLGLDNYRGYSLGNWVC 3.2.1.17) pictus
AAKFESNFNTHATNRNTDGSTDYGILQINSR WWCNDGRTPGSRNLCHIPCSALLSSDITASV
NCAKKIVSDGNGMNAWVAWRNRCKGTDVN AWTRGCRL lysozyme (EC Lophophorus 129
KVYGRCELAAAMKRLGLDNYRGYSLGNWVC 3.2.1.17) impejanus
AAKFESNFNTHATNRNTDGSTDYGILQINSR WWCNDGRTPGSRNLCNIPCSALLSSDITASV
NCAKKIVSDGNGMNAVWAWRNRCKGTDVH AWIRGCRL
lysozyme (EC Manduca 120 KHFSRCELVHELRRQGFPENLMRDWVCLVE 3.2.1.17)
sexta NESSRYTDKVGRVNKNGSRDYGLFQINDKY
WCSNGSTPGKDCNVKCSDLLIDDITKASTCA KKIYKRHKFQAWYGWRNHCQGSLPDISSC
lysozyme (EC Ovis aries 129 KVFERCELARTLKELGLDGYKGVSLANWLCL
3.2.1.17) 1 TKWESSYNTKATNYNPGSESTDYGIFQINSK
WWCNDGKTPNAVDGCHVSCSELMENNIAKA VACAKHIVSEQGITAWVAWKSHCRDHDVSS
YVEGCSL lysozyme (EC Rattus 148 MKALLVLGFLLLSASVQAKIYERCEFARTLKR
3.2.1.17) 1 norvegicus NGMSGYYGVSLADWVCLAQHESNYNTQAR precursor
NYNPGDQSTDYGIFQINSRYWCNDGKTPRA KNACGIPCSALLQDDITQAIQCAKRVVRDPQ
GIRAWVAWQRHCKNRDLSGYIRNCGV lysozyme (EC Bos taurus 129
KTFKRCELARTLKNLGLAGYKGVSLANWMCL 3.2.1.17) 14d,
AKGESNYNTQAKNYNPGSKSTDYGIFQINSK tracheal
WWCNDGKTPKAVNGCGVSCSALLKDDITQA VACAKKIVSQQGITAWVAWKNKCRNRDLTSY
VKGCGV lysozyme (EC Cervus axis 129 KVFERCELARTLKELGLDGYKGVSLANWLCL
3.2.1.17) 2 TKWESSYNTKATNYNPGSESTDYGIFQINSK
WWCNDGKTPNAVDGCHVACSELMENDIAKA VACAKQIVREQGITAWVAWKSHCRDHDVSS
YVEGCTL lysozyme (EC Ovis aries 129 KVFERCELARTLKELGLDGYKGVSLANWLCL
3.2.1.17) 2 TKWESSYNTKATNYNPGSESTDYGIEQINSK
WWCNDGKTPNAVDGCHVSCSALMENDIEKA VACAKHIVSEQGITAWVAWKSHCRDHDVSS
YVEGCTL lysozyme (EC Ovis aries 129 KVFERCELARTLKKLGLDDYKGVSLANWLCL
3.2.1.17) 3 TKWESGYNTKATNYNPGSESTDYGIEQINSK
WWCNDGKTPNAVDGCHVSCSALMENDIEKA VACAKHIVSEQGITAWVAWKSHCRDHDVSS
YVEGCTL lysozyme (EC Bos taurus 130 KVFERCELARSLKRFGMDNFRGISLANWMCL
3.2.1.17) 5a, ARWESNYNTQATNYNAGDQSTDYGIEQINSH tracheal
WWCNDGKTPGAVNACHLPCGALLQDDITQA VACAKRWSDPQGIRAWVAWRSHCQNQDLT
SYIQGCGV lysozyme (EC Drosophila 140
MKAFIVLVALASGAPALGRTMDRCSLAREMS 3.2.1 .17) B melanogaster
NLGVPRDQLARWACIAEHESSYRTGVVGPE precursor
NYNGSNDYGIFQINDYYWCAPPSGRFSYNE CGLSCNALLTDDITHSVRCAQKVLSQQGWSA
WSTWHYCSGWLPSIDDCF lysozyme (EC Papio sp. 130
KIFERCELARTLKRLGLDGYRGISLANWVCLA 3.2.1.17) c
KWESDYNTQATNYNPGDQSTDYGIEQINSHY WCNDGKTPGAVNACHISCNALLQDNITDAVA
CAKRVVSDPQGIRAWVAWRNHCQNRDVSQ YVQGCGV lysozyme (EC Numida 129
KVFGRCELAAAMKRHGLDNYRGYSLGNWVC 3.2.1.17) c meleagris
AAKFESNFNSQATNRNTDGSTDYGVLQINSR [validated]
WWCNDGRTPGSRNLCNIPCSALQSSDITATA NCAKKIVSDGDGMNAWVAWRKHCKGTDVR
VWIKGCRL lysozyme (EC Coturnix 129 KVYGRCELAAAMKRHGLDKYQGYSLGNWV
3.2.1.17) C japonica CAAKFESNFNTQATNRNTDGSTDYGILQINS precursor
RWWCNDGRTPGSRNLCNIPCSALLSSDITAS VNCAKKIVSDVHGMNAWVAWRNRCKGTDV
NVWIRGCRL lysozyme (EC Hyalophora 132
CRSWQFALHCDAKRFTRCGLVQELRRRGFD 3.2.1.17) c cecropia
ETLMSNWVCLVENESGRFTDKIGKVNKNGS precursor
RDYGLFQINDKYWCSKGSTPGKDCNVTCNQ LLTDDISVAATCAKKIYKRHKFDAWYGWKNH
CQHGLPDISDC lysozyme (EC Phasianus 147
MRSLLILVLCFLPLAAPGKVYGRCELAAAMKR 3.2.1.17) c colchicus
MGLDNYRGYSLGNVWCAAKFESNFNTGATN precursor
RNTDGSTDYGILQINSRWWCNDGRTPGSKN [validated]
LCHIPCSALLSSDITASVNCAKKIVSDGDGMN AWVAWRKHCKGTDVNVWIRGCRL lysozyme
(EC Drosophila 140 MKAFIVLVALALAAPALGRTLDRCSLAREMSN 3.2.1.17) E
melanogaster LGVPRDQLARWACIAEHESSYRTGWGPEN precursor
YNGSNDYGIFQINDYYWCAPPSGRFSYNEC GLSCNALLTDDITHSVRCAQKVLSQQGWSA
WSTWHYCSGWLPSIDDCF lysozyme (EC Rhea 185
RTNCYGDVSRIDTTGASCKTAKPEKLNYCGV 3.2.1.17) g americana
AASRKIAERDLRSMDRYKTLIKKVGQKLCVEP AVIAGIISRESHAGKALKNGWGDNGNGFGLM
QVDRRSHKPVGEWNGERHLIQGTEILISMIKA MQRKFPRWTKEQQLKGGISAYNAGPGNVRT
YERMDIGTTHDDYANDVVARAQYYKQHGY lysozyme (EC Casuarius 185
QTGCYGWNRIDTTGASCETAKPEKLNYCGV 3.2.1.17) g casuarius
AASRKIAEGDLQSMDRYKTLIKKVGQKLCVD [validated]
PAVIAGIISRESHAGKALKDGWGDNGNGFGL MQVDKRSHTPVGKWNGERHLTQGTEILISMI
KKIQKKFPRWTKEQQLKGGISAYNAGSGNVR TYERMDIGTTHNDYANDVVARAQYYKQHGY
lysozyme (EC Drosophila 140 MKAFIVLVALACAAPAFGRTMDRCSLAREMS
3.2.1.17) melanogaster NLGVPRDQLNKWACIAEHESSYRTGVVGPE precursor
NYNGSNDYGIFQINDYYWCAPPSGRFSYNE CGLSCNALLTDDITHSVRCAQKVLSQQGWSA
WSTWHYCSGWLPSIDDCF lysozyme (EC Opisthocomus 145
MLFFGFLLAFLSAVPGTEGEIISRCELVKILRE 3.2.1.17) hoazin
HGFEGFEGTTIADWICLVQHESDYNTEAYNN precursor,
NGPSRDYGIFQINSKYWCNDGKTSGAVDGC stomach
HISCSELMTNDLEDDIKCAKKIARDAHGLTPW YGWKNHCEGRDLSSYVKGC lysozyme (EC
Drosophila 139 MKAFFALVLLPLPLCLAGRTLDRCSLAREMA 3.2.1.17) S
melanogaster DLGVPRDQLDKWTCIAQHESDYRTWVVGPA precursor
NSDGSNDYGIFQINDLYWCQADGRFSYNEC GLSCNALLTDDITNSVRCAQKVLSQQGWSA
WAVWHYCSGWLPSIDECF lysozyme (EC Drosophila 81
PNTDGSNDYGIFQINDLYWCQPSSGKFSHN 3.2.1.17) X melanogaster
GCDVSCNALLTDDIKSSVRCALKVLGQQGW SAWSTWHYCSGYLPPIDDCFV Lysozyme
Drosophila 140 MKAFIVLVALACAAPAFGRTMDRCSLAREMS A/C/D melanogaster
NLGVPRDQLARWACIAEHESSYRTGVVGPE precursor (EC
NYNGSNDYGIFQINDYYWCAPPSGRFSYNE 3.2.1.17) (1,4-
CGLSCNALLTDDITHSVRCAQKVLSQQGWSA beta-N- WSTWHYCSGWLPSIDDCF
acetylmurami- dase A/C) Lysozyme C Callipepla 129
KVFGRCELAAAMKRHGLDNYRGYSLGNWVC (EC 3.2.1.17) californica
AAKFESNFNSQATNRNTDGSTDYGVLQINSR (1,4-beta-N-
WWCNDGRTPGSRNLCNIPCSALLSSDITATV acetylmurami-
NCAKKIVSDGNGMNAWVAWRNRCKGTDVH dase C) AWIRGCRL Lysozyme C Colinus
130 MKVFGRCELAAAMKRHGLDNYRGYSLGNW (EC 3.2.1.17) virginianus
VCAAKFESNFNSQATNRNTDGSTDYGVLQIN (1,4-beta-N-
SRWWCNDGKTPGSRNLCNIPCSALLSSDITA acetylmurami-
TVNCAKKIVSDGNGMNAWVAWRNRCKGTD dase C) VQAWIRGCRL Lysozyme C Columba
livia 127 KDIPRCELVKILRRHGFEGFVGKTVANWVCL (EC 3.2.1.17)
VKHESGYRTTAFNNNGPNSRDYGIFQINSKY (1,4-beta-N-
WCNDGKTRGSKNACNINCSKLRDDNIADDIQ acetylmurami-
CAKKIAREARGLTPWVAWKKYCQGKDLSSY dase C) VRGC Lysozyme C Equus asinus
129 KVFSKCELAHKLKAQEMDGFGGYSLANWVC (EC 3.2.1.17)
MAEYESNFNTRAFNGKNANGSYDYGLFQLN (1,4-beta-N-
SKWWCKDNKRSSSNACNIMCSKLLDDNIDD acetylmurami-
DISCAKRVVRDPKGMSAWKAWVKHCKDKDL dase C) SEYLASCNL Lysozyme C Ortalis
vetula 129 KIYKRCELAAAMKRYGLDNYRGYSLGNWVC (EC 3.2.1.17)
AARYESNYNTQATNRNSNGSTDYGILQINSR (1,4-beta-N-
WWCNDGRTPGTKNLCHISCSALMGADIAPS acetylmurami-
VRCAKRIVSDGDGMNAWVAWRKHCKGTDV dase C) STWIKDCKL Lysozyme C
Oryctolagus 130 KIYERCELARTLKKLGLDGYKGVSLANWMCL (EC 3.2.1.17)
cuniculus AKWESSYNTRATNYNPGDKSTDYGIFQINSR (1,4-beta-N-
YWCNDGKTPRAVNACHIPCSDLLKDDITQAV acetylmurami-
ACAKRWSDPQGIRAWVAWRNHCQNQDLTP dase C) YIRGCGV Lysozyme C Syrmaticus
129 KVYGRCELAAAMKRLGLDNFRGYSLGNWVC (EC 3.2.1.17) soemmerringii
AAKFESNFNTHATNRNTDGSTDYGILQINSR (1,4-beta-N-
WWCNDGRTPGSRNLCNIPCSALLSSDTIASV acetylmurami-
NCAKKIVSDGNGMNAWVAWRKRCKGTDVN dase C) (CPL) AWTRGCRL Lysozyme C
Felis catus 20 KIFTKCELARKLRAEGMDGF (EC 3.2.1.17) (1,4-beta-N-
acetylmurami- dase C) (Fragment) Lysozyme C Pseudocheirus 49
SKMKKCEFAKIAKEQHMDGYHGVSLADWVC (EC 3.2.1.17) peregrinus
LVNNESDFNTKAINRNKGI (1,4-beta-N- acetylmurami- dase C) (Fragment)
Lysozyme C Lophura 129 KVYGRCELAAAMKRLGLDNYRGYSLGNWVNC (EC
3.2.1.17) leucomelanos AAKYESNFNTHATNRNTDGSTDYGILQINSR (1,4-beta-N-
WWCNDGKTPGSRNLCHIPCSALLSSDITASV acetylmurami-
NCAKKIVSDGNGMNAWVAWRNRCKGTDVS dase) VWTRGCRL Lysozyme C Pavo 129
KVYGRCELAAAMKRLGLDNYRGYSLGNWVC (EC 3.2.1.17) cristatus
AAKFESNFNTHATNRNTDGSTDYGILQINSR (1,4-beta-N-
WWCNDGRTPGSRNLCNIPCSALLSSDITASV acetylmurami-
NCAKKIVSDRNGMNAWVAWRNRCKGTDVH dase) AWIRGCRL Lysozyme C Phasianus
130 GKVYGRCELAAAMKRMGLDNYRGYSLGNW (EC 3.2.1.17) versicolor
VCAAKFESNFNTGATNRNTDGSTDYGILQIN (1,4-beta-N-
SRWWCNDGRTPGSKNLCHIPCSALLSSDITA acetylmurami-
SVNCAKKIVSDGDGMNAWVAWRKHCKGTD dase) VNVWIRGCRL Lysozyme C
Syrmaticus 129 KVYGRCELAAAMKRLGLDNYRGYSLGNWVC (EC 3.2.1.17) reevesi
AAKFESNFNTHATNRNTDGSTDYGILQINSR (1,4-beta-N-
WWCNDGRTPGSRNLCHISCSALLSSDITASV acetylmurami-
NCAKKIVSDRNGMNAWVAWRNRCKGTDVN dase) AWIRGCRL Lysozyme C 1 Cervus
axis 129 KVFERCELARTLKELGLDGYKGVSLANWLCL and 2 (EC
TKWESSYNTKATNYNPGSESTDYGIFQINSK 3.2.1.17) (1,4-
WWCDDGKTPNAVDGCHVACSELMENNIDKA beta-N-
VTCAKQIVREQGITAWVAWKSHCRGHDVSS acetylmurami- YVEGCTL dase C)
Lysozyme C 1 Bos taurus 147 MKALIILGFLFLSVAVQGKVFERCELARTLKKL
precursor (EC GLDGYKGVSLANWLCLTKWESSYNTKATNY 3.2.1.17) (1,4-
NPGSESTDYGIFQINSKWWCNDGKTPNAVD beta-N-
GCHVSCSELMENDIAKAVACAKQIVSEQGITA acetylmurami-
WVAWKSHCRDHDVSSYVEGCTL dase C) Lysozyme C 2 Bos taurus 147
MKALVILGFLFLSVAVQGKVFERCELARTLKK precursor (EC
LGLDGYKGVSLANWLCLTKWESSYNTKATN 3.2.1.17) (1,4-
YNPSSESTDYGIFQINSKWWCNDGKTPNAV beta-N-
DGCHVSCSELMENDIAKAVACAKHIVSEQGIT acetylmurami-
AWVAWKSHCRDHDVSSYVEGCTL dase C) Lysozyme C 3 Bos taurus 147
MKALIILGFLFLSVAVQGKVFERCELARTLKKL precursor (EC
GLDGYKGVSLANWLCLTKWESSYNTKATNY 3.2.1.17) (1,4-
NPSSESTDYGIFQINSKWWCNDGKTPNAVD beta-N-
GCHVSCSELMENDIAKAVACAKHIVSEQGITA acetylmurami-
WVAWKSHCRDHDVSSYVQGCTL dase C) Lysozyme C I Tachyglossus 125
KILKKQELCKNLVAQGMNGYQHITLPNWVCT (EC 3.2.1.17) aculeatus
AFHESSYNTRATNHNTDGSTDYGILQINSRY (1,4-beta-N-
WCHDGKTPGSKNACNISCSKLLDDDITDDLK acetylmurami-
CAKKIAGEAKGLTPWVAWKSKCRGHDLSKF dase C) KC Lysozyme C II
Oncorhynchus 144 MRAVVVLLLVAVASAKVYDRCELARALKASG precursor (EC
mykiss MDGYAGNSLPNWVCLSKWESSYNTQATNR 3.2.1.17) (1,4-
NTDGSTDYGIFQINSRYWCDDGRTPGAKNV beta-N-
CGIRCSQLLTADLTVAIRCAKRWLDPNGIGA
acetylmurami- WVAWRLHCQNQDLRSYVAGCGV dase C) Lysozyme C Coturnix
147 MRSLLVLVLCFLPLAALGKVYGRCELAAAMK precursor (EC japonica
RHGLDKYQGYSLGNWVCAAKFESNFNTQAT 3.2.1.17) (1,4-
NRNTDGSTDYGILQINSRWWCNDGRTPGSR beta-N-
NLCNIPCSALLSSDITASVNCAKKIVSDVHGM acetylmurami-
NAWVAWRNRCKGTDVNAWIRGCRL dase C) Lysozyme C Meleagris 147
MRSLLILVLCFLPLAALGKVYGRCELAAAMKR precursor (EC gallopavo
LGLDNYRGYSLGNWVCAAKFESNFNTHATN 3.2.1.17) (1,4-
RNTDGSTDYGILQINSRWWCNDGRTPGSKN beta-N-
LCNIPCSALLSSDITASVNCAKKIASGGNGMN acetylmurami-
AWVAWRNRCKGTDVHAWIRGCRL dase C) Lysozyme C Presbytis 148
MKALTILGLVLLSVTVQGKIFERCELARTLKKL precursor (EC entellus
GLDGYKGVSLANWVCLAKWESGYNTEATNY 3.2.1.17) (1,4-
NPGDESTDYGIFQINSRYWCNNGKTPGAVD beta-N-
ACHISCSALLQNNIADAVACAKRVVSDPQGIR acetylmurami-
AWVAWRNHCQNKDVSQYVKGCGV dase C) Lysozyme C Gallus gallus 147
MRSLLILVLCFLPLAALGKVFGRCELAAAMKR precursor (EC
HGLDNYRGYSLGNWVCAAKFESNFNTQATN 3.2.1.17) (1,4-
RNTDGSTDYGILQINSRWWCNDGRTPGSRN beta-N-
LCNIPCSALLSSDITASVNCAKKIVSDGNGMN acetylmurami-
AWVAWRNRCKGTDVQAWIRGCRL dase C) (Allergen Gal d 4) Gal d IV)
Lysozyme C, Rattus 148 MKALLVLGFLLLSASVQAKVFKHCELARILRS type 2
norvegicus SALAGYRGVSLENWMCMAQHESNFDTEAIN precursor (EC
YNSTDQSTDYGIFQINSRYWCNDGKTPRAVN 3.2.1.17) (1,4-
AGGIPCSALLQDDITQAIQCAKRVVRDPQGIR beta-N- AWVAWQRHCQNRDLSGYIRNCGV
acetylmurami- dase C) Lysozyme C, Mus 148
MKTLLTLGLLLLSVTAQAKVYERCEFARTLKR type M musculus
NGMAGYYGVSLADWVCLAQHESNYNTRATN precursor (EC
YNRGDQSTDYGIFQINSRYWCNDGKTPRAV 3.2.1.17) (1,4-
NACGINCSALLQDDITAAIQCAKRWRDPQGI beta-N- RAWVAWRAHCQNRDLSQYIRNCGV
acetylmurami- dase C) Lysozyme C, Mus 148
MKALLTLGLLLLSVTAQAKVYNRCELARILKR type P musculus
NGMDGYRGVKLADWVCLAQHESNYNTRAT precursor (EC
NYNRGDRSTDYGIFQINSRYWCNDGKTPRS 3.2.1.17) (1,4-
KNACGINCSALLQDDITAAIQCAKRVVRDPQG beta-N- IRAWVAWRTQCQNRDLSQYIRNCGV
acetylmurami- dase C) Lysozyme C-1 Anas 147
MKALLTLVFCLLPLAAQGKVYSRCELAAAMK precursor (EC platyrhynchos
RLGLDNYRGYSLGNWVCAANYESGFNTQAT 3.2.1.17) (1,4-
NRNTDGSTDYGILQINSRWWCDNGKTPRSK beta-N-
NACGIPCSVLLRSDITEAVRCAKRIVSDGDGM acetylmurami-
NAWVAWRNRCRGTDVSKWIRGCRL dase C) Lysozyme C-3 Anas 129
KVYERCELAAAMKRLGLDNYRGYSLGNWVC (EC 3.2.1.17) platyrhynchos
AANYESSFNTQATNRNTDGSTDYGILEINSR (1,4-beta-N-
WWCDNGKTPRAKNACGIPCSVLLRSDITEAV acetylmurami-
KCAKRIVSDGDGMNAWVAWRNRCKGTDVS dase) RWIRGCRL Lysozyme G Anser anser
185 RTDCYGNVNRIDTTGASCKTAKPEGLSYCGV (EC 3.2.1.17)
SASKKIAERDLQAMDRYKTIIKKVGEKLCVEP (1,4-beta-N-
AVIAGIISRESHAGKVLKNGWGDRGNGFGLM acetylmurami-
QVDKRSHKPQGTWNGEVHITQGTTILINFIKTI dase) (Goose-
QKKFPSWTKDQQLKGGISAYNAGAGNVRSY type lysozyme)
ARMDIGTTHDDYANDVVARAQYYKQHGY Lysozyme G Cygnus 185
RTDCYGNVNRIDTTGASCKTAKPEGLSYCGV (EC 3.2.1.17) atratus
PASKTIAERDLKAMDRYKTIIKKVGEKLCVEP (1,4-beta-N-
AVIAGIISRESHAGKVLKNGWGDRGNGFGLM acetylmurami-
QVDKRSHKPQGTWNGEVHITQGTTILTDFIK dase) (Goose-
RIQKKFPSWTKDQQLKGGISAYNAGAGNVRS type lysozyme)
YARMDIGTTHDDYANDVVARAQYYKQHGY Lysozyme G Struthio 185
RTGCYGDVNRVDTTGASCKSAKPEKLNYCG (EC 3.2.1.17) camelus
VAASRKIAERDLQSMDRYKALIKKVGQKLCV (1,4-beta-N-
DPAVIAGIISRESHAGKALRNGWGDNGNGFG acetylmurami-
LMQVDRRSHKPVGEWNGERHLMQGTEILIS dase) (Goose-
MIKAIQKKFPRWTKEQQLKGGISAYNAGPGN type lysozyme)
