U.S. patent number 3,842,848 [Application Number 05/147,622] was granted by the patent office on 1974-10-22 for keratin polypeptide hydrolyzates as hair treating agents.
This patent grant is currently assigned to Wilson-Sinclair Co.. Invention is credited to Sulo A. Karjala.
United States Patent |
3,842,848 |
Karjala |
October 22, 1974 |
**Please see images for:
( Certificate of Correction ) ** |
KERATIN POLYPEPTIDE HYDROLYZATES AS HAIR TREATING AGENTS
Abstract
The invention relates to compositions for the treatment of
filamentous keratins, for example, to cosmetic compositions for the
treatment of human hair and compositions for modifying animal hair
or fur. The compositions are made up of water soluble peptide
products of partial hydrolysis of keratinaceous materials, such as
hog hair, resulting from hydrolysis using acids under conditions
which, while breaking down the complex proteins, will leave a
substantial portion of the disulfide linkages present in the
keratinaceous materials intact. Filamentous keratins have the
peptide products chemically bonded thereto by a two step process
wherein disulfide linkages of both the peptide products and the
filamentous keratins are split by the action of a reducing agent
and disulfide linkages are then reformed by action of an oxidizing
agent whereby at least some of the sulfhydryl groups of the peptide
products formed by the action of the reducing agent are bonded to
sulfhydryl groups of the filamentous keratins.
Inventors: |
Karjala; Sulo A. (Chicago,
IL) |
Assignee: |
Wilson-Sinclair Co. (Oklahoma
City, OK)
|
Family
ID: |
22522267 |
Appl.
No.: |
05/147,622 |
Filed: |
May 27, 1971 |
Current U.S.
Class: |
132/204;
424/70.4; 424/70.5; 424/70.14; 8/127.51 |
Current CPC
Class: |
A61Q
5/04 (20130101); A61K 8/65 (20130101) |
Current International
Class: |
A61K
8/65 (20060101); A61K 8/30 (20060101); A61k
007/10 () |
Field of
Search: |
;424/71,72 ;132/7
;8/127.51,128 |
References Cited
[Referenced By]
U.S. Patent Documents
Foreign Patent Documents
Other References
Burnett, Am. Per. & Cos., Vol. 78, No. 10 (1963) pp.
69-72..
|
Primary Examiner: Turner; Vincent D.
Attorney, Agent or Firm: Dressler, Goldsmith, Clement &
Gordon, Ltd.
Claims
I claim:
1. A method of treating hair fibers to provide a permanently bonded
protective and conditioning content of disulfide-containing
proteinaceous agent comprising contacting the hair with an
effective amount of an aqueous composition containing water having
dissolved therein from 4 percent to 8 percent by weight of ammonium
thioglycolate reducing agent and from 5 percent to 25 percent by
weight of a water soluble keratin polypeptide hydrolyzate having an
intact disulfide unit content in the range between 15 and 49 moles
of disulfide linkages per 100,000 grams of hair, said hydrolyzate
being produced by hydrolyzing keratin-containing hair at
100.degree.-160.degree.C. in the presence of phosphoric acid having
a concentration of 4 percent to 85 percent until the disulfide
content is in the range specified while maintaining a pH less than
4 throughout the hydrolysis reaction, draining off said aqueous
composition, and then contacting said hair with an effective amount
of an aqueous solution of an oxidizing agent.
2. The method as recited in claim 1 in which said oxidizing agent
is selected from the group consisting of sodium bromate and
hydrogen peroxide.
Description
This invention relates to materials for modification of filamentous
keratins such as human hair, animal hair and similar filamentous
keratin products by being chemically bonded thereto so as to become
an integral portion thereof. More particularly, it relates to a
method for the coupling of the product of partial hydrolysis of a
keratinaceous material to filamentous keratins by cross-linking of
sulfhydryl groups to improve such characteristics as strength and
manageability and to impart gloss.
In accordance with this invention, compositions derived from
natural sources of keratin by hydrolysis under conditions to
preserve a substantial portion of the disulfide linkages of the
peptide or amino acid such as cystine intact, are produced which
have utility in aqueous media for treatment and protection, during
treatment of filamentous type keratin materials, such as human
hair, animal hair such as wool, fur, etc.
