JPS6222964B2 - - Google Patents

Description

[Detailed description of the invention]

The present invention relates to a cosmetic agent for treating keratin tissue, and more particularly to a cosmetic agent for hair conditioning that has a high ability to repair damaged hair. It is the external keratin tissue that forms the hair, skin and nails as a protective covering of the human body. It is known that various beauty treatments alter keratin, in particular hair bleaching,
Straightening, toning, dyeing and permanent waving have a significant effect on keratin proteins. Mechanical treatments such as combing, brushing, and the use of curling irons can also alter the keratin in the hair. Both bleaching and dyeing are oxidation treatments that convert cystine, a component of keratin, i.e., most of the sulfur-containing crystalline amino acids, into various oxidation products, the main one of which is cysteic acid. Conventional two-stage permanent
In the waving method, the disulfide bond of cystine is first reduced to form two sulfhydryl groups (-
SH), and cystine becomes two cysteine moieties. In the second step, the sulfhydryl group is oxidized and returns to the disulfide bond of cystine. However, in this oxidation reaction, the sulfhydryl groups usually do not completely return to the disulfide bond of cystine, and many of the sulfhydryl groups are oxidized to form the anionic SO ₃ group present in cysteic acid. Because disulfide bonds contribute to hair strength, hair that has been subjected to treatments such as permanent waving exhibits a loss of strength. Keratin tissue is normally acidic, and its isoelectric point is on the acid side of the PH scale. In addition to hair being acidic in its normal state, acidic end groups are formed as a result of cosmetic treatments based on oxidation reactions, so the isoelectric point of the hair decreases and the hair becomes even more acidic. Therefore, hair that has been bleached, dyed or permanently waved exhibits a loss of disulfide bonds and increased acidity, which translates into a loss of the hair's natural strength and flexibility.
Therefore, cosmetically treated hair often requires additives to repair and improve its damaged condition. Treatment with polypeptide-containing agents is already known as a method of cosmetically improving the feel and appearance of various keratinous substances, especially damaged hair, skin and nails. Experience has shown that polypeptides are particularly useful in improving the feel and appearance of hair damaged by bleaching, dyeing, and permanent waving. Polypeptides are naturally occurring proteins that contain acids, bases and/or
Alternatively, it can be prepared by enzymatic hydrolysis. For example US Patent No. 3683939
This product contains polypeptides with a molecular weight of 500 to 1,500 prepared by partially hydrolyzing collagen by applying heat and pressure, recovering anions from the formed protein hydrolyzate, and completing the hydrolysis with a proteolytic enzyme. A hair treatment agent is disclosed.
A common problem with treatments of this type prepared by conventional acid, base and enzymatic hydrolysis methods is that they lack uniformity and consistency for two reasons. First, the quality of the polypeptide product depends on small differences in variables such as collagen source, pressure, pH, time of hydrolysis, and type of enzyme used for enzymatic hydrolysis. The second reason is that
The inability to control which peptide linkages of collagen are hydrolyzed during the polypeptide preparation process. That is, each polypeptide will have a terminal group with different chemical properties, resulting in uneven effects on hair. Polypeptides prepared by known methods also typically lack the positive charge necessary to bind to the acidic end groups of hair formed by relatively harsh salon treatments. Therefore, it is possible to reproduce cosmetic preparations for treating keratinous tissues containing polypeptides that contribute to improving the appearance, compliance, elasticity and luster of damaged keratinous tissues (products of the same quality can be produced again).