VRSYERMDIGTTHDDYANDVVARAQYYKQH GY Lysozyme G Gallus gallus 211
MLGKNDPMCLVLVLLGLTALLGICQGGTGCY precursor (EC
GSVSRIDTTGASCRTAKPEGLSYCGVRASRT 3.2.1.17) (1,4-
IAERDLGSMNKYKVLIKRVGEALCIEPAVIAGII beta-N-
SRESHAGKILKNGWGDRGNGFGLMQVDKRY acetylmurami-
HKIEGTWNGEAHIRQGTRILIDMVKKIQRKFP dase) (Goose-
RWTRDQQLKGGISAYNAGVGNVRSYERMDI type lysozyme)
GTLHDDYSNDVVARAQYFKQHGY Lysozyme P Drosophila 141
MKAFLVICALTLTAVATQARTMDRCSLAREM precursor (EC melanogaster
SKLGVPRDQLAKWTCIAQHESSFRTGVVGPA 3.2.1.17) (1,4-
NSNGSNDYGIFQINNKYWCKPADGRFSYNE beta-N-
CGLSCNALLTDDITNSVKCARKIQRQQGWTA acetylmurami- WSTWKYCSGSLPSINSCF
dase P) Lysozyme Chlamys 137 MMYFVLLCLLATGTTYGAHNFATGIVPQSCL
precursor islandica ECICKTESGCRAIGCKFDVYSDSCGYFQLKQ
AYWEDCGRPGGSLTSCADDIHCSSQCVQHY MSRYIGHTSCSRTCESYARLHNGGPHGCEH
GSTLGYWGHVQGHGC Lysozyme Bombyx mori 137
MQKLIIFALWLCVGSEAKTFTRCGLVHELRK precursor (EC
HGFEENLMRNWVCLVEHESSRDTSKTNTNR 3.2.1.17) (1,4-
NGSKDYGLFQINDRYWCSKGASPGKDCNVK beta-N-
CSDLLTDDITKAAKCAKKIYKRHRFDAWYGW acetylmurami- KNHCQGSLPDISSC dase)
Lysozyme Hyalophora 139 MTKYVILLAVLAFALHCDAKRFTRCGLVQELR precursor
(EC cecropia RLGFDETLMSNWVCLVENESGRFTDKIGKVN 3.2.1.17) (1,4-
KNGSRDYGLFQINDKYWCSKGTTPGKDCNV beta-N-
TCNQLLTDDISVAATCAKKIYKRHKFDAWYG acetylmurami- WKNHCQHGLPDISDC dase)
Maculatin 1.1 Litoria 21 GLFGVLAKVAAHVVPAIAEHF [Contains:
genimaculata Maculatin 1.1.1] Maculatin 1.2 Litoria 23
GLFGVLAKVASHVVPAIAEHFQA genimaculata Maculatin 2.1 Litoria 18
GFVDFLKKVAGTIANVVT genimaculata Maculatin 3.1 Litoria 26
GLLQTIKEKLESLESLAKGIVSGIQA genimaculata Magainins Xenopus 303
MFKGLFICSLIAVICANALPQPEASADEDMDE precursor laevis
REVRGIGKFLHSAGKFGKAFVGEIMKSKRDA EAVGPEAFADEDLDEREVRGIGKFLHSAKKF
GKAFVGEIMNSKRDAEAVGPEAFADEDLDER EVRGIGKFLHSAKKFGKAFVGEIMNSKRDAE
AVGPEAFADEDLDEREVRGIGKFLHSAKKFG KAFVGEIMNSKRDAEAVGPEAFADEDFDERE
VRGIGKFLHSAKKFGKAFVGEIMNSKRDAEA VGPEAFADEDLDEREVRGIGKFLHSAKKFGK
AFVGEIMNSKRDAEAVDDRRWVE Melittin-like Rana 22
FIGSALKVLAGVLPSIVSWVKQ peptide (MLP) temporaria Metchnikowin
Drosophila 52 MQLNLGAIFLALLGVMATTTSVLAEPHRRQG melanogaster
PIFDTRPSPFNPNQPRPGPIY Metchnikowin Drosophila 52
MQLNLGAIFLALLGVMATATSVLAEPHRHQG precursor melanogaster
PIFDTRPSPFNPNQPRPGPIY MGD1 Mytilus 57 CPNNYQCHRHCKSIPGRCGGYCGGWHRLR
antimicrobial galloprovincialis CTCYRCGGRREDVEDIEDIFDNEAADRF
peptide (Fragment) Misgurin Misgurnus 21 RQRVEELSKFSKKGAAARRRK
anguillicaudatus Moricin 1 Bombyx mori 66
MNILKFFFVFIVAMSLVSCSTAAPAKIPIKAIKT precursor
VGKAVGKGLRAINIASTANDVENFLKPKKRKH Moricin 2 Bombyx mori 66
MNILKLFFVFIVAMSLVSCSTAAPAKIPIKAIKT precursor
VGKAVGKGLRAINIASTANDVENFLKPKKRKH myeloid Ovis aries 160
METQRASLSLGRRSLWLLLLGLVLASARAQA antimicrobial
LSYREAVLRAVDQLNEKSSEANLYRLLELDP peptide 29
PPKQDDENSNIPKPVSFRVKETVCPRTSQQP precursor
AEQCDFKENGLLKECVGTVTLDQVGNNFDIT CAEPQSVRGLRRLGRKIAHGVKKYGPTVLRII
RIAG Myeloid Ovis aries 165 METQRAGLSLGRWSLRLLLLGLVLPSASTRS
antimicrobial FSYREAVLRAVDQFNERSAEANLYRLLELDP peptide
PPEQDAEDRGARKPVSFKVKETVCPRTSQQ precursor
PVEQCDFRKNGLVKQCVGTVTRYWIRGDFDI TCKDIQNVGLFGRLRDSLQRGGQKILEKAERI
GDRIKDIFRG Myticin A Mytilus 96 MKATILLAVLVAVFVAGTEAHSHACTSYWCG
precursor galloprovincialis KFCGTASCTHYLCRVLHPGKMCACVHCSRV
NNPFRVNQVAKSINDLDYTPIMKSMENLDNG MDML Myticin B Mytilus 96
MKATMLLAVVVAVFVAGTEAHPHVCTSYYCS precursor galloprovincialis
KFCGTAGCTRYGCRNLHRGKLCFCLHCSRV KFPFGATQDAKSMNELEYTPIMKSMENLDNG MDML
Mytilin A Mytilus edulis 34 GCASRCKAKCAGRRCKGWASASFRGRCYC KCFRC
Mytilin B Mytilus edulis 34 SCASRCKGHCRARRCGYYVSVLYRGRCYCK CLRC
Mytilin B Mytilus 103 MKAAVILAIALVAILAVHEAEASCASRCKGHC
antimicrobial galloprovincialis RARRCGYYVSVLYRGRCYCKCLRCSSEHSM
peptide KFPENEGSSPSDMMPQMNENENTEFGQDM precursor PTGETEQGETGI
Mytimycin Mytilus edulis 33 DCCRKPFRKHCWDCTAGTPYYGYSTRNIFG
(Fragment) CTC Neutrophil Rattus 94
MRTLTLLTALLLLALHTQAKSPQGTAEEAPDQ antibiotic norvegicus
EQLVMEDQDISISFGGDKGTALQDADVKAGV peptide NP-1
TCYCRRTRCGFRERLSGACGYRGRIYRLCC precursor R (Neutrophil defensin 1)
(RatNP-1) Neutrophil Rattus 94 MRTLTLLTALLLLALHTQAKSPQGTAEEAPDQ
antibiotic norvegicus EQLVMEDQDISISFGGDKGTALQDADVKAGV peptide NP-2
TCYCRSTRCGFRERLSGACGYRGRIYRLCC precursor R (Neutrophil defensin 2)
(RatNP-2) Neutrophil Rattus 87 MRTLTLLTTLLLLALHTQAESPQGSTKEAPDE
antibiotic norvegicus EQDISVFFGGDKGTALQDAAVKAGVTCSCRT peptide NP-3
SSCRFGERLSGACRLNGRIYRLCC precursor (Neutrophil defensin 3)
(RatNP-3a) Neutrophil Rattus 87 MRTLILLTTLLLLALHTQAESPQGSTKEAPDE
antibiotic norvegicus EQDISVFFGGDKGTALQDAAVKAGVTCSCRT peptide NP-3
SSCRFGERLSGACRLNGRIYRLCC precursor (Neutrophil defensin 3)
(RatNP-3b) Neutrophil Oryctolagus 95
MRTLALLAAILLVTLQAQAELHSGMADDGVD antibiotic cuniculus
QQQPRAQDLDVAVYIKQDETSPLEVLGAKAG peptide NP-4
VSCTCRRFSCGFGERASGSCTVNGVRHTLC precursor CRR (Microbicidal peptide
NP-4)
Neutrophil Rattus 93 MRTLTLLITLLLLALHTQAESPQERAKAAPDQ antibiotic
norvegicus DMVMEDQDIFISFGGYKGTVLQDAVVKAGQA peptide NP-4
CYCRIGACVSGERLTGACGLNGRIYRLCCR precursor (Neutrophil defensin 4)
(RatNP-4) Neutrophil Oryctolagus 95 MRTLALLAAILLVTLQAQAELHSGMADDGVD
antibiotic cuniculus QQQPRAQDLDVAVYIKQDETSPLEVLGAKAG peptide NP-5
VFCTCRGFLCGSGERASGSCTINGVRHTLCC precursor RR (Microbicidal peptide
NP-5) neutrophil beta- Bos taurus 60
MRLHHLLLALLFLVLSAASGISGPLSCGRNGG defensin 12
VCIPIRCPVPMRQIGTCFGRPVKCCRSW neutrophil beta- Bos taurus 54
MRLHHLLLVLLFLVLSAGSGFTQWRNPQSC defensin 5 RWNMGVCIPISCPGNMRQIGTCS
Neutrophil Cavia 178 MGTPRDAASGGPRLLLPLLLLLLLTPATAWVL cationic
porcellus SYQQAVQRAVDGINKNLADNENLFRLLSLDT antibacterial
QPPGDNDPYSPKPVSFTIKETVCTKMLQRPL polypeptide of
EQCDFKENGLVQRCTGTVTLDSAFNVSSLSC 11 kDa
LGGRRFRRMVGLRKKFRKTRKRIQKLGRKIG KTGRKVWKAWREYGQIPYPCRI Neutrophil
Cavia 93 MRTVPLFAACLLLTLMAQAEPLPRAADHSDT cationic peptide porcellus
KMKGDREDHVAVISFWEEESTSLEDAGAGA 1 precursor
GRRCICTTRTCRFPYRRLGTCIFQNRVYTFC (Neutrophil C defensin) (GPNP)
(Corticostatic peptide GP- CS1) (CP-1) Neutrophil Cavia 93
MRTVPLFAACLLLTLMAQAEPLPRAADHSDT cationic peptide porcellus
KMKGDREDHVAVISFWEEESTSLQDAGAGA 1B precursor
GRRCICTTRTCRFPYRRLGTCIFQNRVYTFC (Neutrophil C defensin) (CP- 1B)
(GNCP) Neutrophil Cavia 93 MRTVPLFAACLLLTLMAQAEPLPRAADHSDT cationic
peptide porcellus KMKGDREDHVAVISFWEEESTSLQDAGAGA 2 precursor
GRRCICTTRTCRFPYRRLGTCLFQNRVYTFC (CP-2) (GNCP) C (GNCP-2) Neutrophil
Mesocricetus 33 VTCFCRRRGCASRERHIGYCRFGNTIYRLCC defensin 1 auratus
RR (HANP-1) Neutrophil Mesocricetus 31
CFCKRPVCDSGETQIGYCRLGNTFYRLCCR defensin 2 auratus Q (HANP-2)
Neutrophil Macaca 30 ACYCRIPACLAGERRYGTCFYMGRVWAFCC defensin 2
mulatta (RMAD-2) Neutrophil Mesocricetus 33
VTCFCRRRGCASRERLIGYCRFGNTIYGLCC defensin 3 auratus RR (HANP-3)
Neutrophil Mesocricetus 33 VTCFCKRPVCDSGETQIGYCRLGNTFYRLCC defensin
4 auratus RQ (HANP-4) Neutrophil Macaca 96
MRTLVILAAILLVALQAQAEPLQARTDEATAA defensins 1, 3 mulatta
QEQIPTDNPEVVVSLAWDESLAPKDSVPGLR and 8
KNMACYCRIPACLAGERRYGTCFYLGRVWA precursor FCC (RMAD) Neutrophil
Macaca 94 MRTIAILAAILLFALLAQAKSLQETADDAATQE defensins 4 mulatta
QPGEDDQDLAVSFEENGLSTLRASGSQARR and 5
TCRCRFGRCFRRESYSGSCNINGRIFSLCCR precursor (RMAD) Neutrophil Macaca
94 MRTIAILAAILLFALLAQAKSLQETADEAATQE defensins 6 mulatta
QPGEDDQDLAVSFEENGLSTLRASGSQARR and 7
TCRCRFGRCFRRESYSGSCNINGRISSLCCR precursor NK-lysin Sus scrofa 129
PGLAFSGLTPEHSALARAHPCDGEQFCQNLA precursor
PEDPQGDQLLQREELGLICESCRKIIQKLEDM (NKL)
VGPQPNEDTVTQAASRVCDKMKILRGVCKKI (Fragment)
MRTFLRRISKDILTGKKPQAICVDIKICKEKTG LI Nonhistone Oncorhynchus 69
PKRKSATKGDEPARRSARLSARPVPKPAAKP chromosomal mykiss
KKAAAPKKAVKGKKAAENGDAKAEAKVQAA protein H6 GDGAGNAK (Histone T)
[Contains: Oncorhyncin III] Oligosacchar- Bos taurus 190
MSRRYTPLAWVLLALLGLGAAQDCGSIVSRG ide-binding
KWGALASKCSQRLRQPVRYVVVSHTAGSVC protein
NTPASCQRQAQNVQYYHVRERGWCDVGYN FLIGEDGLVYEGRGWNTLGAHSGPTWNPIAI
GISFMGNYMHRVPPASALRAAQSLLACGAAR GYLTPNYEVKGHRDVQQTLSPGDELYKIIQQ
WPHYRRV Opistoporin 1 Opistophthalmus 44
GKVWDWIKSTAKKLWNSEPVKELKNTALNAA carinatus KNLVAEKIGATPS Opistoporin
2 Opistophthalmus 44 GKVWDWIKSTAKKLWNSEPVKELKNTALNAA carinatus
KNFVAEKIGATPS Pandinin 1 Pandinus 44 GKVWDWIKSAAKKIWSSEPVSQLKGQVLNA
imperator AKNYVAEKIGATPT Pandinin 2 Pandinus 24
FWGALAKGALKLIPSLFSSFSKKD imperator Parabutoporin Parabuthus 45
FKLGSFLKKAWKSKLAKKLRAKGKEMLKDYA schlechteri KGLLEGGSEEVPGQ
Penaeidin-1 Litopenaeus 50 YRGGYTGPIPRPPPIGRPPLRLVVCACYRLSV (Pen-1)
(P1) vannamei SDARNCCIKFGSCCHLVK Penaeidin-2a Litopenaeus 72
MRLVVCLVFLASFALVCQGEAYRGGYTGPIP precursor (Pen- vannamei
RPPPIGRPPFRPVCNACYRLSVSDARNCCIK 2a) (Pen-2) FGSCCHLVKG (P2)
Penaeidin-2b Litopenaeus 72 MRLVVCLVFLASFALVCQGEAYRGGYTGPIP
precursor (Pen- vannamei RPPPIGRPPLRPVCNACYRLSVSDARNCCIK 2b)
FGSCCHLVKG Penaeidin-2d Litopenaeus 72
MRLVVCLVFLASFALVCQGGAQRGGFTGPIP precursor (Pen- setiferus
RPPPHGRPPLGPICNACYRLSFSDVRICCNFL 2d) GKCCHLVKG Penaeidin-3a
Litopenaeus 82 MRLVVCLVFLASFALVCQGQVYKGGYTRPIP precursor (Pen-
vannamei RPPPFVRPLPGGPIGPYNGCPVSCRGISFSQ 3a) (P3-a)
ARSCCSRLGRCCHVGKGYSG Penaeidin-3b Litopenaeus 82
MRLVVCLVFLASFALVCQGQVYKGGYTRPVP precursor (Pen- vannamei
RPPPFVRPLPGGPIGPYNGCPVSCRGISFSQ 3b) (P3-b) ARSCCSRLGRCCHVGKGYSG
Penaeidin-3c Litopenaeus 81 MRLVVCLVFLASFALVCQGQVYKGGYTRPIP
precursor (Pen- vannamei RPPFVRPVPGGPIGPYNGCPVSCRGiSFSQA 3c) (P3-c)
RSCCSRLGRCCHVGKGYSG Penaeidin-3d Litopenaeus 82
MRLVVCLVFLASFALVCQGQVYKGGYTRPIP precursor (Pen- vannamei
RPPPFVRPLPGGPIGPYNGCPISCRGISFSQA 3d) RSCCSRLGRCCHVGKGYSG
Penaeidin-3e Litopenaeus 82 MRLVVCLVFLAPFALVCHGQVYKGGYTRPIP
precursor (Pen- vannamei RPPPFVRPLPGGPIGPYNGCPVSCRGISFSQ 3e)
ARSCCSRLGRCCHVGKGYSG Penaeidin-3f Litopenaeus 82
MRLVACLVFLASFALVCQGQVYKGGYTRPIP precursor (Pen- vannamei
RPPPFVRPLPGGPIGPYNGCPISCRGISFSQA 3f) RSCCSRLGRCCHVGKGYSG
Penaeidin-3g Litopenaeus 82 MRLVVCLVFLASFALVCQGQVYKGGYTRPIP
precursor (Pen- vannamei RPPPFVRPLPGGPISPYNGCPVSCRGISFSQ 3g)
ARSCCSRLGRCCHVGKGYSG Penaeidin-3h Litopenaeus 82
MRLVVCLVFLASFALVCQGQVYKGGYTRPIP precursor (Pen- vannamei
RPPPFVRPLPGGPIGPYNGCPISCRGISFSQA 3h) RSYCSRLGRCCHVGKGYSG
Penaeidin-3i Litopenaeus 82 MRLVVCLVFLASFALVCQGQVYKGGYTRPIP
precursor (Pen- vannamei RPPPFVRPLPGGPIGPYNGRPVSCRGISFSQ 3i)
ARSCCSRLGRCCHVGKGYSG Penaeidin-3j Litopenaeus 81
MRLVVCLVFLASFALVCQGQVYKGGYTRPVP precursor (Pen- vannamei
RPPFVRPLPGGPIGPYNGCPVSCRGISFSQA 3j) RSCCSRLGRCCHVGKGYSG
Penaeidin-3k Litopenaeus 75 MRLVVCLVFLASFALVCQGQGYKGPYTRPIL
precursor (Pen- setiferus RPYVRPVVSYNACTLSCRGITTTQARSCCTR 3k)
LGRCCHVAKGYSG Penaeidin-3l Litopenaeus 75
MRLVVCLVFLASFALVCQGQGYKGPYTRPIL precursor (Pen- setiferus
RPYVRPVVSYNVCTLSCRGITTTQARSCCTR 3l) LGRCCHVAKGYSG Penaeidin-3m
Litopenaeus 75 MRLVVCLVFLASFALVCQGQGCKGPYTRPIL precursor (Pen-
setiferus RPYVRPVVSYNACTLSCRGITTTQARSCCTR 3m) LGRCCHVAKGYSG
Penaeidin-3n Litopenaeus 75 MRLVVCLVFLASFALVCQGQGYKGPYTRPIL
precursor (Pen- setiferus RPYVRPVVSYNACTLSCRGITTTQARSCSTR 3n)
LGRCCHVAKGYSG Penaeidin-4a Litopenaeus 67
MRLVVCLVFLASFALVCQGHSSGYTRPLPKP precursor (Pen- vannamei
SRPIFIRPIGCDVCYGIPSSTARLCCFRYGDC 4a) CHRG Penaeidin-4c Litopenaeus
67 MRLVVCLVFLASFALVCQGYSSGYTRPLPKP precursor (Pen- vannamei
SRPIFIRPIGCDVCYGIPSSTARLCCFRYGDC 4c) CHRG Penaeidin-4d Litopenaeus
67 MRLLVCLVFLASFAMVCQGHSSGYTRPLRKP precursor (Pen- setiferus
SRPIFIRPIGCDVCYGIPSSTARLCCFRYGDC 4d) CHLG Phormicin Protophormia 94
MKFFMVFVVTFCLAVCFVSQSLAIPADAAND precursor terraenovae
AHFVDGVQALKEIEPELHGRYKRATCDLLSG (Insect
TGINHSACAAHCLLRGNRGGYCNGKGVCVC defensins A RN and B) Phylloxin
Phyllomedusa 64 MVFLKKSLLLVLFVGLVSLSICEENKREEHEEI precursor bicolor
EENKEKAEEKRGWMSKIASGIGTFLSGMQQ G Pleurocidin Pseudopleur- 25
GWGSFFKKAAHVGKHVGKAALHTYL onectes americanus Pleurocidin 2
Pseudopleur- 68 MKFTATFLMMAIFVLMVEPGECGWGSFFKKA precursor onectes
AHVGKHVGKAALTHYLGDKQELNKRAVDED americanus PNVIVFE Pleurocidin
Pseudopleur- 68 MKFTATFLMIAIFVLMVEPGECGWGSFFKKA prepropoly- onectes
AHVGKHVGKAALTHYLGDKQELNKRAVDED peptide americanus PNVIVFE
Pleurocidin Pseudopleur- 68 MKFTATFLMMFIFVLMVEPGECGWGSIFKHG
prepropoly- onectes RHAAKHIGHAAVNHYLGEQQDLDKRAVDED peptide
americanus PNVIVFE Pleurocidin Pseudopleur- 60
MKFTATFLMIAIFVLMVEPGECGWGSFFKKA prepropoly- onectes