Hair, including human hair, and the animal hairs such as wool and
fur, consists of strands of keratin fibers surmounted by a scaly
cuticle of keratin protein. Keratin is unique in its content of
sulfur-containing amino acids, in particular the amino acid
cystine. The disulfide linkages of cystine can be broken to produce
at least one free sulfhydryl group by means of reducing agents, and
the linkages can be reclosed to recover the original cystine by use
of an oxidizing agent. If hair strands are placed under stress,
many of the cystine disulfide units are in a state of tension. If
the strands are treated with a reducing agent while under stress,
the disulfide units are broken. If, while still under stress, after
the disulfide units have been opened up, the strands are subjected
to an oxidizing agent, the disulfide units are reformed, but now
they are reformed with different half-cystine units in a way that
the stress now leaves the strands in their new position, since the
geometry of the strands is "locked in" to the new configuration.
This is the basis of the well-known permanent wave process in which
the hair is treated after curling with ammonium thioglycolate to
open up the disulfide bonds, after which the curled hair is
oxidized with sodium bromate or other oxidizing agents to form the
permanent curl.
It is well known that proteinaceous materials can be produced of a
character which can be adsorbed or absorbed or both when applied to
hair. The disadvantage of the hydrolyzed proteins such as gelatin,
etc., is the non-uniformity in hydrolysis, the salt content present
due to neutralizing the hydrolyzing agents, and the loss of
significant amounts of the hydrolyzates when the treated hair is
subjected to rinses, etc.
It is also well known that treatment of filamentous keratin
materials such as human hair with reducing agents will effect
cleavage of the disulfide linkages. Where the hair, wool, etc., are
treated with reducing and oxidizing agents such as when treating
with hair-waving preparations, the action is damaging and results
in a marked loss in weight from virgin hair strands, and the hair
becomes weak and brittle. Such damage is accentuated when such
treatments are applied to bleached hair.
In keratin fiber dyeing procedures, such as those used in the
treatment of wool, it is generally necessary to heat the keratin
fiber with the dye in water at the boiling point to insure fastness
of the dye. The results of such treatment are that with a fast dye
the color can no longer be removed readily and the keratin fibers
become tenderized by the treatments to add or remove the dye.
Reducing and oxidizing agents are commonly used in the creating of
permanent wave sets for human hair. The hair is put under stress as
by winding on rollers and a reducing agent applied, such as
ammonium thioglycolate, after which the reagent is drained off or
rinsed out and the hair treated with an oxidizing agent such as
sodium bromate or hydrogen peroxide. During treatment with the
reducing agent, the stress on the hair is minimized by the opening
up of the cystine disulfide linkages. Upon oxidation, cystine
disulfide linkages are reformed but the closure occurs between not
only a portion of the original sulfhydryl groups which developed
during the reduction splitting but primarily between sulfhydryl
groups which have been brought into close proximity as a result of
distortion of the keratin filaments due to the applied stress. By
such action, the hair strand is reformed but with a new waved
structure. This remains as a permanent feature of the hair strands
until the hair is subjected to another waving procedure or until
the hair strands grow out.
Now it has been discovered that if keratin-containing material,
such as hog hair, is partially hydrolyzed through the use of dilute
phosphoric acid or of multifunctional organic acids in a manner
such that a substantial proportion of the cystine disulfide units
are retained intact, the keratin polypeptides obtained have
interesting properties.
Since the chemical composition of the keratin polypeptide has
considerable similarity to that of the hair or wool, there is no
direct chemical proof that a reaction occurs to link the
polypeptide directly to the hair other than by the use of keratin
polypeptides containing radioactive elements. However, after
treatment of the hair or wool with the reducing agent containing
the keratin polypeptide, there is generally a gain in weight of the
hair or wool swatch, while with the reducing agent alone there is a
sharp loss in weight. The hair also retains its structure, form and
sheen in the presence of the polypeptide, while keratins treated
with the reducing agent alone show brittleness, shrinkage and loss
in strength.