Manufacturing is desired. This polypeptide must be derived from a protein so that the protein's positive charge neutralizes the acidity of damaged hair. Also, ke〓〓〓〓
It must have a positive group at the end of the molecule to be able to form ionic bridges between the chains of the latin protein. Furthermore, the polypeptide must be of optimal molecular size to allow penetration into the hair shaft, and desirably can be prepared economically by reproducible means. In the light of experience, it has been found that a cosmetic agent for treating keratin tissue containing a polypeptide derived from a protein by the action of the enzyme trypsin has the above-mentioned characteristics. Specifically, this cosmetic agent mainly has two sterically unhindered positive charges, and has the structural formula The main component is a polypeptide with In this structural formula, n is an integer sufficient to give a molecular weight of about 700 to about 1600, and each R ₁ is an independent side chain group attached to the alpha carbon of a natural amino acid; R ₂ is −(CH ₂ ) ₄ −NH ₃ and

Selected from the group consisting of [Formula]. The cosmetic agent of the present invention is prepared by trypsin-catalyzed hydrolysis of an amino acid-containing protein selected from the group consisting of arginine, lysine, and mixtures thereof, and contains a sufficient amount of said amino acid to exert a cosmetic effect. It consists of an aqueous solution containing the polypeptide and having a pH of about 2.5 to about 9. When the cosmetic agent of the present invention is used for hair conditioning, the pH of the aqueous solution is preferably about 4 to about 7, more preferably about 4 to about 5, and contains 30% by weight or less of the charged polypeptide. More preferably, the aqueous hair conditioner solution contains about 15% to about 5% by weight of the charged polypeptide. When the cosmetic composition of the present invention is used for hair shampoo, it is preferred that the aqueous solution contains about 5% or less of the charged polypeptide by weight. When used as a nail or skin conditioner, it is preferred to contain about 30% or less of the charged polypeptide by weight. The keratin tissue treated with the cosmetic agent of the present invention exhibits greater improvement in both strength and texture than the keratin tissue treated with conventional cosmetic agents. In particular, hair treated with the cosmetic agent of the present invention exhibits superior flexibility, volume and shine compared to hair treated with conventional cosmetic agents. The above and other features, aspects, and advantages of the present invention will become clearer from the description of the embodiments and the claims. The present invention relates to cosmetic agents useful in the treatment of keratinous tissue, particularly hair, and methods of use thereof. The cosmetic agent of the present invention usually has two sterically unhindered positively charged structural formulas. The main component is the polypeptide. In this structural formula, n is an integer sufficient to give a molecular weight of about 700 to about 1600, each R ₁ is an independent side chain group bonded to the alpha carbon of a natural amino acid, and R ₂ is −(CH ₂ ) ₄ −NH ₃ and

Selected from the group consisting of [Formula]. Such a cosmetic agent of the present invention exhibits a cosmetic effect prepared by hydrolysis of a protein containing an amino acid selected from the group consisting of arginine, lysine, and a mixture thereof, particularly by trypsin-catalyzed protein hydrolysis. The method consists of an aqueous solution having a pH of about 2.5 to about 9 containing a sufficient amount of the polypeptide. In order for the polypeptide to have a molecular weight of about 700 to about 1,600, <<n>> is usually an integer of about 4 to about 25. The molecular weight of a polypeptide is not only n.
It also depends on R ₁ and R ₂ . For example, R ₂ is α of lysine
A side chain that is bonded to carbon, and in which both R _1s are bonded to the alpha carbon of alanine [-CH ₃ ]
If n is about 12, the molecular weight will be about 1000, and if n is about 21, the molecular weight will be about 1000.
1500 polypeptides. When R ₁ is changed to [(CH ₃ ) ₂ CH ₁ −], which is a side group bonded to the alpha carbon of valine, if n is 12, the molecular weight will be about 1335. That is, n varies depending on the molecular weight of the product and the side groups R ₁ and R ₂ . 〓〓〓〓
R ₁ represents a side group attached to the alpha carbon of the natural amino acid. Since a cleavage reaction occurs at the carboxy end of arginine and lysine during the preparation of the polypeptide used in the cosmetic agent of the invention, R ₁ is usually not a side group of arginine or lysine. That is, wherever arginine or lysine is present in the protein used to prepare the cosmetic agent of the present invention, the derivatives of these two amino acids will appear at the ends of the polypeptide product, rather than at the center.