AHVGKHVGKAALTHYLGDKQELNKRAVDE peptide americanus (Fragment)
Pleurocidin Pseudopleur- 60 MKFTATFLMMFIFVLMVEPGECGWGSIFKHG
prepropoly- onectes RHAAKHIGHAAVNHYLGEQQDLDKRAVDE peptide
americanus (Fragment) Pleurocidin-like Pseudopleur- 89
MKFTATFLLLFIFVLMVDLGEGRRKKKGSKRK prepropoly- onectes
GSKGKGSKGKGRWLERIGKAGGIIIGGALDH peptide americanus
LGQGQVQGPDYDYQEGEELNKRAVDE (Fragment)
Pleurocidin-like Pseudopleur- 72 MKFTATFLLLFIFVLMVDLGEGRRKRKWLRRI
prepropoly- onectes GKGVKIIGGAALDHLGQGQVQGQDYDYQEG peptide
americanus QELNKRAVDE (Fragment) Pleurocidin-like Pseudopleur- 61
MKFTATFLVLSLVVLMAEPGECFLGALIKGAI prepropoly- onectes
HGGRFIHGMIQNHHGYDEQQELNKRAVDE peptide americanus (Fragment)
Polyphemusin I Limulus 18 RRWCFRVCYRGFCYRKCR polyphemus
Polyphemusin Limulus 18 RRWCFRVCYKGFCYRKCR II polyphemus Ponericin
G1 Pachycondyla 30 GWKDWAKKAGGWLKKKGPGMAKAALKAAM goeldii Q
Ponericin G2 Pachycondyla 30 GWKDWLKKGKEWLKAKGPGIVKAALQAATQ goeldii
Ponericin G3 Pachycondyla 30 GWKDWLNKGKEWLKKKGPGIMKAALKAATQ goeldii
Ponericin G4 Pachycondyla 29 DFKDWMKTAGEWLKKKGPGILKAAMAAAT goeldii
Ponericin G5 Pachycondyla 30 GLKDWVKIAGGWLKKKGPGILKAAMAAATQ goeldii
Ponericin G6 Pachycondyla 18 GLVDVLGKVGGLIKKLLP goeldii Ponericin
G7 Pachycondyla 19 GLVDVLGKVGGLIKKLLPG goeldii Ponericin L1
Pachycondyla 24 LLKELWTKMKGAGKAVLGKIKGLL goeldii Ponericin L2
Pachycondyla 24 LLKELWTKIKGAGKAVLGKIKGLL goeldii Ponericin W1
Pachycondyla 25 WLGSALKIGAKLLPSWGLFKKKKQ goeldii Ponericin W2
Pachycondyla 25 WLGSALKIGAKLLPSWGLFQKKKK goeldii Ponericin W3
Pachycondyla 26 GIWGTLAKIGIKAVPRVISMLKKKKQ goeldii Ponericin W4
Pachycondyla 26 GIWGTALKWGVKLLPKLVGMAQTKKQ goeldii Ponericin W5
Pachycondyla 24 FWGALIKGAAKLIPSWGLFKKKQ goeldii Ponericin W6
Pachycondyla 20 FIGTALGIASAIPAIVKLFK goeldii Preprodefensin
Boophilus 74 MRGIYICLXFVLXCGLVSGLADVPAESEMAHL microplus
RVRRGFGCPFNQGACHRHCRSIRRRGGYCA GLIKQTCTCYRN preprodefensin Ixodes
76 MKVLAVSLAFLLIAGLISTSLAQNEEGGEKELV ricinus
RVRRGGYYCPFFQDKCHRHCRSFGRKAGY CGGFLKKTCICVMK Probable Riptortus 678
MRSPRVIHLACVIAYIVAVEAGDKPVYLPRPT antibacterial clavatus
PPRPIHPRLAREVGWELEGQGLSPLSEAELL peptide
PEVRERRSPVDKGGYLPRPTPPRPVYRSRR polyprotein
DASLESELSPLSVAEVLPEVRERRSPVDKGG precursor
YLPRPTPPRPVYRSRRDASLESELSPLSEAE VLPEVRERRSPVDKGGYLPRPTPPRPVYRS
RRVASLESELSPLSEAEVLPEVRERRSPVDK GGYLPRPTPPRPVYRSRRDASLESELSPLSE
EEVLPEVRERGSPVDKGGYLPRPTPPRPVY RSRRDASLESELSPLSVAEDLPEVRERRSPV
DKGGYLPRPTPPRPVYRSRRDASLESELSPL SEAEVLPEVRERRSPVDKGGYLPRPTPPRPV
YRSRRDASLESELSPLSEAEVLPEVRERRSP VDKGGYLPRPTPPRPVYRSRRDASLESELSP
LSEAEVLPEVRERRSPVDKGGYLPRPTPPRP VYRSRRDASLESELSPLSEAEVLPEVRERRS
PVDKGGYLPRPTPPRPVYRSRRDATLESELS PSSEAEVLPEVRERRSPVDKGGYLPRPTPPR
PVYRSRRDASLESELSPLSEAEVLPEVRERR SPVDKGGYLPRPTPPRPVYRSRRDASLESEL
SPLSEAEGLPEVRERRSPGGQGGYLPRPTP RTPLCRSRRDANLDAEQSPVSEGWLPEVR
Probable Riptortus 150 MHIARFCLLSSMAVLALSAGYVSGAVIEIPDEI
antibacterial clavatus LDSARFISLYSDGLRQKRQLNLSGPGSEHAG peptide
TIRLDGQRNIFDNGRTRVDGTGSYQLDYARG precursor
MKPIHGAGLGAEVNHNIWRGRGGQSLDLYG GATRQFNFGNRPNEWGAHGGIRYNF
Proenkephalin Bos taurus 263 MARFLGLCTWLLALGPGLLATVRAECSQDCA A
precursor TCSYRLARPTDLNPLACTLECEGKLPSLKTW [Contains:
ETCKELLQLTKLELPPDATSALSKQEESHLLA Synenkephalin
KKYGGFMKRYGGFMKKMDELYPLEVEEEAN Met-enkephalin
GGEVLGKRYGGFMKKDAEEDDGLGNSSNLL (Opioid growth
KELLGAGDQREGSLHQEGSDAEDVSKRYGG factor) (OGF);
FMRGLKRSPHLEDETKELQKRYGGFMRRVG Met- RPEWWMDYQKRYGGFLKRFAEPLPSEEEG
enkephalin- ESYSKEVPEMEKRYGGFMRF Arg-Gly-Leu; Leu- enkephalin;
Enkelytin; Met- enkephalin- Arg-Phe] Prophenin-1 Sus scrofa 212
LLLLALVVPSASAQALSYREAVLRAVDRLNEQ precursor (PF-
SSEANLYRLLELDQPPKADEDPGTPKPVSFT 1) (C6)
VKETVCPRPTRQPPELCDFKENGRVKQCVG (Fragment)
TVTLDQIKDPLDITCNEGVRRFPWWWPFLRR PRLRRQAFPPPNVPGPRFPPPNFPGPRFPP
PNFPGPRFPPPNFPGPRFPPPNFPGPPFPPP IFPGPWFPPPPPFRPPPFGPPRFPGRR
Prophenin-2 Sus scrofa 228 METQRASLCLGRWSLWLLLLALVVPSASAQA
precursor (PF- LSYREAVLRAVDRLNEQSSEANLYRLLELDQ 2) (PR-2) (C12)
PPKADEDPGTPKPVSFTVKETVCPRPTRRPP (Prophenin-1
ELCDFKENGRVKQCVGTVTLDQIKDPLDITCN like)
EGVRRFPWWWPFLRRPRLRRQAFPPPNVP GPRFPPPNVPGPRFPPPNFPGPRFPPPNFP
GPRFPPPNFPGPPFPPPIFPGPWFPPPPPFR PPPFGPPRFPGRR Protegrin 1 Sus
scrofa 149 METQRASLCLGRWSLWLLLLALVVPSASAQA precursor (PG-
LSYREAVLRAVDRLNEQSSEANLYRLLELDQ 1) (Neutrophil
PPKADEDPGTPKPVSFTVKETVCPRPTRQPP peptide 1)
ELCDFKENGRVKQCVGTVTLDQIKDPLDITCN EVQGVRGGRLCYCRRRFCVCVGRG Protegrin
2 Sus scrofa 147 METQRASLCLGRWSLWLLLLALVVPSASAQA precursor (PG-
LSYREAVLRAVDRLNEQSSEANLYRLLELDQ 2) PPKADEDPGTPKPVSFTVKETVCPRPTRQPP
ELCDFKENGRVKQCVGTVTLDQIKDPLDITCN EVQGVRGGRLCYCRRRFCICVG Protegrin 3
Sus scrofa 149 METQRASLCLGRWSLWLLLLALVVPSASAQA precursor (PG-
LSYREAVLRAVDRLNEQSSEANLYRLLELDQ 3) PPKADEDPGTPKPVSFTVKETVCPRPTRQPP
ELCDFKENGRVKQCVGTVTLDQIKDPLDITCN EVQGVRGGGLCYCRRRFCVCVGRG Protegrin
4 Sus scrofa 149 METQRASLCLGRWSLWLLLLALVVPSASAQA precursor (PG-
LSYREAVLRAVDRLNEQSSEANLYRLLELDQ 4) PPKADEDPGTPKPVSFTVKETVCPRPTRQPP
ELCDFKENGRVKQCVGTVTLDQIKDPLDITCN EVQGVRGGRLCYCRGWCFCVGRG Protegrin
5 Sus scrofa 149 METQRASLCLGRWSLWLLLLGLVVPSASAQ precursor (PG-
ALSYREAVLRAVDRLNEQSSEANLYRLLELD 5) QPPKADEDPGTPKPVSFTVKETVCPRPTRQP
PELCDFKENGRVKQCVGTVTLDQIKDPLDITC NEVQGVRGGRLCYCRPRFCVCVGRG
Protegrin-1 Sus scrofa 19 RGGRLCYCRRRFCVCVGRX Pseudin 1 Pseudis 24
GLNTLKKVFQGLHEAIKLINNHVQ paradoxa Pseudin 2 Pseudis 24
GLNALKKVFQGIHEAIKLINNHVQ paradoxa Pseudin 3 Pseudis 23
GINTLKKVIQGLHEVIKLVSNHE paradoxa Pseudin 4 Pseudis 23
GINTLKKVIQGLHEVIKLVSNHA paradoxa Putative Litopenaeus 188
MKGIKAVILCGLFTAVLAGKYRGFGQPLGGL antimicrobial setiferus
GVPGGGVGVGVGGGLGGGLGGGLGGGLG peptide GGLGGGLGGLGGGLGGLGGGLGGGLGGGL
GGGLGGGLGGSHGTSDCRYWCKTPEGQAY CCESAHEPETPVGTKPLDCPQVRPTCPRFH
GPPTTCSNDYKCAGLDKCCFDRCLGEHVCK PPSFFGQQIFG Putative Litopenaeus 123
MKGLGVILCCVLAVVPAHAGPGGFPGGVPG antimicrobial setiferus
RFPSATAPPATCRRWCKTPENQAYCCETIFE peptide
PEAPVGTKPLDCPQVRPTCPRFHGPPVTCS SDYKCGGVDKCCFDRCLGEHVCKPPSFYSQ FP
Putative Litopenaeus 141 MKGLGVILCCVLAVVPAHAGPGGFSGGVPG
antimicrobial setiferus GFPGGRPGGFPGGVPGGFPSATAPPATCRR peptide
WCKTPENQAYCCETIFEPEAPVGTKPLDCPQ VRPTCPPTRFGGRPVTCSSDYKCGGLDKCC
FDRCLGEHVCKPPSFYSQFR Putative Litopenaeus 163
MKGIKAVILCGLFTAVLAGKFRGFGQPFGGL antimicrobial vannamei
GGPGGGVGVGGGFPGGGLGVGGGLGVGG peptide GLGVGGGLGVGGGLGTGTSDCRYWCKTPE
GQAYCCESAHEPETPVGTKILDCPQVRPTCP RFHGPPTTCSNDYKCAGLDKCCFDRCLGEH
VCKPPSFFGSQVFG Putative Litopenaeus 163
MKGIKAVILCGLFTAVLAGKFRGFGQPFGGL antimicrobial vannamei
GGPGGGVGVGGGFPGGGLGVGGGLGVGG peptide GLGVGGGLGVGGGLGTGTSDCRYWCKTPE
GQAYCCESAHEPETPVGTKPLDCPQVRPTC PRFHGPPTTCSNDYKCAGLDKCCFDRCLGE
HVCKPPSFFGSQVFG Putative Litopenaeus 169
MKGIKAVILCGLFTAVLAGKFRGFGQPFGGL antimicrobial vannamei
GGPGGGVGVGGGFPGGGLGVGGGLGVGG peptide GLGVGGGLGVGGGLGVGGGLGTGTSDCRY
WCKTPEGQAYCCESAHEPETPVGTKILDCP QVRPTCPRFHGPPTTCSNDYKCAGLDKCCF
DRCLGEHVCKPPSFFGSQVFG Putative Litopenaeus 163
MKGIKAVILCGLFTAVLAGKFRGFGQPFGGL antimicrobial vannamei
GGPGGSVGVGGGFPGGGLGVGGGLGVGG peptide GLGVGGGLGVGGGLGTGTSDCRYWCKTPE
GQAYCCESAHEPETPVGTKPLDCPQVRPTC PRFHGPPTTCSNDYKCAGLDKCCFDRCLGE
HVCKPPSFFGSQVFG Putative Litopenaeus 151
MKGIKAVILCGLFTAVLAGKFRGFGRPFGGL antimicrobial vannamei
GGPGGGVGVGGGFPGGGLGVGGGLGVGG peptide GLGTGTSDCRYWCKTPEGQAYCCESAHEPE
TPVGTKPLDCPQVRPTCPRFHGPPTTCSND YKCAGLDKCCFDRCLGEHVCKPPSFFGSQV FG
Putative Litopenaeus 163 MKGIKAVILCGLFTAVLAGKFRGFGRPFGGL
antimicrobial vannamei GGPGGGVGVGGGFPGGGLGVGGGLGVGG peptide
GLGVGGGLGVGGGLGTGTSDYRYWCKTPE GQAYCCESAHEPETPVGTKPLDCPQVRPTC
PRFHGPPTTCSNDYKCAGLDKCCFDRCLGE HVCKPPSFFGSQVFG Putative beta Mus 79
MKTFLFLFAVLFFLDPAKNAFFDEKCSRVNG defensin musculus
RCTASCLKNEELVALCQKNLKCCVTVQPCGK SKSNQSDEGSGHMGTWG Putative beta Mus
63 MPQTFFVFCFLFFVFLQLFPGTGEIAVCETCR defensin musculus
LGRGKCRRACIESEKIVGWCKLNFFCCRERI Putative beta Mus 64
MRIFSLIVAGLVLLIQLYPAWGTLYRRFLCKK defensin musculus
MNGQCEAECFTFEQKIGTCQANFLCCRKRK EH Putative beta Mus 67
MRTLCSLLLICCLLFSYTTPAANSIIGVSEMER defensin musculus
CHKKGGYCYFYCFSSHKKIGSCFPEWPRCC KNIK
Putative beta Mus 77 MRTLCSLLLICCLLFSYTTPAVGDLKHLILKAQ defensin
musculus LARCYKFGGFCYNSMCPPHTKFIGNCHPDHL HCCINMKELEGST Putative
beta Mus 73 MRTLCSLLLICCLLFSYTTPAVGDLKHLILKAQ defensin musculus
LTRCYKFGGFCHYNICPGNSRFMSNCHPENL RCGKNIKQF Putative Mesobuthus 61
MTYAILIIVSLLLISDRISNVVDKYGSENPLDCN potassium martensii
EHCLKTKNQIGICHGANGNEKCSCMES channel blocker TXKs2 PYLa/PGLa Xenopus
64 MYKQIFLCLIIAALCATIMAEASAFADADEDDD precursor laevis
KRYVRGMASKAGAIAGKIAKVALKALGRRDS Pyrrhocoricin Pyrrhocoris 20
VDKGSYLPRPTPPRPIYNRN apterus Ranalexin Rana 66
MFTLKKSLLLLFFLGTINLSLCEEERNAEEER precursor catesbeiana
RDNPDERDVEVEKRFLGGLIKIVPAMICAVTK KC Ranalexin-1CA Rana 20
FLGGLMKAFPALICAVTKKC clamitans Ranalexin-1CB Rana 20
FLGGLMKAFPAIICAVTKKC clamitans Ranatuerin-1C Rana 25
SMLSVLKNLGKVGLGLVACKINKQG clamitans RANATUERIN- Rana 28
GLLDTIKGVAKTVAASMLDKLKCKISGC 2B berlandieri Ranatuerin- Rana 31
GLFLDTLKGAAKDVAGKLLEGLKCKIAGGKP 2CA clamitans Ranatuerin- Rana 27
GLFLDTLKGLAGKLLQGLKGIKAGCKP 2CB clamitans RANATUERIN- Rana 32
GILSSIKGVAKGVAKNVAAQLLDTLKCKITGC 2LB luteiventris RANATUERIN- Rana
pipiens 27 LMDTVKNVAKNLAGHMLDKLKCKITGC 2P RANATUREIN- Rana 32
GILDSFKGVAKGVAKDLAGKLLDKLKGKITGC 2LA luteiventris Rhinocerosin
Oryctes 142 MMKLYIVFGFIAFSAAYVVPEGYYEPEYYPAD precursor rhinoceros
GYESERVARASPAELIFDEDLADEPEVEEPQ YYIRTRRSLQPGAPNFPMPGSQLPTSITSNIE
KQGPNTAATINAQHKTDRYDVGATWSKVIRG PGRSKPNWSIGGTYRW Royalism Apis
mellifera 95 MKIYFIVGLLFMAMVAIMAAPVEDEFEPLEHF precursor
ENEERADRHRRVTGDLLSFKGQVNDSAGAA (Defensin)
NGLSLGKAGGHGEKVGGIGRKTSFKDLWDK RFG Rugosin A Rana rugosa 33
GLLNTFKDWAISIAKGAGKGVLTTLSGKLDKS C Rugosin B Rana rugosa 33
SLFSLIKAGAKFLGKNLLKQGAQYAACKVSKE C Rugosin C Rana rugosa 37
GILDSFKQFAKGVGKDLIKGAAQGVLSTMSC KLAKTC Sapecin B Sarcophaga 88
MKFLTSLLLLFVVVMVSAVNLSMAKESANQL precursor peregrina
TERLQELDGAAIQEPAELNRHKRLTCEIDRSL CLLHCRLKGYLRAYCSQQKVCRCVQ Sapecin
C Sarcophaga 40 ATCDLLSGIGVQHSACALHCVFRGNRGGYCT peregrina GKGICVCRN
Sapecin Sarcophaga 94 MKSFIVLAVTLCLAAFFMGQSVASPAAAAEES precursor
peregrina KFVDGLHALKTIEPELHGRYKRATCDLLSGTG
INHSACAAHCLLRGNRGGYCNGKAVCVCRN Sarcotoxin IA Sarcophaga 63
MNFQNIFIFVALILAVFAGQSQAGWLKKIGKKI precursor peregrina
ERVGQHTRDATIQGLGIAQQAANVAATARG Sarcotoxin IB Sarcophaga 63
MNENKVFIEVALILAVFAGQSQAGWLKKIGKKI precursor peregrina
ERVGQHTRDATIQVIGVAQQAANVAATARG Sarcotoxin IC Sarcophaga 39
GWLRKIGKKIERVGQHTRDATIQVLGIAQQAA peregrina NVAATAR Sarcotoxin ID
Sarcophaga 40 GWIRDFGKRIERVGQHTRDATIQTIAVAQQAA peregrina NVAATLKG
Sarcotoxin II-1 Sarcophaga 265 MKSFVLFAACMAIIALGSLAHAYPQKLPVPIPP
precursor peregrina PSNPPVAVLQNSVATNSKGGQDVSVKLSAT
NLGNNHVQPIAEVFAEGNTKGGNVLRGATV GVQGHGLGASVTKTQTDTKIKGLDFQPQLSS
STLALQGDRLGASISRDVNRGVSDTFTKSVS ANVFRNDNHNLDATVFRSDVRQNNGFNFQK
TGGMLDYSHANGHGLNAGLTHFSGIGNQAN VGGSSTLFKSNDGSLSLKANAGGSQWLSGP
FSNQRDYNVGLSLTHHGCGG Sarcotoxin II-2 Sarcophaga 294
MKSFVFFAACFAIVALNSLAHAYPQKLPVPIP precursor peregrina
PPTNPPVAAFHNSVATNSKGGQDVSVKLAAT NLGNKHVQPIAEVFAKGNTQGGNVLRGATV
GVQGHGLGASVTKTQDGIAESFRKQAEANL RLGDSASLIGKVSQTDTKIKGIDFKPQLSSSSL
ALQGDRLGASISRDVNRGVSDTLTKSISANVF RNDNHNLDASVFRSDVRQNNGFNFQKTGG
MLDYSHANGHGLNAGLTRFSGIGNQANVGG YSTLFRSNDGLTSLKANAGGSQWLSGPFAN
QRDYSFGLGLSHNAWRG Sarcotoxin II-3 Sarcophaga 294
MKSFVLFAACMAIVALSSLAHAYPQKLPVPIP precursor peregrina
PPTNPPVAAFHNSVATNSKGGQDVSVKLXAT NLGNKHVQPIAEVFAEGNTKGGNVIRGATVG
VQGHGLGASVTKSGNGIAESFRKQAEANLRL GDSASLIGKVSQTDTKIKGIDFKPQLSSSSLAL
QGDRLGASISRDVNRGVSDTLTKSISANVFR NDNHNLDASVFRSDVRQNNGFNFQKTGGML
DYSHANGHGLNAGLTRFSGIGNQANVGGYS TLFRSNDGLTSLKANAGGSQWLSGPFANQR
DYSFGLGLSHNAWRG Sarcotoxin IIA Sarcophaga 294
MKSFVFFAACMAIIALSSLVQAYPQKLPVPIPP precursor peregrina
PTNPPVAAFHNSVATNSKGGQDVSVKLAATN LGNKHVQPIAEVFAEGNTKGGNVLRGATVGV
QGHGLGASVTKSQDGIAESFRKQAEANLRLG DSASLIGKVSQTDTKIKGIDFKPQLSSSSLALQ
GDRLGASISRDVNRGVSDTLTKSVSANLFRN DNHNLDASVFRSDVRQNNGFNFQKTGGMLD
YSHANGHGLNAGLTRFSGIGNQATVGGYSTL FRSNDGLTSLKANAGGSQWLSGPFANQRDY
SFGLGLSHNAWRG Scorpine Pandinus 94
MNSKLTALIFLGLIAIAYCGWINEEKIQKKIDER precursor imperator
MGNTVLGGMAKAIVHKMAKNEFQCMANMD MLGNCEKHCQTSGEKGYCHGTKCKCGTPLS Y
Secretogranin I Bos taurus 646 MQPAALLGLLGATVVAAVSSMPVDIRNHNEE