A more definitive proof that linkage has occurred is demonstrated
when the keratin polypeptides are coupled through their free amino
groups to a diazotized dye intermediate by known means, and the
dye-coupled keratin polypeptide is isolated. When human hair or
wool is treated in pH 9.2 buffer with the dye-coupled polypeptide
and washed with water, all of the dye-coupled polypeptide washes
out, since there has been no chemical combination of the two
components and there is little or no physical sorption of the
dye-coupled derivative upon the hair or wool. If, however, the
dye-coupled polypeptide is dissolved in ammonium thioglycolate at
pH 9.2, and the human hair or wool is treated with this solution,
drained and reoxidized with a mild oxidant, the hair strands or
wool swatches are permanently dyed, and the dye cannot be washed
out with water, detergents, acids or alkalis, or organic
solvents.
Coupling of the dye-keratin polypeptide derivative with the hair or
wool occurs at room temperature, and there is no necessity for
heating the reaction mixture in boiling water. The extent of
linkage of the dye-keratin polypeptide complex to the hair or wool
is a function of the concentration of the complex in the reducing
solution, the concentration of added unmodified keratin
polypeptides, if any, and the reaction time used. Thus, by
modifying the conditions, any shade or tint of the dye can be
obtained.
Wool can be modified in the form of yarn, or after weaving.
Permanent prints can be made on wool if, for example, dry virgin
wool is treated with solutions of the keratin-dye complex in a
reducing solution by means of a printing roller in which the design
is transferred to the flannel, dried and subjected to a flow of air
to obtain atmospheric oxidation, or passed through a dilute
solution of mild oxidant, washed, and dried by normal means.
As has been pointed out above, the modification impressed on the
hair or wool is permanent and is not removed by the ordinary rinse
or shampoo treatments. There is one method, however, by which the
modified keratin polypeptide can be substantially removed from the
hair or wool product. This method is to treat the hair or wool
product with thioglycolate alone, in order to reopen the disulfide
linkages, wash the product well with water, and reoxidize with a
mild oxidant. However, since repeated reductant and oxidant
treatments tend to degrade the hair or wool, it is preferred to
inhibit the degradation by adding unmodified keratin polypeptide to
the reductant, so the modified derivative is replaced substantially
by unmodified keratin polypeptide which has the ability to minimize
the damage to hair of such chemical actions.
When preparing the keratin polypeptide having utility as hair
modifiers, the number of intact disulfide linkages remaining in the
keratin polypeptides is dependent upon the purity and cleanliness
of the initial hog hair, and the processing conditions for
hydrolysis. The cleaner the hair, the higher is the amount of
intact disulfide linkage. The more drastic the digestion conditions
generally the lower the amount of intact disulfide linkages. Since,
in a partial hydrolysis, the product will be made up of a
heterogeneous mixture of substances of different molecular weights,
the measure of disulfide units is an average one. On separation of
a hydrolysis mixture by reverse osmosis, it was found that the
lowest molecular weight fraction, below 1,000, had the smallest
number of intact disulfide linkages, while the fraction of
molecular weight 1,000 to 10,000 had a larger number, and the
fraction with a molecular weight over 10,000 had the largest number
of intact disulfide linkages.
The extent of disulfide units is measured by known means, using a
polarograph and a rotating platinum electrode, with titration of
the sulfhydryl groups amperometrically with methyl mercuric iodide.
Under optimum conditions, hydrolysis of clean hog hair with 85
percent phosphoric acid for 10 to 15 minutes at 135.degree.C. gives
a product which shows approximately 50 moles of disulfide linkage
per 100,000 grams of hair. This value approximates the value for
the total sulfur content of the hair. Under plant operating
conditions, however, where it is uneconomical to purify the hair
completely and the use of highly purified reagents is impractical,
intact disulfide values of 15 to 49 moles per 100,000 grams are
normally found, which is the product of subjection of
keratin-containing material to heat for period of 1 to 24 hours at
temperatures in the range between 100.degree.C. and 160.degree.C.
in the presence of acid having a concentration in the range between
4 and 85 percent and in quantities to maintain a pH of less than 4
throughout the hydrolysis reaction, said period varying inversely
with the temperature level. All keratin polypeptides, for example,
dipeptides, tripeptides, tetrapeptides, etc. provided the peptides
still contain one or more intact cystine units, are applicable for
use in this invention.
In Table I are listed a few of the results obtained by the use of
this invention. These results are based on weight changes, so
relative differences in one series are comparable. However, it is
not always possible to compare the results in one series with those
in another, since the weight changes are occasionally modified by
changes in moisture content due to changes in relative
humidity.