Therefore, unless synthetic proteins such as polylysine or polyarginine are used, all R ₁
Only a minority of these represent side groups attached to the alpha carbons of arginine and lysine. In each polypeptide, each R ₁ is
Since it is independent of R ₁ , consecutive R _1s in one polypeptide may be the same or different. _R1 side groups include hydrogen, hydrocarbons, and hydrocarbons bonded to inorganic elements; typical _R1 side groups are bonded to the alpha carbon of amino acids such as glycine, leucine, methionine, threonine, valine, tyrosine, etc. H, (CH ₃ ) ₂ CHCH ₂ −,
CH ₃ SCH ₂ CH ₂ −, CH ₃ CHOH−, (CH ₃ ) ₂ CH−,

Including [formula] etc. The positively charged polypeptide with no steric hindrance used in the cosmetic agent of the present invention is produced by hydrolyzing a protein containing arginine or lysine, or both residues, using trypsin as a catalyst. Prepare by boiling. The enzyme trypsin acts on proteins at the carboxy end of the peptide linkage formed by the two types of amino acids, forming a positively charged NH ₃ group with no steric hindrance at one end of the polypeptide. A second positive charge without steric hindrance is also generated in the R ₂ side group. There are proteins that can be hydrolyzed using trypsin as a catalyst to reproducibly prepare polypeptides bearing two sterically unhindered positive charges. If the frequency and position of lysine and arginine in a protein chain are known, the structure of a polypeptide prepared by trypsin-catalyzed hydrolysis can be predicted. That is, a polypeptide is prepared which carries two sterically unhindered positive charges and whose molecular size, structure and reactivity can be predicted. Furthermore, if a mixture of various proteins is used as a raw material, polypeptides with different molecular sizes and structures can be obtained. This is a new method that differs from conventional acid, base, and high temperature protein hydrolysis methods that are performed alone or in combination with enzymatic hydrolysis; It cannot carry a positive charge without steric hindrance at both ends of the molecule. A wide range of proteins can be used to prepare polypeptides by trypsin-catalyzed hydrolysis. These proteins can be classified according to their biological function: structural proteins such as collagen, keratin, fiveroin, elastin, sclerotin, etc., storage proteins such as ovalbumin, casein, ferritin, gliadin, zein, etc.
These include transport proteins such as serum albumin, hemoglobin, β ₁ -lipoprotein, ceruloplasmin, etc., and contractile proteins such as myosin, actin, dayme, etc. Proteins that can be used in the present invention include metalloproteins, nuclear proteins,
It may be a complex protein such as a protein, a glycoprotein, or a lipoprotein, or a non-complex protein. These proteins come from a variety of sources, including animals, plants, poultry, dairy products, molds, fungi, yeast, and bacteria. Typical proteins that can be used to prepare tryptic peptides, that is, polypeptides produced from trypsin-catalyzed protein hydrolysis, include casein, collagen, feather keratin, and soybean protein. As raw materials for preparing polypeptides from trypsin-catalyzed hydrolysis, not only natural proteins but also synthetic proteins containing lysine or arginine or both can be used. For example, polylysine and polyarginine can also be used to prepare tryptic peptides useful in obtaining the cosmetic agents of the present invention. A mixture of some of the above proteins can also be used as a raw material. The method of using the cosmetic preparation according to the invention is to bring the cosmetic preparation into contact with the keratinous tissue to be treated. Cosmetics of the present invention typically contain from about 0.1 to about 30% by weight of two sterically unhindered positively charged polypeptides. For example, by washing your hair with a shampoo containing about 5% polypeptide by weight.
You can get a hair treatment effect. Similarly, the cosmetic composition of the invention formulated as a hair conditioner preferably consists of an aqueous solution containing about 30% or less by weight of charged polypeptide. In the light of experience, when the aqueous solution has a pH of about 4 to about 5 and contains about 15 to about 25% by weight of two sterically unhindered positively charged polypeptides, it is useful as a hair conditioner. Extremely effective. When prepared as a nail or skin conditioner, the aqueous solution preferably contains about 30% or less of the polypeptide by weight. The cosmetic agent of the present invention consists of an aqueous solution containing two sterically unhindered, positively charged polypeptides obtained mainly by trypsin-catalyzed protein hydrolysis. However, even when natural proteins are hydrolyzed, the aqueous solution contains polypeptides that do not have steric hindrance and do not have two charges, and polypeptides that are not generated from trypsin-catalyzed protein hydrolysis. is inevitable. There are two causes for the appearance of two sterically unhindered, uncharged polypeptides. The first reason is that proteinaceous materials necessarily have amino acid terminal groups other than lysine or arginine. That is, no matter how much lysine or arginine is contained in a protein, at least 1% of it can be obtained from hydrolysis of this protein.