precursor (Sgl) VVTHCIIEVLSNALLKSSAPPITPECRQVLKKN (Chromogranin
GKELKNEEKSENENTRFEVRLLRDPADTSEA B) (CgB)
PGLSSREDSGEGDAQVPTVADTESGGHSRE [Contains:
RAGEPPGSQVAKEAKTRYSKSEGQNREEEM GAWK peptide;
VKYQKRERGEVGSEERLSEGPGKAQTAFLN Secretolytin]
QRNQTPAKKEELVSRYDTQSARGLEKSHSR ERSSQESGEETKSQENWPQELQRHPEGQE
APGESEEDASPEVDKRHSRPRHHHGRSRPD RSSQEGNPPLEEESHVGTGNSDEEKARHPA
HFRALEEGAEYGEEVRRHSAAQAPGDLQGA RFGGRGRGEHQALRRPSEESLEQENKRHGL
SPDLNMAQGYSEESEEERGPAPGPSYRARG GEAAAYSTLGQTDEKRFLGETHHRVQESQR
DKARRRLPGELRNYLDYGEEKGEEAARGKW QPQGDPRDADENREEARLRGKQYAPHHITE
KRLGELLNPFYDPSQWKSSRFERKDPMDDS FLEGEEENGLTLNEKNFFPEYNYDWWEKKP
FEEDVNWGYEKRNPVPKLDLKRQYDRVAEL DQLLHYRKKSAEFPDFYDSEEQMSPQHTAE
NEEEKAGQGVLTEEEEKELENLAAMDLELQK IAEKFSGTRRG Similar to Mus 93
MKKLVLLSALVLLAYQVQTDPIQNTDEETNTE cryptdin-4 musculus
EQPGEEDQAVSVSFGGQEGSALHEKLSRDLI CLCRKRRCNRGELFYGTCAGPFLRCCRRRR
Similar to Mus 93 MKTLVLLSALILLAYQVQTDPIQNTDEETNTEE cryptdin-4
musculus QPGEDDQAVSVSFGGQEGSALHEKLSRDLIC
LCRNRRCNRGELFYGTCAGPFLRCCRRRR Similar to Mus 95
MKTLVLLSALVLLAFQVQADPIQNTDEETNTE cryptdin-4 musculus
EQAGEEDQAVSVSFGDPEGSALHEKSSRDLI CYCRKGGCNRGEQVYGTCSGRLLFCCRRR HRH
Similar to Mus 95 MKTLVLLSALVLLAFQVQADPIQNTDEETNTE cryptdin-4
musculus EQAGEEDQAVSVSFGDPEGSALHEKSSRDLI
CYCRKGGCNRGEQVYGTCSGRLLLCCRRR HRH Similar to Mus 95
MKTLVLLSALVLLAFQVQADPIQNTDEETNTE cryptdin-4 musculus
EQPGEEDQAVSVSFGDPEGSALHEKSSRDLI CYCRKGGCNRGEQVYGTCSGRLLFCCRRR HRH
Single WAP Mus 80 MKLLGLSLLAVTILLCCNMARPEIKKKNVFSK motif protein 1
musculus PGYCPEYRVPCPFVLIPKCRRDKGCKDALKC precursor
CFFYCQMRCVDPWESPE (Elafin-like protein I) Single WAP Mus 85
MWPNSILVLMTLLISSTLVTGGGVKGEEKRV motif protein 2 musculus
CPPDYVRCIRQDDPQCYSDNDCGDQEICCF precursor WQCGFKCVLPVKDNSEEQIPQSKV
(Elafin-like protein II) Spingerin Pseudacan- 25
HVDKKVADKVLLLKQLRIMRLLTRL thotermes spiniger Styelin A Styela clava
20 GXFGKAFXSVSNFAKKHKTA (Fragment) Styelin B Styela clava 20
GXFGPAFHSVSNFAKKHKTA (Fragment) Styelin C Styela clava 80
MQMKATILIVLVALFMIQQSEAGWFGKAFRSV precursor
SNFYKKHKTYIHAGLSAATLLGDMTDEEFQE FMQDIEQAREEELLSRQ Styelin D Styela
clava 81 MQMKATILIVLVALFMIQQSEAGWLRKAAKSV precursor
GKFYYKHKYYIKAAWQIGKHALGDMTDEEFQ DFMKEVEQAREEELQSRQ Styelin E Styela
clava 81 MQMKATILIVLVALFMIQQSEAGWLRKAAKSV precursor
GKFYYKHKYYIKAAWKIGRHALGDMTDEEFQ DFMKEVEQAREEELQSRQ T22H6.7
Caenorhabditis 195 MFRKLIIATFVLSLCDLANSVTICSSSSLLSTFT protein
(ABF-6) elegans DPLCTSWCKVRFCSSGSCRSVMSGSDPTCE
CESCGFGSWFGSSSDSNSNQPVSGQYYAG GSGGEMATPNYGNNNGYNNGYNNGNNMRY
NDNNGYNTNNGYRGQPTPGYGNSNSNFNS NQQYSYQQYYNNRNNQYGNSGYGNAGQAG
QTGYPSGYQNLKKKR tachycitin Tachypleus 98
MASSFMFAVVVLFISLAANVESYLAFRCGRY precursor tridentatus
SPCLDDGPNVNLYSCCSFYNCHKCLARLEN CPKGLHYNAYLKVCDWPSKAGCTSVNKECH
LWKTGRK Tachyplesin I Tachypleus 77 MKKLVIALCLMMVLAVMVEEAEAKWCFRVCY
precursor tridentatus RGICYRRCRGKRNEVRQYRDRGYDVRAIPE
ETFFTRQDEDEDDDEE Tachyplesin II Tachypleus 77
MKKLVIALCLMMVLAVMVEEAEARWCFRVCY precursor tridentatus
RGICYRKCRGKRNEVRQYRDRGYDVRAIPD ETFFTRQDEDEDDDEE Tachystatin A2
Tachypleus 67 MKLQNTLILIGCLFLMGAMIGDAYSRCQLQGF precursor
tridentatus NCVVRSYGLPTIPCCRGLTCRSYFPGSTYGR CQRY Temporin A Rana 13
FLPLIGRVLSGIL temporaria Temporin B Rana 61
MFTLKKSLLLLFFLGTINLSLCEEERNAEEER
precursor temporaria RDEPDERDVQVEKRLLPIVGNLLKSLLGK Temporin C Rana
13 LLPILGNLLNGLL temporaria Temporin D Rana 13 LLPIVGNLLNSLL
temporaria Temporin E Rana 13 VLPIIGNLLNSLL temporaria Temporin F
Rana 13 FLPLIGKVLSGIL temporaria Temporin G Rana 61
MFTLKKSLLLLFFLGTINLSLCEEERDADEER precursor temporaria
RDDLEERDVEVEKRFFPVIGRILNGILGK Temporin H Rana 58
MFTLKKSLLLLFFLGTINLSLCEEERNAEEER precursor temporaria
RDEPDERDVQVEKRLSPNLLKSLLGK Temporin K Rana 10 LLPNLLKSLL temporaria
Temporin L Rana 13 FVQWFSKFLGRIL temporaria Temporin-1CA Rana 13
ELPELAKILTGVL clamitans Temporin-1CB Rana 13 FLPLFASLIGKLL
clamitans Temporin-1CC Rana 13 FLPFLASLLTKVL clamitans Temporin-1CD
Rana 13 FLPFLASLLSKVL clamitans Temporin-1CE Rana 13 FLPFLATLLSKVL
clamitans Temporin-1Ja Rana 13 ILPLVGNLLNDLL japonica Temporin-1LA
Rana 13 VLPLISMALGKLL luteiventris Temporin-1LB Rana 14
NFLGTLINLAKKIM luteiventris Temporin-1LC Rana 14 FLPILINLIHKGLL
luteiventris Temporin-1P Rana pipiens 13 FLPIVGKLLSGLL Tenecin 1
Tenebrio 84 MKLTIFALVACFFILQIAAFPLEEAATAEEIEQG precursor molitor
EHIRVKRVTCDILSVEAKGVKLNDAACAAHCL FRGRSGGYCNGKRVCVCR Tenecin 3
Tenebrio 96 MKTFVICLILVVAVSAAPDHHDGHLGGHQTG precursor molitor
HQGGQQGGHLGGQQGGHLGGHQGGQPGG HLGGHQGGIGGTGGQQHGQHGPGTGAGHQ GGYKTHGH
Termicin Pseudacan- 36 ACNFQSCWATCQAQHSIYFRRAFCDRSQCK thotermes
CVFVRG spiniger Testis defensin Mus 41
MKTLVLLSALFLLAFQVQADPIQNTDEETNTE (Fragment) musculus VQPQEEDQA
Testis defensin Mus 40 MKTLVLLSPSSCWPSRSRLILSKTQMKRLKL (Fragment)
musculus RSSQRKRTR Testis-specific Mus 83
MRLALLLLAILVATELVVSGKNPILQCMGNRG beta-defensin- musculus
FCRSSCKKSEQAYFYCRTFQMCCLQSYVRIS like protein LTGVDDNTNWSYEKHWPRIP
Thanatin Podisus 21 GSKKPVPIIYCNRRTGKCQRM maculiventris Theta
Defensin Macaca 18 GFCRCLCRRGVCRCICTR 1 mulatta theta defensin
Macaca 76 MRTFALLTAMLLLVALHAQAEARQARADEAA 1a precursor mulatta
AQQQPGTDDQGMAHSFTWPENAALPLSESA KGLRCICTRGFCRLL theta defensin
Macaca 76 MRTFALLTAMLLLVALHAQAEARQARADEAA 1b precursor mulatta
AQQQPGADDQGMAHSFTRPENAALPLSESA RGLRCLCRRGVCQLL theta defensin-
Macaca 18 RCICTRGFCRCLCRRGVC 1 mulatta Tigerinin-1 Hoplobatrachus
11 FCTMIPIPRCY tigerinus Tigerinin-2 Hoplobatrachus 12 RVCFAIPLPICH
tigerinus Tigerinin-3 Hoplobatrachus 12 RVCYAIPLPICY tigerinus
Tigerinin-4 Hoplobatrachus 11 RVCYAIPLPIC tigerinus tracheal Bos
taurus 64 MRLHHLLLALLFLVLSASSGFTQGVGNPVSC antimicrobial
VRNKGICVPIRCPGNMKQIGTCVGRAVKCCR peptide KK Tracheal Bos taurus 64
MRLHHLLLALLFLVLSAWSGFTQGVGNPVSC antimicrobial
VRNKGICVPIRCPGSMKQIGTCVGRAVKCCR peptide KK precursor (TAP) Xenopsin
Xenopus 81 MYKGIFLCVLLAVICANSLATPSSDADEDNDE precursor laevis
VERYVRGWASKIGQTLGKIAKVGLKELIQPKR [Contains: EAMLRSAEAQGKRPWIL
Xenopsin precursor fragment (XPF); Xenopsin]
[0077] TABLE-US-00003 Plant Antimicrobial Peptides Protein Name
Organism Name Length Sequence 22K Zea mays 206
AVFTVVNQCPFTVWAASVPVGGGR antifungal QLNRGESWRITAPAGTTAARIWAR
protein TGCQFDASGRGSCRTGDCGGVVQC TGYGRAPNTLAEYALKQFNNLDFF
DISLIDGFNVPMSFLPDGGSGCSR GPRCAVDVNARCPAELRQDGVCNN
ACPVFKKDEYCCVGSAANNCHPTN YSRYFKGQCPDAYSYPKDDATSTF TCPAGTNYKVVFCP
AC- Amaranthus 29 VGECVRGRCPSGMCCSQFGYCGKG AMP1 = caudatus PKYCG
ANTIMICROBIAL peptide Alpha- Zea mays 206 AVFTVVNQCPFTVWAASVPVGGGR
amylase/ QLNRGESWRITAPAGTTAARIWAR trypsin TGCQFDASGRGSCRTGDCGGVVQC
inhibitor TGYGRAPNTLAEYALKQFNNLDFF (Antifungal
DISILDGFNVPYSFLPDGGSGCSR protein) GPRCAVDVNARCPAELRQDGVCNN
ACPVFKKDEYCCVGSAANNCHPTN YSRYFKGQCPDAYSYPKDDATSTF TCPAGTNYKVVFCP
Alpha- Basella alba 20 GADFQECMKEHSQKQHQHQG basrubrin (Fragment)
antifungal Linum 37 ARFDIQNKCPYTVWAASVPVGGGR 25K protein
usitatissimum QLNSGQTWXIDAP antifungal Diospyros 30
ATFDIQNKXTYTVWAAAWAPSYPG 27K protein texana GXKQLD antifungal 2S
Raphanus 20 PQGPQQRPPLLQQCCNNLLQ storage sativus albumin large
chain antifungal 2S Raphanus 30 PAGPFRIPRCRREFQQAQHLRACQ storage
sativus QWLHRQ albumin small chain Antifungal Phytolacca 38
AGCIKNGGRCNASAGPPYCCSSYC Peptide americana FQIAGQSYGVCKNR
Antifungal Eucommia 41 QTCASRCPRPCNAGLCCSIYGYCG peptide 1 ulmoides
SGNAYCGAGNCRCQCRG (EAFP1) Antifungal Eucommia 41
QTCASRCPRPCNAGLCCSIYGYCG peptide 2 ulmoides SGAAYCGAGNCRCQCRG
(EAFP2) Antifungal Gastrodia 171 MAASASTAVILFFAVTTMMSLSAI protein
elata PAFASDRLNSDHQLDTGGSLAQGG YLFIIQNDCNLVLYDNNRAVWASG
TNGKASNCFLKMQNDGNLVIYSGS RAIWASNTNRQKGNYYLILQRDRN
VVIYDNSNNAIWATHTNVGNAEIT VIPHSNGTAAASGAAQNKVNELYI SMY Antifungal
Gastrodia 169 MASPASSAVIFLFAVAALMSLLAM protein elata
PALAASQLNAGQTLGTGQSLAQGP DQFVIQNDCNLVLYDSNRVVWASG
TNGKASGCVLRMQRDGNLVIYSGS RVIWASNTNRRDDNYYLLLQRDRN
VVIYDSSNNAIWATGTNVGNAAIT VIPHSNGTAAASGAAQNKVNEYLR P Antifungal
Ipomoea nil 92 MKFCTMFLVVLALASLLLTPSTIM protein
AQQCGSQARGRLCGNGLCCSQWGY CGSTAAYCGAGCQSQCKSTAASAT
DTTTTANQSTAKSDPAGGAN Antifungal Capsicum 85
MKFQVVILVLFALLLTRTSAQNCG protein annuum RQAGRRVCANRLCCSQFGFCGTTR
EYCGAGCQSNCRRYATDTTGEGEN VNNDEHKNNGGPN Antifungal Ipomoea nil 91
MKYCTMFIVLLGLGSLLLTPTTIM protein AQQCGRQASGRLCGNGLCCSQWGY
CGSTAAYCGAGCQSQCKSTAASST TTTTANQSTAKSDPAGGAN antifungal Sinapis
alba 25 QKLCERPSGTWSGVCGNNNACKNQ protein 1 C antifungal Brassica 30
QKLCERPSGTWSGVCGNNNACKNQ protein 1 napus CINLEK antifungal
Arabidopsis 27 QKLCERPSGTWSGVCGNSNACKNQ protein 1 thaliana CIN
Antifungal Raphanus 51 XKLCERPSGTWSGVCGNNNACKNQ Protein 1 sativus
CINLEKARHGSCNYVFPAHKCICY FPC Antifungal Malva 15 VAGPFRIPPLRREFQ
protein 1 parviflora large subunit (CW-1) (Fragment) Anti-fungal
Phytolacca 65 MAKVSSAYLKFALVMILLLSVISA protein 1 americana
VMSAGCIKNGGRCNASAGPPYCCS precursor SYCFQIAGQSYGVCKNR (PAFP-S)
Antifungal Malva 16 PAGPFRIPPRXRXEFQ protein 1 parviflora small
subunit (CW-1) (Fragment) antifungal Sinapis alba 26
QKLCQRPSGTWSGVCGNNNACRNQ protein 2 CI Antifungal Malva 20
PEDPQRRYQEXQREXRXQQE protein 2 parviflora large subunit (CW-2)
(Fragment) Antifungal Malva 15 PEDPQRRYQEEQRRE protein 3 parviflora
(CW-3) (Fragment) Antifungal Malva 37 DRQIDMEEQQLEKLNKQDRXPGLR
protein 4 parviflora YAAKQQMXTXRMG (CW-4) (Fragment) Antifungal
Malva 38 ITCGQVTSQVAGCLSYLQRGGAPA protein 5 parviflora
PXXXXGIRNLXXMA (CW-5) (Fragment) Antifungal Beta vulgaris 46
AICKKPSKFFKGACGRDADCEKAC protein AX1 DQENWPGGVCVPFLRCECQRSC
Antifungal Beta vulgaris 46 ATCRKPSMYFSGACFSDTNCQKAC protein AX2
NREDWPNGKCLVGFKCECQRPC Antifungal Gastrodia 129
SDRLNSGHQLDTGGSLAEGGYLFI protein elata IQNDCNLVLYDNNRAVWASGTNGK
GAFP-1 ASGCVLKMQNDGNLVIYSGSRAIW (Fragment) ASNTNRQNGNYYLILQRDRNVVIY
DNSNNAIWATHTNVGNAEITVIPH SNGTAAASG Antifungal Medicago 72
MEKKSLAGLCFLFLVLFVAQEIVV protein sativa TEARTCENLADKYRGPCFSGCDTH
precursor CTTKENAVSGRCRDDFRCWCTKRC Antifungal Gastrodia 178
MLEWGDGVFCGGCVGYLRGDSVEC protein elata GNCSDRLNSGHQLDTGGSLAQGGY
precursor LFIIQNDCNLVLYDNNRAVWASGT NGKASGCVLKMQNDGNLVIYSGSR
AIWASNTNRQNGNYYLILQRDRNV VIYDNSNNAIWATHTNVGNAEITA
IPHSNGTAAASGAAQNKVNELYIS MYSRSKRIAG Antifungal Hordeum 44
ATITWNRCSYTVWPGALPGGGVRL protein R vulgare DPGQRWALNMPAGTAGAAV
(Fragment) Antifungal Hordeum 37 ATFTVINKCQYTVWAAAVPAGGGQ protein S
vulgare KLDAGQTWSIXXP (Fragment) Antifungal Arabidopsis 80
MAKSATIITFLFAALVLFAAFEAP protein-like thaliana
TMVEAQKLCEKPSGTWSGVCGNSN ACKNQCINLEGAKHGSCNYVFPAH KCICYVPC
Antimicrobial Pisum 60 ALSFLFLFLFVAQEIVVTEANTCE detensin sativum
HLADTYRGVCFTDASCDDHCKNKA peptide HLISGTCHNFKC DRR230-c (Fragment)
Antimicrobial Macadamia 76 SAFTVWSGPGCNNRAERYSKCGCS Peptide 1
integrifolia AIHQKGGYDFSYTGQTAALYNQAG CSGVAHTRFGSSARACNPFGWKSI FIQC
Antimicrobial Mesembryan 64 MAKVSSSLLKFAIVLILVLSMSAI peptide 1
themum ISAKCIKNGKGCREDQGPPFCCSG precursor crystallinum
FCYRQVGWARGYCKNR Antimicrobial Macadamia 102
MASTKLFFSVITVMMLIAMASEMV peptide 1 integrifolia
NGSAFTVWSGPGCNNRAERYSKCG precursor CSAIHQKGGYDFSYTGQTAALYNQ (AMP1)
AGCSGVAHTRFGSSARACNPFGWK SIFIQC Antimicrobial Mirabilis 61
LPVAFLKFAIVLILFIAMSAMIEA peptide 1 jalapa QCIGNGGRCNENVGPPYCCSGFCL
precursor RQPGQGYGYCKNR (AMP1) (MJ-AMP1) (Fragment) Antimicrobial
Amaranthus 30 VGECVRGRCPSGMCCSQFGYCGKG Peptide 2 caudatus PKYCGR
Antimicrobial Mirabilis 63 MAKVPIAFLKFVIVLILFIAMSGM peptide 2
jalapa IEACIGNGGRCNENVGPPYCCSGF precursor CLRQPNQGYGVCRNR (AMP2)
(MJ-AMP2) Antimicrobial Spinacia 22 XTCESPSHKFKGPCATNRNCES peptide
D1 oleracea (So-D1) (Defensin D1) (Fragment) Antimicrobial Spinacia
52 GIFSSRKCKTPSKTFKGICTRDSN peptide D2 oleracea
CDTSCRYEGYPAGDCKGIRRRCMC (So-D2) SKPC (Defensin D2) (Fragment)
Antimicrobial Spinacia 25 GIFSSRKCKTVSKTFRGICTRNAN peptide D3
oleracea C (So-D3) (Defensin D3) (Fragment) Antimicrobial Spinacia
23 MFFSSKKCKTVSKTFRGPCVRNA peptide D4 oleracea (So-D4) (Defensin
D4) (Fragment)
Antimicrobial Spinacia 24 MFFSSKKCKTVXKTFRGPCVRNAN peptide D5
oleracea (So-D5) (Defensin D5) (Fragment) Antimicrobial Spinacia 24
GIFSNMYXRTPAGYFRGPXGYXXN peptide D6 oleracea (So-D6) (Defensin D6)
(Fragment) Antimicrobial Spinacia 38 GIFSSRKCKTPSKTFKGYCTRDSN