After treatment with keratin polypeptide, the samples were washed
thoroughly with water and detergent, dehydrated with acetone, and
finally air-dried.
After treatment with ammonium thioglycolate the samples were washed
with water, oxidized for 5 minutes with 1.5 percent sodium bromate
solution, washed again with water and detergent, dehydrated with
acetone, followed by air-drying.
After treatment with mixtures of keratin polypeptides and ammonium
thioglycolate, the samples were drained a short time to remove the
excess solution, after which they were oxidized with 1.5 percent
sodium bromate solution for 5 minutes, and washed and dried as
above.
The wool swatches were 100 percent worsted flannel, and the human
hair samples were of white virgin hair and a medium bleached hair
obtained from commercial sources.
The invention will be further understood from the following
examples which are given for the purposes of illustration and
without any intention that the invention be limited thereto.
The method of preparing a water soluble product by partial
hydrolysis of keratinaceous materials is as follows:
EXAMPLE I
To 100 grams of 75% H.sub.3 PO.sub.4, heated in a large test tube
to 125.degree.C. to 130.degree.C. in an oil bath, was added
portions of hair over a period of 5 hours. A total of 56 grams of
hair was added, and this amount appeared to be about the maximum
which could be added under these conditions. The mixture was heated
for another 1.5 hours at this temperature, and cooled. No unchanged
hair particles were observed. The mixture was then diluted with 4
to 5 volumes of water, centrifuged to remove dark insoluble
material, and the supernatant, at pH 1.7, was brought up to pH 6.7
with solid CaCO.sub.3. The light yellow filtrate was concentrated
to approximately 50 percent polypeptide solids by vacuum
evaporation.
The method of treating hair to incorporate the products of
hydrolysis as an integral part of filamentous keratins is
illustrated by the following examples.
EXAMPLE II
50 grams of the dry hydrolyzate product of Example I were dissolved
in 1,000 grams of aqueous solution containing 6 percent by weight
of ammonium thioglycolate to form a 5 percent by weight solution.
Coils of medium bleached hair strands were placed in the solution
for 15 minutes, the solution drained off and then the coils are
oxidized by treatment for 5 minutes with an aqueous solution
containing 1.5 percent by weight of sodium bromate. The hair coils
were then washed with water, detergent, acetone, alcohol and
finally ether. Additional coils of the medium bleached hair were
similarly treated with the 6 percent ammonium thioglycolate
solution not containing any hydrolyzate. Similar coupling
operations were carried out on white virgin hair using 6 percent
ammonium thioglycolate solutions.
EXAMPLE III
250 grams of the dry hydrolyzate product of Example I were
dissolved in 1,000 grams of aqueous solution containing 6 percent
by weight of ammonium thioglycolate to form a 25 percent by weight
solution. Coils of medium bleached hair strands were placed in the
solution for 15 minutes, the solution drained off and then oxidized
by treatment for 5 minutes with an aqueous solution containing 1.5
percent by weight of sodium bromate. The hair coils were then
washed with water, detergent, acetone, alcohol and finally ether.
Additional coils of the medium bleached hair were similarly treated
with the 4 percent ammonium thioglycolate solution not containing
any hydrolyzate. Similar coupling operations were carried out on
white virgin hair using 4 percent ammonium thioglycolate
solutions.
EXAMPLE IV
50 grams of the dry hydrolyzate product of Example I were dissolved
in 1,000 grams of aqueous solution containing 8 percent by weight
of ammonium thioglycolate to form a 5 percent by weight solution.
Segments of wool flannel were placed in the solution for one half
hour, the solution drained off and the wool flannel then oxidized
by treatment for 5 minutes with an aqueous solution containing 1.5
percent by weight of sodium bromate. The wool segment was then
washed with water, detergent, acetone, alcohol and finally
ether.
Additional segments of wool flannel were similarly treated with 8
percent ammonium thioglycolate solution not containing any
hydrolyzate.
Additional segments of wool flannel were treated in a similar
manner with an 8 percent thioglycolate solution containing 10
percent and 20 percent by weight of the hydrolyzate product of
Example I.
Details of the additional wool treatment and the results thereof
are set forth in Examples VI and VII.