The types of polypeptides do not correspond to the structural formulas listed above. The second cause lies in the protein extraction method before hydrolysis using trypsin as a catalyst. For example, collagen can be extracted from pig's feet by so-called hot water extraction, and it is inevitable that some of the protein in collagen will be hydrolyzed during this hot water extraction process. The ratio of two sterically unhindered, positively charged polypeptides to two sterically unhindered, positively charged polypeptides can be controlled by appropriate selection of the protein mixture to be hydrolyzed. . For example, the longer the protein chain and the higher the frequency of lysine and arginine in the protein chain, the more likely it is that two sterically unhindered positively charged polypeptides will be present in an aqueous solution after trypsin-catalyzed protein hydrolysis. The proportion will also increase. That is, the cosmetic agent of the present invention consists of an aqueous solution containing trypsin polypeptide as a main component, and at least about 60% of the polypeptide can be obtained by hydrolysis using trypsin as a catalyst. Preferably, at least about 80% of the polypeptide is obtained by this method. One method that can be applied to the preparation of tryptic polypeptides is enzymatic hydrolysis of collagen.
This reaction is preferably carried out under basic conditions with a pH of about 8 to about 8.5. It is preferable to increase the temperature of the collagen solution to promote hydrolysis, but it must be below about 82.2°C (180°C) to prevent denaturation of the enzyme. The reaction is usually allowed to proceed to completion, which is checked against known molecular weight standards using liquid chromatography. If you want to stop the reaction before it goes to completion, add acid to the solution or heat the solution to about 93.3°C (200°C).
〓) to denature the trypsin. Although it cannot be supported theoretically, it is believed that the cosmetic composition of the present invention improves the cosmetic quality of the hair by eliminating the excess of anions resulting from cosmetic treatments. This excess anion elimination is achieved by the generation of an extra number of positively charged groups in the tryptic peptide contained in the cosmetic agent of the present invention. Since the aqueous solution utilized in the cosmetic preparation of the present invention has a pH of about 2.5 to about 9, there are sufficient protons in the solution to impart a net positive charge to the polypeptide. This extra positive charge appears on the proton acceptor _R2 side group formed upon tryptic cleavage of proteins containing lysine or arginine. This extra positive charge on the polypeptide is present when the cosmetic agent is acidic. Therefore, the cosmetic agent of the present invention is preferably acidic. However, the cosmetic composition of the present invention is effective over a pH range of about 2.5 to about 9. The more basic the solution, the less positive charge the trypsin polypeptide will have, so a lower pH is preferable. However, if the pH drops below about 2.5, there is a risk of damaging the skin. For maximum effectiveness when used on weakened hair, a pH of about 4 to about 7, particularly about 4 to about 5, is preferred. The tryptic peptide, which has two sterically unhindered positive charges, has a hair-like structure due to its ability to form cross salt linkages at the cystine-cystine cross structure due to chemically broken disulfide bonds. Regenerates keratin tissue〓〓〓〓
Ru. The sterically unhindered N-terminus of the tryptic polypeptide and the NH ₃ group of the R ₂ side group in the cosmetic agent of the present invention are positively charged, providing maximum binding effect on weakened hair. Therefore, the cross-salt bond results in a three-dimensional structure reinforcement. Although it cannot be theoretically supported, it is believed that hair that has been oxidized by treatment at a beauty salon is reconstituted by the cosmetic agent of the present invention as described below. That is, In the process, keratin cystine-cystine
Disulfide bonds are reduced to sulfhydryl groups and then oxidized to form cysteic acid. In the step, the sterically unhindered positively charged N-terminal group of the polypeptide according to the invention and the R _2
3 binds to the anionic SO ₃ group of cysteic acid and strengthens the three-dimensional structure of the keratin tissue. The tryptic peptides of the present invention reduce the water absorption of hair by occupying anionic positions in oxidatively damaged hair. This action of tryptic peptides also serves to strengthen the hair, since water absorption by the anionic sites of the hair contributes to the loss of hair strength. The above and other advantages of the cosmetic composition of the present invention will be clarified in the following examples. EXAMPLE Control Groups 1A-8L Each of the 8 subjects (#1-#8) received 12 doses for the 12 control treatments (A-K).