peptide D7 oleracea CDTSCRYEGYPAGD (So-D7) (Defensin D7) (Fragment)
Antimicrobial Zea mays 33 RSGRGECRRQCLRRHEGQPWETQE peptide MBP-1
CMRRCRRRG Antimicrobial Capsella 120 MASKTLILLGLFAILLVVSEVSAA
peptide shep- bursa- RESGMVKPESEETVQPEGYGGHGG GRP pastoris
HGGHGGHGGHGGHGHGGGGHGLDG YHGGHGGHGGGYNGGGGHGGHGGG
YNGGGHHGGGGHGLNEPVQTQPGV Antimicrobial Impatiens 333
MVQKGWFGVLLILFICSTLTSADS peptides balsamina
KPNPTKEEEPAKKPDEVSVKSGGP precursor EVSEDQYRHRCCAWGPGRKYCKRW
(IB-AMP) CANAEEAAAAIPEASEELAQEEAP [Contains:
VYSEDQWGRRCCGWGPGRRYCVRW Basic peptide CQNAEEAAAAIPEATEKAQEAPVY
AMP3 (IB- SEDQWGRRCCGWGPGRRYCVRWCQ AMP3); Basic
NAEEAAAAVAIPEASEKAQEGPVY peptide AMP1- SEDQWGRRCCGWGPGRRYCVRWCS 1
(IB-AMP1- NAADEVATPEDVEPGQYGRRCCNW 1); Basic
GPGRRYCKRWCHNAAEEATLKAFE peptide AMP1- EEAAREQPVYSEDQWGRRCCGWGP 2
(IB-AMP1- GRRYCRRWCQSAEEAAAFQAGEVT 2); Basic ASLMLIMFKACPCMGPVPSV
peptide AMP1- 3 (IB-AMP1- 3); Basic peptide A Antimicrobial Allium
cepa 132 MVRVVSLLAASTFILLIMIISSPY protein Ace-
ANSQNICPRVNRIVTPCVAYGLGR AMP1 APIAPCCRALNDLRFVNTRNLRRA precursor
ACRCLVGVVNRNPGLRRNPRFQNI PRDCRNTFVRPFWWRPRIQCGRIN LTDKLIYLDAEE
Antimicrobial Ipomoea nil 41 QQCGRQASGRLCGNRLCCSQWGYC protein PN-
GSTASYCGAGCQSQCRS AMP (PN- AMP1/PN- AMP2) antimicrobial Amaranthus
86 MVNMKCVALIVIVMMAFMMVDPSM protein hypochondriacus
GVGECVRGRCPSGMCCSQFGYCGK precursor GPKYCGRASTTVDHQADVAATKTA
KNPTDAKLAGAGSP Antimicrobial Phytolacca 37 ACIKNGGRCVASGGPPYCCSNYCL
seed protein americana QIAGQSYGVCKKH (Fragment) avematin Avena
sativa 26 TTITVVNKCSYTVWPGALPGGGVV LD Basal layer Zea mays 93
MAKFFNYTIIQGLLMLSMVLLASC antifungal AIHAHIISGETEEVSNTGSPTVMV
peptide TMGANRKIIEDNKNLLCYLRALEY precursor CCARTRQCYDDIKKCLEHCRG
Basal layer Zea mays 96 MVKILDHISIRGFFLLFMVLVASF antifungal
VGHAQIIRGETKEDNDTKSMTMTT peptide MRPGSYVTSMDEKSSLCFEDIKTL precursor
WYICRTTYHLYRTLKDCLSHCNSM Basal layer Zea mays 95
MVKSLDHITIRGLFLLFMFLVASF antifungal VGHAQIIRGETKENKDTNSMTMTT
peptide RPGSYVISMDEKSSLCFLDPRTLW precursor YICKITYRLFRTLKDCLEFCHSI
Basal layer Zea mays 73 MVLLASCVIHAHIISGEIEDVSNT antifungal
RSPTMMGANRKIIGDNKNLLCYLK peptide ALEYCCERTKQCYDDIKKCLEHCH precursor
S Beta-basrubin Basella alba 16 KIMAKPSKFYEQLRGR (Fragment) CBP20
Nicotiana 208 GKLSTLLLVLILYFIAAGANAQQC (Fragment) tabacum
GRQRGGALCSGNLCCSQFGWCGST PEYCSPSQGCQSQCSGGGGGGGGG
GGGGAQNVRATYHIYNPQNVGWDL YAVSAYCSTWDGNKPLAWRRKYGW
TAFCGPVGPRGRDSCGKCLRVTNT GTGAQTTVRIVDQCSNGGLDLDVN
VFRQLDTDGRGNQRGHLIVNYEFV NCGDNMNVLLSPVDKE CBP20 Nicotiana 211
MGKLSTLLFALVLYVIAAGANAQQ preproprotein tabacum
CGRQRGGALCSGNLCCIQFGWCGS TQEYCSPSQGCQSQCSGGGGGGGG
GGGGGGAAQNVRATYHIYNPQNVG WDLYAVSAYCSTWDGNKPLAWRRK
YGWTAFCGPVGPRGRDSCGKCLRV TNTGTGAQTTVRIVDQCSNGGLDL
DVNVFRQLDTDGRGNQRGHLIVNY EFVNCGDNMNVLVSPVDKE chitinase (EC
Nicotiana 378 MANSVTLFSIIFSCFLLRQLVCTN 3.2.1.14)/ tabacum
SQNVIKGGYWFKNSGLALNNIDST lysozyme (EC LFTHLFCAFADLNPQSNQLIISPE
3.2.1.17) PZ NQDSFSQFTSTVQRKNPSVKTFLS precursor,
IAGGRADTTAYGIMARQPNSRKSF pathogenesis- IDSSIRLARQFGFHGLDLDWEYPL
related SATDMTNLGILLNEWRTAINMEAR NSGRAALLLTAAVSYSPRVNGLNY
PVESVARNLNWINLMAYDFYGPNW SPSQTNSHAQLFDPVNHISGSDGI
NAWIQAGVPTKKLVLGIPFYGYAW RLVNPNIHDLRAPAAGKSNVGAVD
DGSMTYNRIRDYIVQSRATTVYNA TIVGDYCYSGSNWISYDDTQSVRN
KVNYVKGRGLLGYFAWHVAGDQNW GLSRTASQTWGVSSQEMK chitinase (EC Zea mays
280 MANAPRILALGLLALLCAAAGPAA 3.2.1.14) A AQNCGCQPNFCCSKFGYCGTTDAY
CGDGCQSGPCRSGGGGGGGGGGGG GGSGGANVANVVTDAFFNGIKNQA
GSGCEGKNFYTRSAFLSAVNAYPG FAHGGTEVEGKREIAAFFAHVTHE
TGHFCYISEINKSNAYCDASNRQW PCAAGQKYYGRGPLQISWNYNYGP
AGRDIGFNGLADPNRVAQDAVIAF KTALWFWMNNVHRVMPQGFGATIR
AINGALECNGNNPAQMNARVGYYK QYCQQLRVDPGPNLIC chitinase (EC Zea mays
268 QLVALGLALLCAVAGPAAAQNCGC 3.2.1.14) QPNVCCSKFGYCGTTDEYCGDGCQ
precursor SGPCRSGRGGGGSGGGGANVASVV TSSFFNGIKNQAGSGCEGKNFYTR
SAFLSAVKGYPGFAHGGSQVQGKR EIAAFFAHATHETGHFCYISEINK
SNAYCDPTKRQWPCAAGQKYYGRG PLQISWNYNYGPAGRAIGFDGLGD
PGRVARDAVVAFKAALWFWMNSVH GVVPQGFGATTRAMQRALECGGNN
PAQMNARVGYYRQYCRQLGVDPGP NLTC Chitinase, Nicotiana 377
MANSVTLFAIIFSCFLLQQLVCTN class V tabacum SQNVKGGYWFKDSGLALNNIDSTL
ETHLFCAFADLNPQLNQLIISPEN QDSFRQFTSTVQRKNPSVKTFLSI
AGGRANSTAYGIMARQPNSRKSFI DSSIRLARQLGFHGLDLDWEYPLS
AADMTNLGTLLNEWRTAINTEARN SGRAALLLTAAVSNSPRVNGLNYP
VESLARNLDWINLMAYDFYGPNWS PSQTNSHAQLFDPVNHVSGSDGIN
AWIQAGVPTKKLVLGIPFYGYAWR LVNANIHGLRAPAAGKSNVGAVDD
GSMTYNRIRDYIVESRATTVYNAT IVGDYCYSGSNWISYDDTQTVRNK
VNYVKGRGLLGYFAWHVAGDQNWG LSRTASQTWGVSFQEMK Chitin- Hydrangea 15
NSMERVEELRKKLQD binding macrophylla protein HM30 (Fragment)
Chitin-binding Hordeum 52 ATYHYYRPAQNNWDLGAPAVSAYC protein N, CBP
vulgare ATWDASKYGWTAFIVDQCANGGLD N (Fragments) LDWN Circulin A
Chassalia 30 GIPCGESCVWIPCISAALGCSCKN (CIRA) parviflora KVCYRN
Circulin B Chassalia 31 GVIPCGESCVFIPCISTLLGCSCK (CIRB) parviflora
NKVCYRN Cyclo- Psychotria 31 SIPCGESCVFIPCTVTALLGCSCK psychotride A
longipes SKVCYKN (CPT) Cysteine-rich Brassica 27
QKLCERPSGTWSGVCGNNNACKNQ antifungal rapa CIN protein 1 (AFP1)
(Fragment) Cysteine-rich Sinapis alba 51 QKLCERPSGTWSGVCGNNNACKNQ
antifungal CINLEKARHGSCNYVFPAHKCICY protein 1 FPC (AFP1) (M1)
Cysteine-rich Raphanus 80 MAKFASIIALLFAALVLFAAFEAP antifungal
sativus TMVEAQKLCERPSGTWSGVCGNNN protein 1 ACKNQCINLEKARHGSCNYVFPAH
precursor KCICYFPC (AFP1) Cysteine-rich Arabidopsis 80
MAKSATIVTLFFAALVFFAALEAP antifungal thaliana
MVVEAQKLCERPSGTWSGVCGNSN protein 1 ACKNQCINLEKARHGSCNYVFPAH
precursor KCICYFPC (AFP1) (Anther- specific protein S18 homolog)
Cysteine-rich Brassica 23 QKLCERPSGTWSGVCGNNNACKN antifungal napus
protein 2 (AFP2) (Fragment) Cysteine-rich Brassica 27
QKLCERPSGTXSGVCGNNNACKNQ antifungal rapa CIR protein 2 (AFP2)
(Fragment) Cysteine-rich Raphanus 80 MAKFASIIVLLFVALVVFAAFEEP
antifungal sativus TMVEAQKLCQRPSGTWSGVCGNNN protein 2
ACKNQCIRLEKARHGSCNYVFPAH precursor KCICYFPC (AFP2) Cysteine-rich
Sinapis alba 51 QKLCQRPSGTWSGVCGNNNACRNQ antifungal
CINLEKARHGSCNYVFPAHKCICY protein 2A FPC (AFP2A) (M2A) Cysteine-rich
Sinapis alba 52 QKLCARPSGTWNSSGNCRNNNACR antifungal
NFCIKLEKSRHGSCNIPFPSNKCI protein 2B CYFPC (AFP2B) (M2B)
Cysteine-rich Brassica 79 MAKFASIITLLFAALVVFAAFEAP antifungal napus
TMVEAKLCERSSGTWSGVCGNNNA
protein 3 CKNQCIRLEGAQHGSCNYVFPAHK precursor CICYFPC (AFP3)
Cysteine-rich Raphanus 79 MAKFASIVALLFAALVVFAAFEAP antifungal
sativus TVVEAKLCERSSGTWSGVCGNNNA protein 3 CKNQCIRLEGAQHGSCNYVFPAHK
precursor CICYFPC (AFP3) Cysteine-rich Raphanus 80
MAKFVSIITLLFVALVLFAAFEAP antifungal sativus
TMVEAQKLCERSSGTWSGVCGNNN protein 4 ACKNQCINLEGARHGSCNYIFPYH
precursor RCICYFPC (AFP4) Defense- Pisum 46
KTCEHLADTYRGVCFTNASCDDHC related sativum KNKAHLISGTCHNWKCFCTQNC
peptide 1 (Defensin 1) (Antifungal protein Psd1) Defense- Pisum 47
KTCENLSGTFKGPCIPDGNCNKHC related sativum RNNEHLLSGRCRDDFRCWCTNRC
peptide 2 (Defensin 2) (Antifungal protein Psd2) defensin Capsicum
75 MAGFSKVIATIFLMMMLVFATDMM annuum AEAKICEALSGNFKGLCLSSRDCG
NVCRREGFTSGVCRGFPLKCFCRK PGA Defensin Brassica 80
MAKFVSIITLFFAALVLFAAFEAP rapa TMVKAQKLCERSSGTWSGVCGNNN
ACKNQCINLEGARHGSCNYVFPYH RCICYFPC Defensin Helianthus 108
MAKISVAFNAFLLLLFVLAISEIG annuus SVKGELCEKASQTWSGTCGKTKHC
DDQCKSWEGAAHGACHVRDGKHMC FCYFNCSKAQKLAQDKLRAEELAK EKIEPEKATAKP
Defensin Helianthus 41 SHRFQGTCLSDTNCANVCHSERFS (Fragment) annuus
GGKCRGFRRRCFCTTHC defensin 1 Triticum 82 MASTRRMAAAPAVLLLLLLLVATE
precursor aestivum MGTMKTAEARTCLSQSHKFKGTCL
SNSNCAAVCRTENFPDGECNTHLV ERKCYCKRTC defensin AFP1 Heuchera 54
DGVKLCDVPSGTWSGHCGSSSKCS sanguinea QQCKDREHFAYGGACHYQFPSVKC FCKRQC
defensin AMP1 Dahlia 50 ELCEKASKTWSGNCGNTGHCDNQC merckii
KSWEGAAHGACHVRNGKHMCFCYF NC defensin AMP1 Aesculus 50
LCNERPSQTWSGNCGNTAHCDKQC hippocastanum QDWEKASHGACHKRENHWKCFCYF NC
defensin AMP1 Clitoria 49 NLCERASLTWTGNCGNTGHCDTQC ternatea
RNWESAKHGACHKRGNWKCFCYFN C defensin AMP2 Dahlia 20
EVCEKASKTWSGNCGNTGHC merckii Defensin CUA1 Helianthus 42
LSHSFKGTCLSDTNCANVCHSERF (Fragment) annuus SGGKCRGFRRRCFCTTHC
Defensin Elaeis 77 MEHSRRMLPAILLLLFLLMPSEMG EGAD1 guineensis
TKVAEARTCESQSHKFQGTCLRES NCANVCQTEGFQGGVCRGVRRRCF CTRLC Defensin
J1-1 Capsicum 75 MAGFSKVVATIFLMMLLVFATDMM precursor annuum
AEAKICEASGNFKGLCLSSRDCGN VCRREGFTDGSCIGFRLQCFCTKP CA Defensin J1-2
Capsicum 74 MAGFSKVIATIFLMMMLVFATGMV precursor annuum
AEARTCESQSHRFKGLCFSKSNCG SVCHTEGFNGGHCRGFRRRCFCTR HC Defensin
Brassica 80 MAKVASIVALLFPALVIFAAFEAP precursor oleracea
TMVEAQKLCERPSGWNSGVCGNN NACKNQCIRLEKARHGSCNYVFPA HKCICYFPC Defensin
Prunus 79 MERSMRLFSTAFVFFLLLAAAGMM protein 1 persica
MGPMVAEARTCESQSNRFKGTCVS TSNCASVCQTEGFPGGHCRGFRRR CFCTKHC
Endochitinase Zea mays 280 MANAPRILALGLLALLCAAAGPAA A precursor
AQNCGCQPNFCCSKFGYCGTTDAY (EC 3.2.1.14) CGDGCQSGPCRSGGGGGGGGGGGG
(Seed GGSGGANVANVVTDAFFNGIKNQA chitinase A)
GSGCEGKNFYTRSAFLSAVNAYPG FAHGGTEVEGKREIAAFFAHVTHE
TGHFCYISEINKSNAYCDASNRQW PCAAGQKYYGRGPLQISWNYNYGP
AGRDIGFNGLADPNRVAQDAVIAF KTALWFWMNNVHGVMPQGFGATIR
AINGALECNGNNPAQMNARVGYYK QYCQQLRVDPGPNLIC Endochitinase Zea mays
269 PQLVALGLALLCAVAGPAAAQNCG B precursor CQPNVCCSKFGYCGTTDEYCGDGC
(EC 3.2.1.14) QSGPCRSGRGGGGSGGGGANVASV (Seed
VTSSFFNGIKNQAGSGCEGKNFYT chitinase B) RSAFLSAVKGYPGFAHGGSQVQGK
(Fragment) REIAAFFAHATHETGHFCYISEIN KSNAYCDPTKRQWPCAAGQKYYGR
GPLQISWNYNYGPAGRAIGFDGLG DPGRVARDAVVAFKAALWFWMNSV
HGVVPQGFGATTRAMQRALECGGN NPAQMNARVGYYRQYCRQLGVDPG PNLTC Fabatin-1
Vicia faba 47 LLGRCKVKSNRFHGPCLTDTHCST VCRGEGYKGGDCHGLRRRCMCLC
Fabatin-2 Vicia faba 47 LLGRCKVKSNRFNGPCLTDTHCST
VCRGEGYKGGDCHGLRRRCMCLC Floral Petunia x 103
MARSICFFAVAILALMLFAAYDAE defensin-like hybrida
AATCKAECPTWDSVCINKKPCVAC protein 1 CKKAKFSDGHCSKILRRCLCTKEC
VFEKTEATQTETFTKDVNTLAEAL LEADMMV Floral Petunia x 101
MARSICFFAVAILALMLFAAYETE defensin-like hybrida
AGTCKAECPTWEGICINKAPCVKC protein 2 CKAQPEKFTDGHCSKILRRCLCTK
PCATEEATATLANEVKTMAEALVE EDMME Flower- Helianthus 78
MKSSMKMFAALLLVVMCLLANEMG specific annuus GPLVVEARTCESQSHKFKGTCLSD
gamma-thionin TNCANVCHSERFSGGKCRGFRRRC precursor FCTTHC (Defensin
SD2) Gamma-thionin Arabidopsis 77 MKLSMRLISAVLIMFMIFVATGMG homolog
thaliana PVTVEARTCESQSHRFKGTCVSAS At2g02100
NCANVCHNEGFVGGNCRGFRRRCF precursor CTRHC Gamma-thionin Arabidopsis
77 MKFSMRLISAVLFLVMIFVATGMG homolog thaliana
PVTVEARTCASQSQRFKGKCVSDT At2g02120 NCENVCHNEGFPGGDCRGFRRRCF
precursor CTRNC Gamma-thionin Arabidopsis 77
MKLSVRFISAALLLFMVFIATGMG homolog thaliana PVTVEARTCESKSHRFKGPCVSTH
At2g02130 NCANVCHNEGFGGGKCRGFRRRCY precursor CTRHC Gamma-thionin
Arabidopsis 73 MKLSLRLISALLMSVMLLFATGMG homolog thaliana
PVEARTCESPSNKFQGVCLNSQSC At2g02140 AKACPSEGFSGGRCSSLRCYCSKA
precursor C Gamma- Eutrema 80 MAKFASIIALLFAALVLFSAFEAP thionin 1
wasabi SMVEAQKLCEKSSGTWSGVCGNNN precursor ACKNQCINLEGARHGSCNYIFPYH
RCICYFPC gamma- Lycopersicon 105 MARSIFFMAFLVLAMMLFVTYEVE
thionin-like esculentum AQQICKAPSQTFPGLCFMDSSCRK protein
YCIKEKFTGGHCSKLQRKCLCTKP precursor CVFDKISSEVKATLGEEAKTLSEW
LEEEIMME Gastrodianin- Gastrodia 171 MAASASTAVILFFAVTTMMSLSAI MGM
protein elata PAFASDRLNSGHQLDTGGSLAQGG YLFIIQNDCNLVLYDNNRAVWASG
TNGKASGCMLKMQNDGNLVIYSGS RAIWASNTNRQNGNYYLILQRDRN
VVIYDNSNNAIWATHTNVGNAEIT VIPHSNGTAAASGAAQNKVNELYI SMY Gastrodianin-
Gastrodia 171 MAASASTAVILFFAVTTMMSLSAI MNF protein elata
PAFASDRLNSGHQLDTGGSLAQGG YLFIIQNDCNLVLYDNNRAVWASG
TNGKASNCFLKMQNDGNLVIYSGS RAIWASNTNRQNGNYYLILQRDRN
VVIYDNSNNAIWATHTNVGNAEIT VIPHSNGTAAASGAAQNKVNELYI SMY Gastrodianin-
Gastrodia 171 MAASASTAVILFFAVTTVMSLSAI VGM protein elata
PAFASDRLNSGHQLDTGGSLAQGG YLFIIQNDCNLVLYDNNRAVWASG
TNGKASGCMLKMQNDGNLVIYSGS RAIWASNTNRQNGNYYLILQRDRN
VVIYDNSNNAIWATHTNVGNAEIT VIPHSNGTAAASGAAQNKVNELYI SMY Gastrodianin-
Gastrodia 171 MAASASTAVILFFAVTTVMSLSAI VNF protein elata
PAFASDRLNSGHQLDTGGSLAQGG YLFIIQNDCNLVLYDNNRAVWASG
TNGKASNCFLKMQNDGNLVIYSGS RAIWASNTNRQNGNYYLILQRDRN
VVIYDNSNNAIWATHTNVGNAEIT VIPHSNGTAAASGAAQNKVNELYI SMY Genomic DNA,
Arabidopsis 73 MENKFFAAFFLLLVLFSSQEIIGG chromosome 5, thaliana
EGRTCQSKSHHFKYMCTSNHNCAI P1 clone:MBK5 VCRNEGFSGGRCHGFHRRCYCTRL C
Ginkbilobin Ginkgo 40 ANTAFVSSAHNTQKIPAGAPFNRN (GNL) biloba
LRAMLADLRQNAAFAG (Fragment) Hevein Hevea 204
MNIFIVVLLCLTGVAIAEQCGRQA precursor brasiliensis
GGKLCPNNLCCSQWGWCGSTDEYC (Major SPDHNCQSNCKDSGEGVGGGSASN hevein)