EXAMPLE V
200 grams of the dry hydrolyzate product of Example I were
dissolved in 1,000 grams of aqueous solution containing 4 percent
by weight of ammonium thioglycolate solution to form a 20 percent
by weight solution. Segments of wool flannel were placed in the
solution for one half hour, the solution drained off and then
oxidized by treatment for 5 minutes with an aqueous solution
containing 1.5 percent by weight of sodium bromate. The wool
segment was then washed with water, detergent, acetone, alcohol and
finally ether.
The weight changes effected by the treatments described in Examples
II through V are set forth hereinafter in Table I. Table I also
shows the result of subsequently treating the products with
thioglycolate solutions with and without the presence of the
polypeptide product of Example I.
TABLE I
__________________________________________________________________________
Initial Treatment Subsequent Treatment Keratin Keratin Sample and
Polypep- Thio- Weight Polypep- Thio- Weight Reaction Time tide
glycolate Change tide glycolate Change
__________________________________________________________________________
Wool Flannel 20% 0% +0.02% 1/2 hour 20% 4% +0.8 % 20% 4% +0.65% 0
4% -2.6% Medium Bleached 25% 4% +2.4 % Hair 25% 4% +3.6 % 0 4%
-9.3% 1/2 hour 0 4% -11.0% Medium Bleached 5% 0 -1.0 % Hair 0 6%
-8.5 % 15 minutes 0 6% -10.0% 5% 6% +0.97% 5% 6% -6.1 % 0 6% -3.0 %
5% 6% -6.1 % White Virgin 5% 0 +0.3% Hair 0 6% -0.9% 1 hour 0 6%
-0.54% 5% 6% +1.45% 5% 6% 0 5% 6% +0.15% 0 6% -0.23%
__________________________________________________________________________
EXAMPLE VI
Three swatches of 100 percent worsted wool test flannel were
treated as follows:
Sample No. 1 2 3 Weight of sample 99.52 mg 87.86 mg 88.82 mg
Treatment 1 hr. 1 hr. 1 hr. % Keratin poly- peptide in pH 9.2
buffer 10% solution 10% solution 10% solution % Ammonium
thioglycolate pH 9.2 0 8% 8%
Sample 1 was washed 4 times with water, while samples 2 and 3 were
drained for a short time, oxidized with 1.5 percent sodium bromate,
and washed four times in water, after which all samples were air
dried overnight.
______________________________________ Weight of Sample 98.87 mg
90.58 mg 92.26 mg Weight change -0.65 mg +2.72 mg +3.44 mg % Weight
change -.65% +3.1% +3.9% ______________________________________
Sample 2 was immersed for one hour in 8 percent ammonium
thioglycolate, washed well with water, oxidized with 1.5 percent
sodium bromate solution, washed again with water, and air
dried.
______________________________________ Final weight of sample 86.98
mg Weight change -3.60 mg % Change -4.14%
______________________________________
Treatment of human hair or wool with ammonium thioglycolate always
results in a loss in weight of the sample, but in the presence of
keratin polypeptides there is a gain in weight, or, at the most, a
smaller loss in weight than when ammonium thioglycolate is used
alone without keratin peptides. This is shown in Sample 3 which
showed a sharp loss in weight when treated with the reducing agent
alone. The insignificant change in weight in Sample 1, treated with
the keratin polypeptides alone at pH 9.2, shows that the increase
in weight is not due to sorption of the polypeptide.
EXAMPLE VII
The effect of increasing concentration of keratin polypeptides was
shown when four swatches of the test flannel were treated as
follows:
Sample No. 4 5 6 7
__________________________________________________________________________
Weight of sample 100.32 mg 101.52 mg 98.56 mg 94.12 mg Treatment
time 1/2 hr. 1/2 hr. 1/2 hr. 1/2 hr. % Keratin poly- peptide in pH
0.2 buffer 20% 5% 10% 20% % Ammonium thio- glycolate pH 9.2 0 8% 8%
8%
__________________________________________________________________________
Sample 4 was drained, washed well with water, and air dried.
Samples 5, 6 and 7 were drained, treated for 5 minutes with 1.5
percent sodium bromate, washed with water and air dried.