of hair samples, resulting in a total of 96 control samples. Individual samples were designated by a combination of numbers and letters, where the numbers were the subject's number and the letters represented the treatment. The backgrounds of subjects 1, 3, 4, 7, and 8 are as follows. Subject #1: 23-year-old Caucasian female with medium-dense, light brown hair. Wavy, thick, no experience with dyeing or straightening. The scalp is normal. I have experience with permanent waving in 1963 and no experience with bleaching. #3 A 19-year-old Caucasian woman with dark, matte, thick, long, wavy hair. No experience with dyeing, bleaching, permanent waving, or chemical straightening. #4 A 22-year-old white woman with no experience in dyeing, bleaching, chemical straightening, or permanent waving. #7 Caucasian woman with short, brown, oily, unwavy hair of medium density. #8 Thin, sparse brown hair that breaks easily. It has been dyed, but I have never had it bleached. I have short hair with no experience in chemical straightening or permanent waves. The backgrounds of subjects 2, 5, and 6 are unclear. The samples were subjected to the following treatments. Treatment A No treatment was given. B Only shampoo. The practitioner wears rubber gloves,
Tap water was used both when shampooing and when rinsing. PH samples of subjects #1, #2 and #3
I washed my hair with Anion Shampoo, which has a strong cleaning power of 5 to 6. Samples of test subjects #4, #5, and #6 washed their hair with anion shampoo that has a gentle conditioning effect and has a pH of 4.5 to 5.5〓〓〓〓
Ta. Samples from subjects #7 and #8 were washed three times with conditioning shampoo, leaving the soap suds on the hair for the third time. Neither shampoo left a filmy residue on the hair. C-K A sample to which Treatment C-K containing a polypeptide outside the scope of the present invention is applied is shampooed in the same manner as Treatment B, and an aqueous solution as listed in Table 1 is applied with a hair dye brush, and left for 20 minutes. Then rinsed with tap water. In addition, treatments C to H use pancreatic secretory enzymes having proteolytic ability, and treatments I, J, and K contain polypeptides obtained by hydrolyzing proteins with acid. Table 1 Control group treatment solution C Pancreatic secretory enzyme hydrolysis product of Carnapro (trade name of milk protein hydrolyzate) with pH 4.0 (15% concentration) D Pancreatic secretory enzyme hydrolysis product of Carnapro (20% concentration) %
Concentration) E Pancreatic secretory enzyme hydrolysis product of casein at PH4.0 (15% concentration) F Pancreatic secretory enzyme hydrolysis product of casein at PH4.0 (20% concentration) G Pancreatic secretory enzyme hydrolysis product of collagen (15%
Concentration) H Pancreatic secretory enzyme hydrolysis product of collagen (20%
Concentration) I Acid hydrolysis product of feather keratin (10% concentration) J Climatress K PPT “S-77” Example treatment solution L Hydrolysis product by trypsin (15% concentration) M Hydrolysis product by trypsin (15% concentration) 20% concentration) Note (1) All percentages are by weight. (2) Climatress is a trade name for an acid hydrolysis product of collagen commercially available from Redken Laboratories, California. (3) PPT "S-77" is the brand name of a conditioner containing acid-hydrolyzed polypeptide of collagen, which is also commercially available from Redken Laboratories. Two trained beauty experts graded each sample for compliance, volume and shine according to the criteria below.