VLATYHLYNSQDHGWDLNAASAYC [Contains: STWDANKPYSWRSKYGWTAFCGPV Hevein
GAHGQSSCGKCLSVTNTGTGAKTT (Allergen Hev VRIVDQCSNGGLDLDVNVFRQLDT b
6); Win- DGKGYERGHITVNYQFVDCGDSFN like protein] PLFSVMKSSVIN
hevein-like Euonymus 320 MKYLWVFIVFSIAVLSHACSAQQC antimicrobial
europaeus GRQAGNRRCANNLCCSQYGYCGRT peptide NEYCCTSQGCQSQCRRCGVRTVGE
IVVGDIGGIISKGMFNNILKHRDD DACEGKGFYTYEAFVAAARSFPAF
GSTGDDATRKREIAAFLAQTSHET SAGWPSAPDGPYAWGYCFVRERNP
PSKYCDTTTPCPKSYYGRGPIQLT WNYNYEQAGRAIGADLLNNPDLVA
TDAVISFKTAIWFWMTAQSSKPSC HDVITGSWRPSASDNSVCHVPDYA
VVTNIISGEIEYGKSRNPQVEDRI EFFKRYCQILGVSPGKCYEERTFV
SGLMMETI hevein-like Euonymus 305 MKYLWVFIVFSIAVLSLACSAQQC
antimicrobial europaeus GRQAGNRRCPNNLCCSQFGYCGRT peptide
NEYCCTGFGCQSNCRRCGVRTVGE DVVGDIGGIISKGMFNNILKHRDD
DACEGKGFYTYEAFVAAARSFPAF GSTGDDTTRKREIAAFLAQTSHET
SGGRPSAPDGPYAWGYCFVKERNP PSKYCDTITPCPKSYYGRGPLQLT
WNYNYAQAGRAIGVDLLNNPDLVA TDAVTSFKTAIWFWMTAHSSKPSC
HDVITGSWRPSASDNSVRHVPDYA VVTNIINGEIEYGKSRNPQVEDRI EFFKRYCQILGVSPGKF
Leaf-specific Hordeum 137 MAPSKSIKSVVICVLILGLVLEQV thionin vulgare
QVEGKSCCKDTLARNCYNTCHFAG precursor GSRPVCAGACRCKIISGPKCPSDY (Clone
DB4) PKLNLLPESGEPDVTQYCTIGCRN SVCDNMDNVFRGQEMKFDMGLCSN
ACARFCNDGAVIQSVEA Lectin-like Gastrodia 111
QSSPGILLNQPASMASPASSAVIF protein elata FFAVAALMSLLAMPALAASQLNAG
(Fragment) QTLGTGQSLAQGPNQFIIQNDCNL VLYASNKAVWATGTNGKASGCVLR
MQRDGNLVIYSGSKV Nicotiana Nicotiana 47 RECKTESNTFPGICITKPPCRKAC
Alata Plant tabacum ISEKFTDGHCSKILRRCLCTKPC Defensin 1 (Nad1)
osmotin Nicotiana 250 MSNNMGNLRSSFVFFLLALVTYTY precursor tabacum
AATIEVRNNCPYTVWAASTPIGGG RRLDRGQTWVINAPRGTKMARVWG
RTNCNFNAAGRGTCQTGDCGGVLQ CTGWGKPPNTLAEYALDQFSGLDF
WDISLVDGFNIPMTFAPTNPSGGK CHAIHCTANINGECPRELRVPGGC
NNPCTTFGGQQYCCTQGPCGPTFF SKFFKQRCPDAYSYPQDDPTSTFT
CPGGSTNYRVIFCPNGQAHPNFPL EMPGSDEVAK Osmotin-like Nicotiana 251
MSHLTTFLVFFLLAFVTYTYASGV protein tabacum FEVHNNCPYTVWAAATPVGGGRRL
precursor ERGQSWWFWAPPGTKMARIWGRTN (Patho- CNFDGAGRGWCQTGDCGGVLECKG
genesis- WGKPPNTLAEYALNQFSNLDFWDI related SVIDGFNIPMSFGPTKPGPGKCHG
protein PR- IQCTANINGECPGSLRVPGGCNNP 5D) CTTFGGQQYCCTQGPCGPTELSRW
FKQRCPDAYSYPQDDPTSTFTCTS WTTDYKVMFCPYGSAHNETTNFPL EMPTSTHEVAK
Osmotin-like Lycopersicon 238 FFFLLAFVTYTYAATFEVRNNCPY protein
TPM-1 esculentum TVWAASTPIGGGRRLDRGQTWVIN precursor (PR
APRGTKMARIWGRTNCNFDGDGRG P23) SCQTGDCGGVLQCTGWGKPPNTLA (Fragment)
EYALDQFSNLDFWDISLVDGFNIP MTFAPTNPSGGKCHAIHCTANING
ECPGSLRVPGGCNNPCTTFGGQQY CCTQGPCGPTDLSRFFKQRCPDAY
SYPQDDPTSTFTCPSGSTNYRVVF CPNGVTSPNFPLEMPSSDEEAK pathogenesis-
Lycopersicon 233 AFVTYTYAATFEVRNNCPYTVWAA related esculentum
STPIGGGRRLDRGQTWVINAPRGT protein P23 KMARIWGRTNCNFDGAGRGSCQTG
precursor DCGGVLQCTGWGKPPNTLAEYALD QFSNLDFWDISLVDGFNIPMTFAP
TNPSGGKCHAIHCTANINGECPGS LRVPGGCNNPCTTFGGQQYCCTQG
PCGPTDLSRFFKQRCPDAYSYPQD DPTSTFTCPSGSTNYRVVFCPNGV TSPNFPLEMPSSDEEAK
plant Arabidopsis 76 MKVSPRLNSALLLLFMILATVMGL defensin thaliana
VTVEARTCETSSNLFNGPCLSSSN protein, CANVCHNEGFSDGDCRGFRRRCLC putative
TRPC (PDF2.4) plant Arabidopsis 122 MERIPSLASLVSLLIIFATVVNQT
defensin- thaliana RASICNDRLGLCDGCDQRCKAKHG fusion
PSCESKCDGPVGMLLCTCTYECGP protein, TKLCNGGLGNCGESCNEQCCDRNC putative
AQRYNGGHGYCNTLDDFSLCLCKY PC Plant Pyrus 81 LVSTAFVLVLLLATIEMGPMGVEA
defensin-like pyrifolia RTESSKAVEGKICEVPSTLFKGLC protein
FSSNNCKHTCRKEQFTRGHCSVLT (Fragment) RACVCTKKC probable Arabidopsis
80 MAKFCTTITLILVALVLFADFEAP antifungal thaliana
TIVKAELCKRESETWSGRCVNDYQ protein CRDHCINNDRGNDGYCAGGYPWYR
[imported] SCFCFFSC Probable Arabidopsis 80
MAKSAAIITFLFAALVLFAAFEAP cysteine-rich thaliana
IMVEAQKLCEKPSGTWSGVCGNSN antifungal ACKNQCINLEGAKHGSCNYVFPAH
protein KCICYFPC At2g26010 precursor (AFP) Probable Arabidopsis 80
MAKFASIITFIYAALVLFAAFEVP cysteine-rich thaliana
TMVEAQKLCEKPSGTWSGVCGNSN antifungal ACKNQCINLEGAKHGSCNYVFPAH
protein KCICYVPC At2g26020 precursor (AFP) Probable Arabidopsis 80
MAKFASIITLIFAALVLFAAFDAP cysteine-rich thaliana
AMVEAQKLCEKPSGTWSGVCGNSN antifungal ACKNQCINLEGAKHGSCNYVFPAH
protein LCR77 KCICYVPC precursor (AFP) Protease Pyrus 87
MEPSMRLISAAFVLILLLATTEMG inhibitor- pyrifolia
PMGVEAKSKSSKEVEKRTCEAASG like protein KFKGMCFSSNNCANTCAREKFDGG
KCKGFRRRCMCTKKC Protease Pyrus 87 MERSMRLVSAAFVLVLLLAATEMG
inhibitor- pyrifolia PMGVEARTESSKAVEGKICEVPST like protein
LFKGLCFSSNNCKHTCRKEQFTRG HCSVLTRACVCTKKC Proteinase Capsicum 78
MAHSMRFFAIVLLLAMLVMATEMG inhibitor annuum PMRIVEARTCESQSHRFKGVCASE
precursor TNCASVCQTEGFSGGDCRGFRRRC FCTRPC Putative Arabidopsis 78
MASSYTLMLFLCLSIFLIASTEMM defensin AMP1 thaliana
AVEGRICERRSKTWTGFCGNTRGC protein DSQCKRWERASHGACHAQFPGFAC FCYFNC
Putative Picea abies 83 MADKGVGSRLSALFLLVLLVISIG plant
MMQLEPAEGRTCKTPSGKFKGVCA defensin SRNNCKNVCQTEGFPSGSCDFHVA SPI1B
NRKCYCSKPCP sormatin Sorghum 22 AVFTVVNRCPYTVWAASVPVGG bicolor TOM
P14A Lycopersicon 41 AVHNDARAQVGVGPMSXDANLASR protein esculentum
AQNYANSRAXDXNLIXS (Fragment) TOM P14B Lycopersicon 35
DXLAVHNDARAQVGAGPMDANLAS pathogenesis- esculentum RAQNXANSRAG
related PR-1 protein (Fragments) TOM P14C Lycopersicon 97
DYLNAHNAARRQVGVGPMTXDNRL pathogenesis- esculentum
AAFAQNYANQRADXRMQHSGGPYG related PR-1 ENLAAAFPQLNCQAGKVCGHYTQV
protein VWRNSVRLGCARVRCNNGWYFITC (Fragments) N trimatin Triticum 23
ATITVVNRCSYTVWPGALPGGGA aestivum Vicilin Macadamia 666
MAINTSNLCSLLFLLSLFLLSTTV integrifolia SLAESEFDRQEYEECKRQCMQLET
SGQMRRCVSQCDKRFEEDIDWSKY DNQDDPQTDCQQCQRRCRQQESGP
RQQQYCQRRCKEICEEEEEYNRQR DPQQQYEQCQERCQRHETEPRHMQ
TCQQRCERRYEKEKRKQQKRYEEQ QREDEEKYEERMKEEDNKRDPQQR
EYEDCRRRCEQQEPRQQYQCQRRC REQQRQHGRGGDLINPQRGGSGRY
EEGEEKQSDNPYYFDERSLSTRFR TEEGHISVLENFYGRSKLLRALKN
YRLVLLEANPNAFVLPTHLDADAI LLVTGGRGALKMIHRDNRESYNLE
CGDVIRIPAGTTFYLINRDNNERL HIAKFLQTISTPGQYKEFFPAGGQ
NPEPYLSTFSKEILEAALNTQAER LRGVLGQQREGVIISASQEQIREL
TRDDSESRRWHIRRGGESSRGPYN LFNKRPLYSNKYGQAYEVKPEDYR
QLQDMDVSVFIANITQGSMMGPFF NTRSTKVVVVASGEADVEMACPHL
SGRHGGRRGGKRHEEEEDVHYEQV KARLSKREAIVVPVGHPVVFVSSG
NENLLLFAFGINAQNNHENFLAGR ERNVLQQIEPQAMELAFAAPRKEV
EELFNSQDESIFFPGPRQHQQQSS RSTKQQQPLVSILDFVGF Vicilin Macadamia 666
MAINTSNLCSLLFLLSLFLLSTTV integrifolia SLAESEFDRQEYEECKRQCMQLET
SGQMRRCVSQCDKRFEEDIDWSKY DNQEDPQTECQQCQRRCRQQESGP
RQQQYCQRRCKEICEEEEEYNRQR DPQQQYEQCQKHCQRRETEPRHMQ
TCQQRCERRYEKEKRKQQKRYEEQ QREDEEKYEERMKEEDNKRDPQQR
EYEDCRRRCEQQEPRQQHQCQLRC REQQRQHGRGGDMMNPQRGGSGRY
EEGEEEQSDNPYYFDERSLSTRFR TEEGHISVLENFYGRSKLLRALKN
YRLVLLEANPNAFVLPTHLDADAI LLVIGGRGALKMIHHDNRESYNLE
CGDVIRIPAGTTFYLINRDNNERL HIAKFLQTISTPGQYKEFFPAGGQ
NPEPYLSTFSKEILEAALNTQTEK LRGVFGQQREGVIIRASQEQIREL
TRDDSESRHWHIRRGGESSRGPYN LFNKRPLYSNKYGQAYEVKPEDYR
QLQDMDLSVFIANVTQGSMMGPFF NTRSTKVVVVASGEADVEMACPHL
SGRHGGRGGGKRHEEEEDVHYEQV RARLSKREAIVVLAGHPVVFVSSG
NENLLLFAFGINAQNNHENFLAGR ERNVLQQIEPQAMELAFAAPRKEV
EESFNSQDQSIFFPGPRQHQQQSP RSTKQQQPLVSILDFVGF Vicilin Macadamia 625
QCMQLETSGQMRRCVSQCDKRFEE (Fragment) integrifolia
DIDWSKYDNQEDPQTECQQCQRRC RQQESDPRQQQYCQRRCKEICEEE
EEYNRQRDPQQQYEQCQKRCQRRE TEPRHMQICQQRCERRYEKEKRKQ
QKRYEEQQREDEEKYEERMKEGDN KRDPQQREYEDCRRHCEQQEPRLQ
YQCQRRCQEQQRQHGRGGDLMNPQ RGGSGRYEEGEEKQSDNPYYFDER
SLSTRFRTEEGHISVLENFYGRSK LLRALKNYRLVLLEANPNAFVLPT
HLDADAILLVIGGRGALKMIHRDN RESYNLECGDVIRIPAGTTFYLIN
RDNNERLHIAKFLQTISTPGQYKE FFPAGGQNPEPYLSTFSKEILEAA
LNTQTERLRGVLGQQREGVIIRAS QEQIRELTRDDSESRRWHIRRGGE
SSRGPYNLFNKRPLYSNKYGQAYE VKPEDYRQLQDMDVSVFIANITQG
SMMGPFFNTRSTKVVVVASGEADV
EMACPHLSGRHGGRGGGKRHEEEE EVHYEQVRARLSKREAIVVLAGHP
VVFVSSGNENLLLFAFGINAQNNH ENFLAGRERNVLQQIEPQAMELAF
AASRKEVEELFNSQDESIFFPGPR QHQQQSPRSTKQQQPLVSILDFVG F Wheatwin1
Triticum 146 MAARPMLVVALLCAAAAAATAQQA precursor aestivum
TNVRATYHYYRPAQNNWDLGAPAV (Patho- SAYCATWDASKPLSWRSKYGWTAF genesis-
CGPAGAHGQASCGKCLQVTNPATG related AQITARIVDQCANGGLDLDWDTVF protein
4a) TKIDTNGIGYQQGHLNVNYQFVDC (Protein RD 0.14) Wheatwin2 Triticum
148 MTMAARLMLVAALLCAAAAAATAQ precursor aestivum
QATNVRATYHYYRPAQNNWDLGAP (Patho- AVSAYCATWDASKPLSWRSKYGWT genesis-
AFCGPAGAHGQAACGKCLRVTNPA related TGAQITARIVDQCANGGLDLDWDT protein
4b) VFTKIDTNGIGYQQGHLNVNYQFV DCRD Zeamatin Zea mays 206
AVFTVVNQCPFTVWAASVPVGGGR QLNRGESWRITAPAGTTAARIWAR
TGCKFDASGRGSCRTGDCGGVLQC TGYGRAPNTLAEYALKQFNNLDFF
DISLIDGFNVPMSFLPDGGSGCSR GPRCAVDVNARCPAELRQDGVCNN
ACPVFKKDEYCCVGSAANDCHPTN YSRYFKGQCPDAYSYPKDDATSTF TCPAGTNYKVVFCP
Zeamatin Zea mays 227 MAGSVAIVGIFVALLAVAGEAAVF precursor
TVVNQCPFTVWAASVPVGGGRQLN RGESWRITAPAGTTAARIWARTGC
KFDASGRGSCRTGDCGGVLQCTGY GRAPNTLAEYALKQFNNLDFFDIS
LIDGFNVPMSFLPDGGSGCSRGPR CAVDVNARCPAELRQDGVCNNACP
VFKKDEYCCVGSAANDCHPTNYSR YFKGQCPDAYSYPKDDATSTFTCP AGTNYKVVFCP
[0078] TABLE-US-00004 TABLE 2 {PRIVATE} Defensins Name Organism
Sequence HNP-1 Human ACYCRIPACIAGERRYGTCIYQGRLWAFCC HNP-2 Human
CYCRIPACIAGERRYGTCIYQGRLWAFCC HNP-3 Human
DCYCRIPACIAGERRYGTCIYQGRLWAFCC HNP-4 Human
VCSCRLVFCRRTELRVGNCLIGGVSFTYCCTRV NP-1 Rabbit
VVCACRRALCLPRERRAGFCRIRGRIHPLCCRR NP-2 Rabbit
VVCACRRALCLPLERRAGFCRIRGRIHPLCCRR NP-3A Rabbit
GICACRRRFCPNSERFSGYCRVNGARYVRCCSRR NP-3B Rabbit
GRCVCRKQLLCSYRERRIGDCKIRGVRFPFCCPR NP-4 Rabbit
VSCTCRRFSCGFGERASGSCTVNGVRHTLCCRR NP-5 Rabbit
VFCTCRGFLCGSGERASGSCTINGVRHTLCCRR RatNP-1 Rat
VTCYCRRTRCGFRERLSGACGYRGRIYRLCCR Rat-NP-3 Rat
CSCRYSSCRFGERLLSGACRLNGRIYRLCC Rat-NP-4 Rat
ACTCRIGACVSGERLTGACGLNGRIYRLCCR GPNP Guinea pig
RRCICTTRTCRFPYRRLGTCIFQNRVYTFCC
[0079] B. Growth Factors
[0080] In some embodiments of the present invention, trophic factor
combinations for treating injured nervous systems comprise one or
more growth factors. Growth factors useful in the present invention
include, but are not limited to, the following broad classes of
cytoactive compounds: Insulin, Insulin like growth factors such as
IGF-I, IGF-IB, IGF-II, and IGF-BP; Heparin-binding growth factors
such as Pleiotrophin (NEGF1) and Midkine (NEGF2); PC-cell derived
growth factors (PCDGF); Epidermal Growth Factors such as
.alpha.-EGF and .beta.-EGF; EGF-like molecules such as
Keratinocyte-derived growth factor (which is identical to KAF,
KDGF, and amphiregulin) and vaccinia virus growth factor (VVGF);
Fibroblast Growth Factors such as FGF-1 (Basic FGF Protein), FGF-2
(Acidic FGF Protein), FGF-3 (Int-2), FGF-4 (Hst-1), FGF-5, FGF-6,
and FGF-7 (identical to KGF); FGF-Related Growth Factors such as
Endothelial Cell Growth Factors (e.g., ECGF-.alpha. and
ECGF-.beta.); FGF- and ECGF-Related Growth Factors such as
Endothelial cell stimulating angiogenesis factor and Tumor
angiogenesis factor, Retina-Derived Growth Factor (RDGF), Vascular
endothelium growth factors (VEGF, VEGF-B, VEGF-C, and VEGF-D),
Brain-Derived Growth Factor (BDGF A- and -B), Astroglial Growth
Factors (AGF 1 and 2), Omentum-derived factor (ODF),
Fibroblast-Stimulating factor (FSF), and Embryonal
Carcinoma-Derived Growth Factor; Neurotrophic Growth Factors such
as .alpha.-NGF, .beta.-NGF, .gamma.-NGF, Brain-Derived Neurotrophic
Factor (BDNF), Neurotrophin-3, Neurotrophin-4, and Ciliary
Nuerotrophic Factor (CNTF); Glial Growth Factors such as GGF-I,
GGF-II, GGF-III, Glia Maturation Factor (GMF), and Glial-Derived
Nuerotrophic Factor (GDNF); Organ-Specific Growth Factors such as
Liver Growth Factors (e.g., Hepatopoietin A, Hepatopoietin B, and
Hepatocyte Growth Factors (HCGF or HGF), Prostate Growth Factors
(e.g., Prostate-Derived Growth Factors [PGF] and Bone
Marrow-Derived Prostate Growth Factor), Mammary Growth Factors
(e.g., Mammary-Derived Growth Factor 1 [MDGF-1] and Mammary
Tumor-Derived Factor [MTGF]), and Heart Growth Factors (e.g.,
Nonmyocyte-Derived Growth Factor [NMDGF]); Cell-Specific Growth
Factors such as Melanocyte Growth Factors (e.g.,
Melanocyte-Stimulating Hormone [.alpha.-, .beta.-, and .gamma.-MSH]
and Melanoma Growth-Stimulating Activity [MGSA]), Angiogenic
Factors (e.g., Angiogenin, Angiotropin, Platelet-Derived ECGF,
VEGF, and Pleiotrophin), Transforming Growth Factors (e.g.,
TGF-.alpha., TGF-.beta., and TGF-like Growth Factors such as
TGF-.beta..sub.2, TGF-.beta..sub.3, TGF-e, GDF-1, GDF-9, CDGF and
Tumor-Derived TGF-.beta.-like Factors), ND-TGF, and Human
epithelial transforming factor [h-TGFe]); Regulatory Peptides with