__________________________________________________________________________
Weight of Sample 100.44 mg. 101.44 mg. 96.16 mg. 95.68 mg. Weight
change +0.16 mg. +0.03 mg. +0.60 mg. +1.5 mg. % Change +0.16%
-0.079% +0.61% +1.65%
__________________________________________________________________________
Thus there is an increase in pickup of the peptide with increase in
concentration. The ammonium thioglycolate concentration was double
that in Example V and Sample 5 indicates that the 5 percent level
of peptide under these conditions essentially balances out the
normal weight loss to be expected from thioglycolate treatment. An
increase in color occurs from Sample 5 to 7 since the peptide is
darker than the flannel swatch.
The effect of the keratin peptides on samples of medium bleached
human hair is shown in the following example. In this case, all of
the original samples showed weight losses as a result of humidity
changes on standing overnight. However, the relative weight changes
are of greater importance than the absolute changes.
EXAMPLE VIII
__________________________________________________________________________
Sample No. 8 9 10 11 12
__________________________________________________________________________
Weight sample 19.28 mg. 37.52 mg. 41.24 mg. 30.12 mg. 87.84 mg.
Treatment time 15 min. 15 min. 15 min. 15 min. 15 min. % Keratin
pep- tide in pH 9.2 buffer 5% sol. 0 0 5% sol. 5% sol. % Ammonium
thio- glycolate pH 9.2 0 6% 6% 6% 6%
__________________________________________________________________________
Sample 8 was washed in water and dried, while samples 9, 10, 11 and
12 were immersed in 1.5 percent sodium bromate for 5 minutes,
washed well with water, and air dried.
__________________________________________________________________________
Weight after 19.08 mg. 34.32 mg. 37.12 mg. 28.28 mg. 73.12 mg.
drying Weight change -0.20 mg. -3.20 mg. -4.12 mg. -1.84 mg. -4.72
mg. % Weight change -1.0% -8.5% -10% -6.1% -6.1%
__________________________________________________________________________
There is thus less weight loss in the presence of keratin peptide.
The hair samples 11 and 12 were smooth, soft and silky, very
similar to the initial samples and Sample 1.
Samples 10 and 11 were treated as follows:
Sample 10 Sample 11 ______________________________________
Treatment time 15 minutes 15 minutes % Keratin peptide in pH 9.2
buffer 5% solution 0 % Ammonium thioglycolate pH 9.2 6% 6%
______________________________________
Sample 10 was subjected to the same treatment as the initial
treatment of samples 11 and 12, while sample 11 was given the same
treatment as that of samples 10 and 11.
The samples were then allowed to dry.
______________________________________ Sample 10 Sample 11
______________________________________ Weight after drying 37.48
mg. 27.44 mg. Weight change +0.36 mg. -0.84 mg. % Weight change
+0.97% -2.97% ______________________________________
Thus, this example again illustrates the protective action of
keratin polypeptide during treatment of human hair with reducing
and oxidizing agents.
Since the weight changes which occur in the above examples are
small, and at times may be overshadowed by weight changes due to
changes in relative humidity, a more positive demonstration is
necessary to show that the effect observed is actually due to a
chemical reaction, with the formation of stable covalent bonds
which are much stronger than the bonds associated normally with
sorption of peptides or protein by hair strands. One indication is
that shown in Example VII, in which the color of the flannel
swatches increases with increase in peptide concentration.
Additional proof of the bonding of disulfide linkage containing
polypeptides to filamentous keratins is shown by the following
example.
EXAMPLE IX
Cystine was converted to dinitrophenylcystine by a known reaction
with fluorodinitrobenzene. The product was crystallized from
alcohol, dissolved in ammonium thioglycolate, and swatches of wool
flannel and coils of hair were immersed in the solution for a short
time, drained, and the keratin samples oxidized with dilute sodium
bromate, washed with water, detergent, and organic solvents. The
bright golden color in the samples was impervious to all solvents
which did not destroy the wool or hair swatches.
Similar results were obtained when keratin polypeptides, prepared
as described in Example I, were converted to dinitrophenyl
derivatives by the same reaction procedure.
Although the best mode contemplated for carrying out the present
invention has been herein shown and described, it will be apparent
that modification and variation may be made without departing from
what is regarded to be the subject matter of the invention as set
forth in the appended claims.
* * * * *