Evaluation was made on a scale of 5 to 5. Obedience 1 Excellent: Suitable for styling, especially easy to comb and does not get messy. 2 Excellent: Easy to comb, style, and obedient. 3 Good... Somewhat easily disturbed. 4 Fair...Drugs are passable. Slightly stiff. 5 Not acceptable...Easily disturbed, lacks drag, stiff, and pine-like. Volume 1 Excellent...Beautiful and rich volume. 2 Excellent: Excellent feel, excellent elasticity. 3 Good: Contains a moderate amount of moisture, has a fair level of smoothness, has a moderate texture, is silky, and is soft. 4 Fair...The elasticity is fair, but it's a little dry. 5 Not acceptable...Dryness, lack of volume, oily, weak texture, and lack of smoothness. Gloss 1 Excellent...Beautiful and rich luster. 2 Excellent......completely excellent. 3 Good...Excellent. 4 Fair: Slightly glossy and slightly sticky. 5 Not acceptable: No gloss, no stains, and adhesive. Table 2 shows the analysis results of the treated control group samples. In this table, each analyst's evaluation is indicated by the first, second, and third numbers representing compliance, volume, and gloss analysis, respectively. In other words, scores of 1, 2, and 4 indicate excellent obedience;
It means that the volume is excellent and the gloss is fair. The lower the score, the better the quality of the hair〓〓〓〓
This means that The average treatment scores were calculated by computer and are also listed in Table 2. Examples 1L-8M Control Group Each of the eight subjects (#1-#8) who provided samples 1A-8K provided two hair samples for treatment with the solution of the present invention. In addition, Example Treatments L and M in Table 1 contain gelatin, which is collagen (trade name of Kind and Knowx Company).
225Bloom) was hydrolyzed with trypsin. Each sample was shampooed in the same manner as in Treatment B, and the aqueous solution shown in Table 1 was applied with a hair dye brush, left for 20 minutes, and then rinsed with tap water. The analysis results of the samples treated with the example treatments are shown in Table 2 in the same format as the control group samples. Comparing the results of the example samples with the results of the control group samples, it is clear from Table 2 that the cosmetic agent of the present invention can provide hair with superior flexibility, volume, and luster than conventional hair agents. . Examples Example-1 The properties of polypeptides obtained by hydrolyzing collagen by different means were compared. When collagen was hydrolyzed using trypsin as a catalyst and the resulting polypeptide was treated with carboxypeptidase B, the production of free arginine and lysine was observed. This indicates that the polypeptide has arginine or lysine residues at its ends. On the other hand, when the same collagen was hydrolyzed with acid to produce a polypeptide and this polypeptide was similarly treated with carboxypeptidase B, no free arginine or lysine was observed. This indicates that there are no terminal arginine or lysine residues on which carboxypeptidase B can act due to unregulated hydrolysis. Example-2 Comparative study of the effects on hair of the hair treatment cosmetic of the present invention containing a polypeptide prepared using trypsin and the hair treatment cosmetic containing a polypeptide prepared by acid hydrolysis. did. Two types of polypeptides obtained using trypsin were prepared for use in cosmetics of the present invention. 1
The first type is collagen produced by Kind & Notes Company under the trade name ``225Bloom'', which is hydrolyzed with trypsin. The other is casein produced by National Casein Company and hydrolyzed with trypsin. Hydrolysis is PH8,
The temperature was 40℃. On the other hand, a collagen hydrolyzate manufactured by Stepan Chemical Company was used for cosmetics in a comparative example. This collagen hydrolyzate is a polypeptide obtained by acid hydrolyzing collagen. As described in Example 1 above, this polypeptide has peptide bonds broken down in a disordered manner, so there are extremely few positively charged polypeptides that are free from steric hindrance. The three above-mentioned hydrolysates were prepared by Humble et al.
“Journal of Biological Chemistry” No. 248, 5532
- Labeled with tritium according to the procedure described on page 40 (1973). All replaceable hydrogen atoms of the polypeptide present in the hydrolyzate were replaced with tritium atoms. The specific radioactivity of tryptic hydrolyzate of casein is 245 μc/mg, and the specific radioactivity of tryptic hydrolyzate of collagen is 135
μc/mg, and the acid hydrolyzate of collagen is
It was 400 μm/mg. Corresponding peptide-containing non-radioactive hydrolyzate solutions with concentrations of 5%, 10%, 15% and 20% (each % by weight in distilled water) were prepared. That is, four different concentrations of non-radioactive samples were prepared for each polypeptide: collagen tryptic polypeptide, casein tryptic polypeptide, and collagen acid hydrolyzed polypeptide. The pH of each solution was adjusted to 4.3±0.1 with hydrochloric acid. A sufficient amount of the corresponding radioactively labeled polypeptide was applied at approximately 1×10 ⁸ dpm (disintegrations per minute).