Growth Factor-like Properties such as Bombesin and Bombesin-like
peptides (e.g., Ranatensin, and Litorin], Angiotensin, Endothelin,
Atrial Natriuretic Factor, Vasoactive Intestinal Peptide, and
Bradykinin; Cytokines such as connective tissue growth factor
(CTGF), the interleukins IL-1 (e.g., Osteoclast-activating factor
(OAF), Lymphocyte-activating factor (LAF), Hepatocyte-stimulating
factor (HSF), Fibroblast-activating factor (FAF), B-cell-activating
factor (BAF), Tumor inhibitory factor 2 (TIF-2),
Keratinocyte-derived T-cell growth factor (KD-TCGF)), IL-2 (T-cell
growth factor (TCGF), T-cell mitogenic factor (TCMF)), IL-3 (e.g.,
Hematopoietin, Multipotential colony-stimulating factor
(multi-CSF), Multilineage colony-stimulating activity (multi-CSA),
Mast cell growth factor (MCGF), Erythroid burst-promoting activity
(BPA-E), IL-4 (e.g., B-cell growth factor I (BCGF-I), B-cell
stimulatory factor I (BSF-1)), IL-5 (e.g., B-cell growth factor II
(BCGF-II), Eosinophil colony-stimulating factor (Eo-CSF),
Immunoglobulin A-enhancing factor (IgA-EF), T-cell replacing factor
(TCRF)), IL-6 (B-cell stimulatory factor 2 (BSF-2), B-cell
hybridoma growth factor (BCHGF), Interferon .beta..sub.2 (IFN-B),
T-cell activating factor (TAF), IL-7 (e.g., Lymphopoietin 1 (LP-1),
Pre-B-cell growth factor (pre-BCGF)), IL-8 (Monocyte-derived
neutrophil chemotacetic factor (MDNCF), Granulocyte chemotatic
factor (GCF), Neutrophil-activating peptide 1 (NAP-1), Leukocyte
adhesion inhibitor (LAI), T-lymphocyte chemotacetic factor (TLCF)),
IL-9 (e.g., T-cell growth factor III (TCGF-III), Factor P40,
MegaKaryoblast growth factor (MKBGF), Mast cell growth enhancing
activity (MEA or MCGEA)), IL-10 (e.g., Cytokine synthesis
inhibitory factor (CSIF)), IL-11 (e.g., Stromal cell-derived
cytokine (SCDC)), IL-12 (e.g., Natural killer cell stimulating
factor (NKCSF or NKSF), Cytotoxic lymphocyte maturation factor
(CLMF)), TNF-.alpha. (Cachectin), TNF-.beta. (Lymphotoxin), LIF
(Differentiation-inducing factor (DIF), Differentiation-inducing
activity (DIA), D factor, Human interleukin for DA cells (HILDA),
Hepatocyte stimulating factor III (HSF-III), Cholinergic neuronal
differentiation factor (CNDF), CSF-1 (Macrophage colony-stimulating
factor (M-CSF)), CSF-2 (Granulocyte-macrophage colony-stimulating
factor (GM-CSF)), CSF-3 (Granulocyte colony-stimulating factor
(G-CSF)), and erythropoietin; Platelet-derived growth factors
(e.g., Placental growth factor (PlGF), PDGF-A, PDGF-B, PDGF-AB,
p28-sis, and p26-cis), and Bone Morphogenetic proteins (e.g., BMP
and BMP-15), neuropeptides (e.g., Substance P, calcitonin
gene-regulated peptide, and neuropeptide Y), and neurotransmitters
(e.g., norepinephrine and acetylcholine).
[0081] Suitable growth factors may be obtained from commercial
sources, purified from natural sources, or be produced by
recombinant methods. Recombinant growth factors can be produced
from wild-type coding sequences or from variant sequences that
encode functional growth factors. Suitable growth factors also
include analogs that may be smaller peptides or other molecules
having similar binding and biological activity as the natural
growth factors. Methods for producing growth factors are described
in U.S. Pat. Nos. 5,183,805; 5,218,093; 5,130,298; 5,639,664;
5,457,034; 5,210,185; 5,470,828; 5,650,496; 5,998,376; and
5,410,019; all of which are incorporated herein by reference.
[0082] C. Neurotrophins
[0083] The trophic factor combinations provided herein also can
include one or more neurotrophic growth factors such as
Brain-Derived Neurotrophic Factor (BDNF), Neurotrophin-3,
Neurotrophin-4, and Ciliary Nuerotrophic Factor (CNTF).
[0084] Nerve growth factor s, such as .alpha.-NGF, .beta.-NGF,
.gamma.-NGF, and the like, are neurotrophins. In an embodiment, the
trophic factor combination does not include a nerve growth factor,
which results in lessened pain.
[0085] D. Neuropeptides
[0086] The trophic factor combinations provided herein also can
include one or more neuropeptides, e.g., PBAN-type neuropeptides
(e.g., Diapause hormone homolog (DH); Alpha-SG neuropeptide
(MAB-alpha-NP); Beta-SG neuropeptide (MAB-beta-NP)); Pheromone
biosynthesis activating neuropeptide (M); PBAN-type neuropeptides
(e.g., Diapause hormone (DH); Alpha-SG neuropeptide (Alpha-SGNP);
Beta-SG neuropeptide (Beta-SGNP); Pheromone biosynthesis activating
neuropeptide I (PBAN-I) (BoM)); Neuropeptides B/W receptor type 2
(G protein-coupled receptor 8); Neuropeptides B/W receptor type 1
(G protein-coupled receptor 7); Neuropeptides B/W receptor type 1
(G protein-coupled receptor 7) (Fragment); neuropeptides
[similarity]; Glucagon-family neuropeptides (e.g., Growth
hormone-releasing factor (GRF) (Growth hormone-releasing hormone)
(GHRH); Pituitary adenylate cyclase activating polypeptide
(PACAP)); Pol-RFamide neuropeptides; Antho-RFamide neuropeptides
type 1; LWamide neuropeptides (e.g., LWamide I; Metamorphosin A
(LWamide II) (MMA); LWamide III; LWamide IV; LWamide V; LWamide VI;
LWamide VII; LWamide VIII; LWamide IX); Antho-RFamide neuropeptides
type 2; Glucagon-family neuropeptides (e.g., Growth
hormone-releasing factor (GRF) (Growth hormone-releasing hormone)
(GHRH); Pituitary adenylate cyclase activating polypeptide-27
(PACAP-27) (P)); Glucagon-family neuropeptides (e.g., Growth
hormone-releasing factor (GRF) (Growth hormone-releasing hormone)
(GHRH); Pituitary adenylate cyclase activating polypeptide-27
(PACAP-27) (P)); LWamide neuropeptides (e.g., LWamide I; LWamide
II; LWS); Glucagon-family neuropeptides (e.g., Growth
hormone-releasing factor (GRF) (Growth hormone-releasing hormone)
(GHRH); Pituitary adenylate cyclase activating polypeptide
(PACAP)]; FMRFamide-like neuropeptides); PBAN-type neuropeptides
(e.g., Diapause hormone homolog (DH); Alpha-SG neuropeptide;
Beta-SG neuropeptide); Pheromone biosynthesis activating
neuropeptide (AgI-PBAN); Gamma-SG neuropeptide; FMRFamide-related
neuropeptides; Myomodulin neuropeptides (e.g., GLQMLRL-amide;
QIPMLRL-amide; SMSMLRL-amide; SLSMLRL-amide; Myomodulin A
(PMSMLRL-amide)); FMRFamide neuropeptides; neuropeptides (e.g.,
Substance P, calcitonin gene-regulated peptide, and neuropeptide
Y); LWamide neuropeptides (e.g., LWamide I; LWamide II; LWamide
III; LWamide IV; LWamide V; LWamide VI; Metamorphosin A (MMA);
Mwamide) (Fragment); PBAN-type neuropeptides (e.g., Diapause
hormone homolog (DH); Alpha-SG neuropeptide; Beta-SG neuropeptide);
Pheromone biosynthesis activating neuropeptide (HeA-PBAN); Gamma-SG
neuropeptide; Antho-RFamide neuropeptides; Neuropeptides capa
receptor (Cap2b receptor); Neuropeptides B/W receptor type 2 (G
protein-coupled receptor 8); Neuropeptides B/W receptor type 1 (G
protein-coupled receptor 7); FMRFamide-like neuropeptides [e.g.,
Neuropeptide AF 10 (GFGDEMSMPGVLRF-amide); Neuropeptide AF20
(GMPGVLRF-amide); Neuropeptide AF3 (AVPGVLRF-amide); Neuropeptide
AF4 (GDVPGVLRF-amide); N PBAN-type neuropeptides [e.g., Diapause
hormone homolog (DH); Alpha-SG neuropeptide; Beta-SG neuropeptide;
Pheromone biosynthesis activating neuropeptide (HeZ-PBAN); Gamma-SG
neuropeptide; FMRFamide neuropeptides type FMRF-1 (Fragment);
Abdominal ganglion neuropeptides L5-67 (e.g., Luqin; Luqin-B;
Luqin-C; Proline-rich mature peptide (PRMP)); FMRFamide
neuropeptides type FMRF-2; FMRFamide neuropeptides type FMRF-4
(Fragment); Myomodulin neuropeptides (e.g., Myomodulin A (MM-A)
(PMSMLRL-amide) (Neuron B16 peptide); Myomodulin B (MM-B)
(GSYRMMRL-amide); Myomodulin D (MM-D) (GLSMLRL-amide); Myomodulin F
(MM-F); LWamide neuropeptides (e.g., LWamide I; LWamide II;
Metamorphosin A (MMA); Iwamide) (Fragment) (Substance P, calcitonin
gene-regulated peptide, and neuropeptide Y.)
[0087] E. Other Components
[0088] The trophic factor combinations can be used with various
delivery systems. In some embodiments, the trophic factor
combination is mixed with a viscous substance to increase the
viscosity of the combination. The increased viscosity retains the
trophic factor combination at the site of the injury longer than it
would be retained in the absence of the viscous substance. The
viscous substance can be, for example, a polysaccharide, such as
hyaluranic acid.
[0089] In another embodiment, the trophic factor combination is
delivered in a slow release formula, such as in a matrix, for
example, a woundhealing matrix, either with or without a viscous
substance. In an embodiment, the matrix is a hydrogel, such as a
hydrogel disclosed in U.S. Patent Application No. US 20030083389A1,
which describes hydrogels wherein a polymer matrix is modified to
contain a bifunctional poly(alkylene glycol) molecule covalently
bonded to the polymer matrix. The hydrogels can be cross-linked
using, for example, glutaraldehyde. The hydrogels can also be
crosslinked via an interpenetrating network of a photopolymerizable
acrylates. In one embodiment of the invention, the components of
the trophic factor combination are incorporated into the hydrogel,
for example, through covalent bonds to poly(alkylene glycol)
molecules of the hydrogel or through entrainment within the
hydrogel. In other embodiments, the matrix is a collagen gel
matrix, which can be impregnated with a trophic factor combination.
Other matrices can also be used.
[0090] The trophic factor combination can also be delivered in a
base solution, such as UW solution (DuPont Critical Care, Waukegan,
Ill.), or other base solutions.
[0091] The neurochemical combinations can be used in conjunction
with cell therapy, where transfected cells are produced to release
the ingredients and obtain continual delivery of a trophic factor
combination. For example, embryonic or adult stem cells can be
modified to express trophic factors, antimicrobial peptides, and
other relevant neurochemicals, to deliver the trophic factor
combination endogenously to the injured spinal cord. In the case of
genetically modified cell transplants, the transfected cells can be
tagged with cell surface antigens so that the cells can be
controlled. For example, antibodies targeting the specific antigen
could be used to kill the implanted cells after therapeutic results
have been achieved.
[0092] Delivery of the neurochemical combinations can also be
achieved by media with spaced supports, such as sponges, gels, or
biopolymers.
[0093] F. Exemplary Formulations
[0094] A trophic factor combination includes one or more
antimicrobial peptide and/or one or more substance having an
antimicrobial peptide effect, alone or with one or more of the
following trophic factors: growth factors, neuropeptides, and
neurotrophins. Another trophic factor combination includes a
viscous substance, such as hyaluronic acid, among others. Another
trophic factor combination includes other cytoactive compounds,
such as one or more cytokine and/or one or more chemokine.
Non-limiting examples of these trophic factor combinations are
provided in Tables 3a-3h below. It will be recognized that the
trophic factor combinations can comprise one or more antimicrobial
polypeptides (e.g., a defensin such as BNP-1). The trophic factor
combinations described below can also comprise one or more trophic
factors above. Accordingly, in some preferred embodiments, the
trophic factor combination is supplemented with one or more of the
following trophic factors: trehalose (Sigma, St. Louis Mo.; e.g.,
about 15 mM), substance P (Sigma; e.g., about 10 .mu.g/ml), IGF-1
(Collaborative Biologicals; e.g., about 10 ng/ml), EGF (Sigma;
e.g., about 10 ng/ml), and BDNF (2 .mu.g/ml). In some preferred
embodiments, the trophic factor combination is also supplemented
with insulin (1-200 units, preferably 40 units) prior to use. In
some embodiments, an antimicrobial polypeptide is not included in
the trophic factor combination.
[0095] In some exemplary embodiments, EGF and/or IGF-1 are included
in the trophic factor combination at a concentration of about 1
ng/ml to about 100 ng/ml, most preferably about 10 ng/ml. In other
exemplary embodiments, substance P is included at a concentration
of about 0.1 .mu.g/ml to about 100 .mu.g/ml, most preferably about
2.5 .mu.g/ml.
[0096] It will be recognized that the Tables below provide
formulations that are exemplary and non-limiting. For example,
alterations in the specific substances used and the number of those
substances are all within the scope of the invention. In some
embodiments, the antimicrobial polypeptide and/or substance having
an antimicrobial peptide effect and/or one or more trophic factor,
are provided in stable form that can be reconstituted. Methods for
stabilization include, for example, lyophilization. In embodiments
where the antimicrobial polypeptide and/or one or more growth
factors are provided in lyophilized form, they can conveniently
reconstituted prior to use, for example, in sterile water or in an
aliquot of a base medium (e.g., UW solution), prior to addition to
a base medium (e.g., hyaluronic acid, UW solution).
[0097] Alternatively, the at least one microbial polypeptide and/or
one or more trophic factor can be provided as a separate
composition (i.e., a "bullet") that is added to a base medium. In
preferred embodiments, the bullet contains an antimicrobial peptide
and/or a substance having an antimicrobial peptide effect and/or
one or more trophic factor as described above. In some embodiments,
the bullet contains an antimicrobial peptide and/or a substance
having an antimicrobial peptide effect and/or one or more of the
trophic factor as described above in concentrations that provide
the appropriate concentration when added to a specific volume of
the base medium, where used. TABLE-US-00005 TABLE 3a Component Type
Substance Antimicrobial peptide BNP-1
[0098] TABLE-US-00006 TABLE 3b Component Type Substance
Antimicrobial peptide BNP-1 Growth factor IGF-1
[0099] TABLE-US-00007 TABLE 3c Component Type Substance
Antimicrobial peptide BNP-1 Neuropeptide Substance P
[0100] TABLE-US-00008 TABLE 3d Component Type Substance
Antimicrobial peptide BNP-1 Neurotrophin BDNF
[0101] TABLE-US-00009 TABLE 3e Component Type Substance
Antimicrobial peptide BNP-1 Growth factor IGF-1 Neuropeptide
Substance P
[0102] TABLE-US-00010 TABLE 3f Component Type Substance
Antimicrobial peptide BNP-1 Growth factor IGF-1 Neurotrophin
BDNF
[0103] TABLE-US-00011 TABLE 3g Component Type Substance
Antimicrobial peptide BNP-1 Neuropeptide Substance P Neurotrophin
BDNF
[0104] TABLE-US-00012 TABLE 3h Component Type Substance
Antimicrobial peptide BNP-1 Growth factor IGF-1 Neuropeptide
Substance P Neurotrophin BDNF
[0105] It is contemplated that the trophic factor combination can
be provided in a pre-formulated form, such as in a kit format. The
kit can include (1) at least one of an antimicrobial peptide and a
substance having an antimicrobial peptide effect and (2) a
neurotrophin. The kit can also include a viscous substance. At
least one of a growth factor and a neuropeptide can also be
included.
II. Uses of Trophic Factor Combinations and Their Individual
Components
[0106] It is contemplated that the trophic factor combinations and
their individual components described above may be utilized in a
variety of procedures related to injury to the nervous system and
other medical procedures. It is contemplated that the trophic
factor combinations and their individual components can be used for
the treatment of any part of the nervous system, including the
central nervous system and the peripheral nervous system.
[0107] In one embodiment, the trophic factor combinations or one or
more of their individual components are used during surgery of the
disc and/or other portions of the nervous system. In an embodiment,
a trophic factor combination or one or more of their individual
components applied to surgical hardware and/or other implants, such
as surgical screws, plates, pins, clamps, wires, pins, rods, nails,
probes, spinal fixation devices, and the like. In another
embodiment, a trophic factor combination or one or more of their
individual components is applied directly during surgery, such as
to a surgical opening, for example, an incision, a section, or any
other opening. In one embodiment, a trophic factor combination or
one or more of their individual components is applied to one or
more tissue, nerve, organ, or cavity. A trophic factor combination
or one or more of their individual components can also be applied
to a surgical instrument such that when the instrument is used, the
trophic factor combination or one or more of their individual
components is delivered to injury and/or surrounding tissue, fluid,
organ, and the like.
[0108] In use, an injury to the nervous system is identified. At
least one component of the trophic factor combination is applied to
the injury to the nervous system.
[0109] In some embodiments, the trophic factor combinations can be
utilized to reduce body weight loss post injury in injured animals
treated with the combination when compared to injured animals not
treated with the trophic factor combination. Preferably, the
decrease in loss of body weight is improved by at least 25% and
more preferably by at least 50% as compared to animals not
receiving the trophic factor combination. In some embodiments, the
trophic factor combinations are used to strengthen motor recovery
in injured animals treated with the trophic factor combination when
compared to injured animals not treated with the trophic factor
combination. In some embodiments, the trophic factor combinations
are used to increase evoked potential amplitudes in injured animals
treated with the trophic factor combination when compared to
injured animals not treated with the trophic factor combination. In
some embodiments, the trophic factor combinations are used to lower
the current required to evoke a response (threshold current) in
injured animals treated with the trophic factor combination when
compared to injured animals not treated with the trophic factor
combination. Application of the trophic factor combination
according to the invention can also have at least one of the
following additional effects: reduced pain in the animal, a
neuroprotective effect, triggered neuronal plasticity, reduced
inflammation, and growth of new cells.
EXAMPLES
[0110] The following examples serve to illustrate certain preferred
embodiments and aspects of the present invention and are not to be
construed as limiting the scope thereof.
Example 1
Materials and Methods
[0111] Experiments were performed on 3-5 month old male
Sprague-Dawley (SD) and Lewis rats that were housed individually
with free access to food and water. Rats were placed into four
groups: 1) spinally injured SD rats without a trophic factor
combination administered (n=8), 2) spinally injured SD rats with a
trophic factor combination (n=2); 3) spinally injured Lewis rats
without a trophic factor combination administered (n=5), and 4)
spinally injured Lewis rats with a trophic factor combination
administered (n=2).
[0112] Spinal cord injury. Rats were anesthetized with medetomidine
(75 .mu.g/kg i.m.) and isoflurane in oxygen. After oro-tracheal
intubation, anesthesia was maintained with isoflurane in oxygen and
rats were mechanically ventilated. A laminectomy was made at the
second cervical vertebral level to allow the second cervical spinal
segment and the cranial segment of the third cervical spinal
segment to be exposed. A 1-mm-long left-sided hemisection was made
in the cranial segment of C.sub.2 and the section aspirated with a
fine tipped glass pipette. The surgical wound was closed using
standard techniques. All animals were allowed to recover and
received atipamezole (0.1 mg/kg i.v.) to antagonize the anesthetic
effects of medetomidine. Buprenorphine (50 .mu.g/kg i.v.) and
carprofen (5 mg/kg i.v.) were administered for postsurgical pain
control. Analgesics were repeated as required over the next 2
days.
[0113] Trophic Factor Combination. The trophic factor combination
(also referred to as the trophic factor combination) was made by
adding 10 ug of BNP-1 (bactenecin), 100 ng of insulin-like growth
factor (IGF-1), and 25 mg of Substance P to 200 ul of distilled
water.
[0114] Trophic factor combination administration. Prior to closure
of the surgical wound, hyaluronic acid (Hylartin V, sodium
hyalurate) (10%) was added to the neurotrophin mixture to thicken
the solution and improve retention at the site of spinal injury.
Two ug of BDNF was added to 0.4-0.45 ml of the mixture. The mixture
(0.4-0.45 ml) was then administered using a syringe and 22-gauge
needle into the hemisection cavity. The wound was closed
immediately after injection.
[0115] Experimental preparation. Two weeks after surgical spinal
injury, respiratory motor output was measured from both phrenic
nerves using two distinct experimental techniques. First,
spontaneous (brain-stem driven) phrenic motor activity was measured
in anesthetized rats during standardized conditions. Second,
spontaneous activity was removed by hyperventilating the rats and
evoke potentials were elicited by spinal stimulation to evaluate
the strength of the spinal pathways contributing to motor
recovery.
[0116] Isoflurane anesthesia was induced in a closed chamber and
maintained (2.5-3.5%) via nose cone while rats were tracheotomized.
Rats were mechanically ventilated following tracheal cannulation.
Following femoral venous catheterization rats were converted to
urethane anesthesia (1.6 g/kg) then bilaterally vagotomized and
paralyzed with pancuronium bromide (2.5 mg/kg, i.v.). Blood
pressure was monitored via a femoral arterial catheter and pressure
transducer (Gould P231D, Valley View, Ohio). End-tidal CO.sub.2 was
monitored with a rapidly responding analyzer (Novametrix,
Wallingford, Conn.). Arterial partial pressures of O.sub.2
(PaO.sub.2) and CO.sub.2 (PaCO.sub.2) as well as pH were determined
from 0.2 ml blood samples (ABL-500, Radiometer, Copenhagen,
Denmark); unused blood was returned to the animal. Rectal
temperature was maintained (37-39.degree. C.) with a heated table.
Phrenic nerves were isolated with a dorsal approach, cut distally,
desheathed, bathed in mineral oil and placed on bipolar silver
electrodes. Nerve activity was amplified (1000-10,000.times.) and
filtered (100-10,000 Hz bandpass; model 1800, A-M Systems,
Carlsborg, Wash.).
[0117] Spontaneous phrenic motor output. In all rats, the CO.sub.2
apneic threshold for inspiratory activity in the phrenic nerve
contralateral to hemisection was determined after waiting a minimum
of one hour following conversion to urethane anesthesia. This delay
allowed blood pressure and respiratory motor output to stabilize.
The procedure to establish the apneic threshold began by increasing
the ventilator frequency until inspiratory activity ceased.
Ventilator rate was then decreased slowly until inspiratory
activity re-appeared. The end-tidal CO.sub.2 partial pressure
(P.sub.ETCO.sub.2) corresponding to the onset of inspiratory
bursting was defined as the CO.sub.2 apneic threshold.
P.sub.ETCO.sub.2 was maintained 3 mmHg above the apneic threshold
by adjusting the ventilator pump rate and inspired CO.sub.2
content. After the CO.sub.2 apneic threshold and baseline
PaCO.sub.2 levels were established, 30-45 minutes were allowed to
attain stable baseline conditions.
[0118] Evoked phrenic potentials. Rats were hyperventilated
(PaCO.sub.2<30 mmHg) to prevent spontaneous inspiratory efforts.
A monopolar tungsten electrode (5 M.OMEGA., A-M Systems) was
inserted contralateral to the spinal hemisection and adjacent to
the C2 dorsal roots. The electrode tip was placed in or in close
proximity to the ventrolateral funiculus (1.8-2.3 mm below the
dorsal root entry zone). Electrode position was selected by
maximizing the amplitude of a short latency (<1.0 ms) evoked
potential in the phrenic nerve contralateral to SCI.
Stimulus-response relationships were obtained by applying current
pulses (20-1000 .mu.A, 0.2 ms duration) with a stimulator (model
S88, Grass Instruments, Quincy, Mass.) and stimulus isolation unit
(model PSIU6E, Grass Instruments). Phrenic potentials were
digitized and analyzed with P-CLAMP software (Axon Instruments,
Foster City, Calif.).
Results:
[0119] Body Weight. Body weight decreased by 2 weeks post-injury in
rats that had received a spinal hemisection (FIG. 1). Decreased
body mass may represent disuse atrophy of skeletal muscles or
inadequate caloric intake. Reduced food consumption may occur
secondary to spinal cord injury because of motor paresis, reduced
locomotor coordination, and/or decreased appetite. Spinally injured
rats that received the trophic factor combination had significantly
less reduction in body weight compared to the control group (FIG.
1).
[0120] Spontaneous Phrenic Nerve Activity. Spontaneous recovery of
phrenic motor function on the injured side was evident as
inspiratory bursts that were in synchrony with phrenic motor
activity on the uninjured side. Phrenic motor recovery was present
in all spinally injured rats regardless of treatment. However, the
magnitude of this recovery differed between groups (FIG. 2).
Administration of the trophic factor combination at the time of
injury strengthened motor recovery at 2 weeks post-injury as
evident by the significantly larger peak inspiratory voltage during
baseline recording conditions (FIG. 2). Phrenic peak inspiratory
voltage is correlated to tidal volume. Although tidal volume was
not measured in these rats, it is reasonable to assume that the
increased peak inspiratory voltage would translate to larger tidal
volumes in these animals compared to spinally injured rats that did
not receive the trophic factor combination.
[0121] Evoked Phrenic Nerve Potentials. Evoked potentials were
recorded from the phrenic nerve on the side of injury (FIG. 3).
Consistent with the effects of treatment on spontaneous phrenic
nerve activity data, administration of trophic factor combination
at the time of injury significantly increased evoked potential
amplitudes compared to rats that only received a spinal injury.
[0122] In addition, a strong trend existed for the current required
to evoke a response (threshold current) to be lower after trophic
factor combination administration compared to the control group
(FIG. 4). Collectively, these data suggest that the trophic factor
combination strengthens motor recovery via a spinal mechanism that
strengthens existing synaptic pathways onto phrenic
motoneurons.
Example 2
[0123] This study was performed to determine whether application of
a trophic factor combination can improve motor function after
spinal cord injury (SCI). In this study, the trophic factor
combination of Example 1 was applied and included insulin-like
growth factor (IGF-1), brain-derived neurotrophic factor (BDNF),
bactenesin (BNP-1), and substance P. The trophic factor combination
was applied to test whether this combination would augment
spontaneous respiratory motor recovery in a well-defined model of
high cervical incomplete spinal cord injury (C2 hemisection). The
trophic factor combination was applied to the injured spinal cord
at the time of surgical injury. At 2 weeks post-injury, respiratory
motor output was recorded bilaterally from phrenic nerves in
urethane anesthetized, vagotomized, and mechanically ventilated
spinally injured Lewis male rats (SCI-only: n=6; SCI+ trophic
factor combination; n=6, with some of these rats being the same as
the rats in Example 1). Body weight decreased in all rats after
injury. However, the change in body weight was significantly less
after trophic factor combination treatment (see FIG. 5; p<0.05).
Spontaneous recovery of phrenic motor output on the side of injury
was present in all rats and represents activation of a latent
population of bulbospinal premotor synaptic pathways to ipsilateral
phrenic motoneurons that cross the spinal midline caudal to injury.
The trophic factor combination increased the amplitude of phrenic
inspiratory bursts on the injured side when measured as rectified
and moving-averaged voltages and indexed to the maximal amplitude
during hypercapnia (see FIG. 5; p<0.05). In contrast, the
trophic factor combination did not alter phrenic motor output on
the side opposite injury. Thus, combined treatment with the trophic
factor combination improves phrenic motor recovery after C2
hemisection by selectively augmenting crossed spinal synaptic
pathways.
Example 3
[0124] Subtractive studies. Experiments can be performed on rats in
accordance with the methods described in Example 2 except that
fewer than all four components, i.e., insulin-like growth factor
(IGF-1), brain-derived neurotrophic factor (BDNF), bactenesin
(BNP-1), and substance P, of the trophic factor combination can be
used (except for one or more controls using all four components).
Different components can also be used. For example, a different
growth factor (and/or neurotrophin and/or neuropeptide and/or
antimicrobial peptide) can be used than the one listed above.
Studies can also be run using only one component, i.e., either
IGF-1, BDNF, BNP-1, or substance P or any other trophic factor to
determine the effects of the individual components. Studies can
also be performed using combinations of two of the components and
using combinations of three of the components to determine whether
all four components are needed to achieve the desired results.
Example 4
[0125] Experiments can be performed on dogs having herniated discs.
Traditionally, many dogs undergo surgical treatment of disc
herniation, but no trophic factor combination has been administered
during such surgery. Four naive dogs can be first treated to test
for unanticipated common severe negative effects of the trophic
factor combination. Once this is done, 50 dogs presenting to the
Veterinary Medical Teaching Hospital (VTMH) at the University of
Wisconsin with severe spinal cord dysfunction can be tested.
[0126] Trophic factor combination. The trophic factor combination
can be formulated of insulin like growth factor-1 (IGF-1) (10
ng/ml), substance P (2.5 .mu.g/ml), bactenecin (1 .mu.g/ml) and
brain derived neurotrophic factor (BDNF) (2 .mu.g/ml). The factors
can be dissolved in a 1% hyaluronic acid solution. The hyaluronic
acid is used in order to increase the contact time of the factors
with the tissues.
[0127] Dogs that are clinical patients. Surgery can be performed
under general anesthesia. A hemilaminectomy can be done at the site
of the disc herniation. A 22-gauge catheter can be placed through
the dura mater and arachnoid membrane and inserted in the
subarachnoid space just caudal to the disc herniation. One ml of
the trophic factor combination can be injected in the subarachnoid
space. The surgery site can be closed routinely.
[0128] After recovery from anesthesia, intravenous lactated
Ringer's solution and analgesics can be continued until the dog is
able to drink on its own and does not appear painful. Neurologic
examinations can be done twice a day. The dogs can be discharged to
the owner when they are considered not to need pain medication, can
urinate on their own, and are eating and drinking. Follow up
examinations can be scheduled as appropriate clinically.
[0129] Pain or discomfort during surgery can be alleviated by
maintenance of a surgical plane of anesthesia and constant rate
infusion (CRI) of fentanyl 10 .mu.g/kg/hr. The fentanyl CRI can be
continued up to 12 hours post operatively at a dose of 2-5
.mu.g/kg/hr. A Fentanyl Patch (50 mcg/hr, 5 mcg/kg/hr for total of
72 hours) can be administered as a routine postoperative treatment.
Butorphanol can be further administered if the dogs demonstrate
discomfort and can be given as long as clinical signs of pain, as
indicated by abnormal posturing, vocalization, or discomfort upon
palpation of the surgical wound site are present.
[0130] Immediately after surgery, the dogs can be monitored
continuously until the animals are able to drink water on their own
sufficient to maintain their hydration. After this recovery period,
the animals can be checked a minimum of 3 times daily to determine
if they are experiencing pain or discomfort. The dogs can be
evaluated by physical exam, neurological exam, and direct palpation
of the surgical wound. The dogs can receive routine recumbent
care.
[0131] Dogs can be monitored post-surgically for cardiovascular
stability by physical exam, pulse character, capillary refill time,
heart rate, respiratory rate, and packed cell volume, if needed.
Fluids can be administered if needed to maintain hydration.
Postoperative discomfort can be alleviated by administration of
fentanyl CRI (10 .mu.g/kg/hr) during surgery and fentanyl CRI (2-5
.mu.g/kg/hr) after surgery or butorphanol (0.2-0.4 mg/kg/IV or SQ)
every 4-6 hours thereafter and a Fentanyl Patch (50 mcg/hr, 5
mcg/kg/hr for total of 72 hours).
Example 5
[0132] Safety trial of trophic factor combination on dogs. The
toxicity of the trophic factor combination described in Example 4
was tested on dogs. Four beagle dogs were studied over a three-day
period. While the dogs were anesthetized, the trophic factor
combination described in Example 4 in hyaluronic acid was injected
into 1) the lumbar cerebrospinal fluid (2 dogs) and 2) the cisterna
magna cerebrospinal fluid (2 dogs). In all four cases, the dogs
recovered easily and showed no signs of toxic reactions. There was
no evidence for chronic pain on neurological exam. All dogs were
euthanized on the third day of the study. In summary, no adverse
reactions were observed in any animal.
[0133] It is understood that the various preferred embodiments are
shown and described above to illustrate different possible features
of the invention and the varying ways in which these features may
be combined. Apart from combining the different features of the
above embodiments in varying ways, other modifications are also
considered to be within the scope of the invention.
[0134] The invention is not intended to be limited to the preferred
embodiments described above, but rather is intended to be limited
only by the claims set out below. Thus, the invention encompasses
all alternate embodiments that fall literally or equivalently
within the scope of these claims.
Sequence CWU 0 SQTB SEQUENCE LISTING The patent application
contains a lengthy "Sequence Listing" section. A copy of the
"Sequence Listing" is available in electronic form from the USPTO
web site
(http://seqdata.uspto.gov/?pageRequest=docDetail&DocID=US20070207209A1).
An electronic copy of the "Sequence Listing" will also be available
from the USPTO upon request and payment of the fee set forth in 37
CFR 1.19(b)(3).
0 SQTB SEQUENCE LISTING The patent application contains a lengthy
"Sequence Listing" section. A copy of the "Sequence Listing" is
available in electronic form from the USPTO web site
(http://seqdata.uspto.gov/?pageRequest=docDetail&DocID=US20070207209A1).
An electronic copy of the "Sequence Listing" will also be available
from the USPTO upon request and payment of the fee set forth in 37
CFR 1.19(b)(3).
* * * * *
References