It was added to each solution so that natural damaged hair, curling iron damaged hair,
Hair samples of 100 mg each were prepared for bleached damaged hair and permanently waved damaged hair. These hair samples were treated with Triton
100 (1%) (trade name of nonionic surfactant), rinse with distilled water, and air before weighing.
Dry. Each type of hair sample was soaked in 12 polypeptide solutions. There are 4 types of hair samples and 12 types of polypeptide solutions, so in total 48
of hair samples and 48 polypeptide solutions are required. After treatment with the polypeptide solution, each hair sample was rinsed five times with distilled water at 1 minute intervals to remove radioactive polypeptide that was not incorporated into the hair. Analysis of the rinse water confirmed that the radioactive polypeptide was completely removed. Of this hair sample, 2 samples of 10 mg were
Add 0.2 ml of distilled water to each of the above samples to which 1 ml of Solen 350 (trade name) was added, and place the samples in a scintillation container for 50 min.
℃ for 1 hour. After immersion, 10 ml of Aquasol Cocktail (trade name) was added and counted using a Beckman LS250 scintillation counter. The internal standard method was used to determine the effectiveness rate and the dpm (disintegrations per minute) was calculated. Table 3 shows the results obtained by averaging three sets of experimental values. According to these results, it can be seen that the amount of polypeptides obtained by hydrolysis with trypsin is significantly increased in the amount taken into the hair shaft compared to polypeptides obtained by acid hydrolysis. In other words, the uptake of tryptic polypeptide into collagen is 250% compared to the acid-hydrolyzed polypeptide of collagen.
The uptake of trypsin polypeptide in casein was also improved in the range of 460% to 1880% compared to the acid-hydrolyzed polypeptide of collagen.

[Table] Although the cosmetic agent of the present invention has been described above according to preferred embodiments and preferred methods of use, it will be obvious to those skilled in the art that other embodiments are possible. i.e. fragrance, zinc methionine (zinc)
Additives widely used in the art, such as chelating agents such as methionate, may also be added to cosmetic formulations. Furthermore, polypeptides obtained by methods other than trypsin-catalyzed hydrolysis may be added to the aqueous solution. Since various changes are possible in this way, the original
The spirit and scope of the present disclosure is not necessarily limited to the description of the preferred embodiments. 〓〓〓〓

[Table] 〓〓〓〓

Claims (1)

[Scope of Claims] 1. A keratin tissue treatment comprising an aqueous solution with a pH of about 2.5 to about 9 containing a sufficient amount of primarily two sterically unhindered positively charged polypeptides to produce a cosmetic effect. cosmetic agent for use, wherein the polypeptide has the structural formula in the above structural formula, where n is an integer sufficient to give the polypeptide a molecular weight of about 700 to about 1600, and each R ₁ is an independent side chain attached to the alpha carbon of a natural amino acid. group,
hydration of a protein, wherein R ₂ is selected from the group consisting of -(CH ₂ ) ₄ -NH ₃ and [Formula], and the polypeptide contains an amino acid selected from the group consisting of arginine, lysine, and a mixture of both. 1. A cosmetic agent for treating keratin tissue, which is prepared by decomposition, and mainly by protein hydrolysis using trypsin as a catalyst. 2. The cosmetic agent according to claim 1, wherein the pH of the aqueous solution is about 4 to about 5. 3. The cosmetic agent according to claim 1, wherein the aqueous solution contains a sterically unhindered polypeptide having two positive charges at a concentration of up to about 30% by weight. 4. The cosmetic agent according to claim 1, wherein the aqueous solution contains about 15 to 25% by weight of a polypeptide having two positive charges without steric hindrance. 5. Claim 1, wherein the aqueous solution is for hair shampoo containing a sterically unhindered polypeptide having two positive charges at a concentration of up to about 5% by weight.
Cosmetics listed in section. 6 The protein to be hydrolyzed is free of steric hindrance2
Stereometry for polypeptides that do not have positive charges
The cosmetic agent according to claim 1, which is selected to control the ratio of two positively charged polypeptides without any hindrance. 7. Claim 1, which is a hair conditioning cosmetic agent whose aqueous solution mainly contains 30% by weight or less of two sterically unhindered positively charged polypeptides and has a pH of about 4 to about 7. Cosmetics listed in section.