JPH0460083B2 - - Google Patents

Description

[Detailed description of the invention]

[Technical Field] The present invention relates to a novel hair protection agent. [Background Art] Various hair cosmetics such as shampoos, conditioners, and permanent waving agents are used for hair, but the use of these hair cosmetics may actually damage the hair. Even if a permanent wave agent is used, a part of the keratin protein that makes up the hair is eluted, and the remaining part of the hair undergoes physical and chemical changes, causing the hair to feel strange and dry. arise. In addition, because the surfactant contained in Shampoo has a strong surfactant ability, even the sebum and constituent proteins of the hair are eluted, damaging the hair and causing it to feel dry or coarse after drying. Become. The conditioner is used after shampooing to give the hair flexibility and natural shine.The main ingredients used in the conditioner are long-chain alkyltrimethylammonium chloride with 16 to 18 carbon atoms, Dialkyl trimethyl ammonium chloride, alkyl dimethyl benzyl ammonium chloride, etc. have strong surfactant ability, so if they are used in large quantities, sebum and constituent proteins of the hair will be eluted, as in the case of shampoo, and they will actually damage the hair. begins to feel dry or rough. [Object of the Invention] In view of the above-mentioned circumstances, an object of the present invention is to provide a hair protectant that prevents hair damage caused by these hair cosmetics and protects the hair. [Summary of the invention] The present invention is based on the general formula () (In the formula, R is a side chain of an amino acid constituting a polypeptide derived from animal protein, and n
is 3 to 20). The quaternary trimethylammonium-derived polypeptide represented by the above general formula () has a polypeptide portion derived from animal proteins such as collagen, keratin, and silk protein, and has a chemical structure similar to that of hair. In addition to having the effect of adsorbing to the hair through the action of its amino groups, carboxyl groups, and side chains of various amino acids, it has the effect of protecting the hair and regenerating damaged hair.
The quaternization greatly improves adsorption to the hair, giving the hair a high degree of flexibility and natural luster. A hair protectant made of a quaternary trimethylammonium-derived polypeptide represented by the general formula () is obtained by dissolving the quaternary trimethylammonium-derived polypeptide in water or a base mainly composed of water, and adding an emulsifier if necessary. , a wetting agent, a preservative, a fragrance, a coloring agent, a chelating agent, and various anionic, cationic, and nonionic surfactants may be appropriately added before use. It may be used before, during or after use of other hair cosmetics, or may be used alone regardless of the use of other hair cosmetics. In addition, hair dye, bleach, shampoo, hair rinse, hair treatment,
It may be added to various hair cosmetics such as hair conditioners, hair packs, and permanent waving agents. The above-mentioned water-based base refers to alcohols or polyhydric alcohols such as ethyl alcohol, ethylene glycol, propylene glycol, butylene glycol, glycerin, and polyols, as well as quaternary trimethylammonium represented by the general formula (). Water is added to the extent that it does not inhibit the dissolution of the induced polypeptide, and the amount of water is usually 50% by weight or more of the total amount. When used, the concentration of the quaternary trimethylammonium-derived polypeptide represented by the general formula () is 2 to 2.
About 20% by weight is preferable. The polypeptide portion in the general formula () includes collagen, keratin, proteins constituting silk (silk protein), elastin, actin,
It is derived from animal proteins such as myosin, and the amino acids whose side chains are represented by R in the general formula () include alanine, glycine, valine, leucine, isoleucine, proline, phenylalanine, and tyrosine. , serine, threonine, methionine, arginine, histidine, lysine, aspartic acid, asparagine, glutamic acid, glutamine, cystine, cysteic acid, tributophane, hydroxyproline, hydroxylysine, and the like. Table 1 shows an example of the composition ratio of these amino acids.

【table】

〔Example〕

Next, the present invention will be explained in more detail with reference to reference examples (manufacturing examples of animal protein-derived polypeptides and manufacturing examples of quaternary trimethylammonium-derived polypeptides) and examples. Reference example 1 Production of collagen-derived polypeptide Reference example 1-1 (Acid hydrolysis) Add 700 g of water to 300 g of powdered gelatin, dissolve while heating, add 60 g of concentrated hydrochloric acid at 70°C, and stir for 1 hour. After hydrolysis, the reaction mixture was filtered, the filtrate was diluted to 2 with water, and the weakly basic anionic exchange resin Diaion WA20 (trade name,
The solution was neutralized by passing it through a 290 ml resin column (Mitsubishi Chemical Industries, Ltd.). This was concentrated under reduced pressure and filtered to obtain an aqueous solution of collagen-derived polypeptide with a concentration of 40%.
The molecular weight of the collagen-derived polypeptide thus obtained was measured by gel filtration and found to have an average molecular weight of 900. Reference Example 1-2 (Alkaline hydrolysis) Dissolve 500 g of plate gelatin while heating 700 g of 6% sodium hydroxide aqueous solution, perform hydrolysis for 1 hour while stirring at 80°C, and then filter the reaction mixture. Then, dilute the filtrate to 2 with water and add weakly acidic cation exchange resin Amberlite IRC-50 (trade name,
The solution was neutralized by passing it through a 500 ml resin column manufactured by Organo Co., Ltd.
This was concentrated under reduced pressure and filtered to obtain an aqueous solution of collagen-derived polypeptide with a concentration of 35%. The molecular weight of the collagen-derived polypeptide thus obtained was measured by gel filtration and found to have an average molecular weight of 500. Reference Example 1-3 (Enzymatic degradation) Add 650 g of water to 350 g of granular gelatin, heat to 50°C to dissolve the gelatin, then add 20 mg of the neutral proteolytic enzyme papain, and stir at 50°C for 3 hours. After hydrolysis, the reaction mixture was filtered to obtain an aqueous solution of collagen-derived polypeptide with a concentration of 35%. The molecular weight of the collagen-derived polypeptide thus obtained was measured by gel filtration and found to have an average molecular weight of 1,700. Reference example 2 Reference example of production of keratin-derived polypeptide 2-1 (Acid hydrolysis) 450 g of 35% hydrochloric acid to 500 g of wool in a three-necked flask
was added and hydrolysis was carried out under stirring at 80°C for 16 hours. After hydrolysis, the reaction mixture was filtered, and the filtrate was neutralized with 1400 ml of a weakly basic anion exchange resin Diaion WA20 (described above), concentrated, and filtered to remove the ion exchange resin, yielding keratin with a concentration of 40%. An aqueous solution of induced polypeptide was obtained. The molecular weight of the keratin-derived polypeptide thus obtained was measured by gel filtration, and the average molecular weight was found to be
It was 800. Reference Example 2-2 (Alkaline hydrolysis) Add 100 g of sodium hydroxide and 3 kg of water to 500 g of pig hair, leave it at 40°C for 24 hours to perform hydrolysis, then filter the reaction mixture and make the filtrate into a weakly acidic solution. Cation exchange resin Amberlite IRC-50 (mentioned above) 600ml
It was neutralized by After concentrating this, the ion exchange resin was removed by filtration to obtain an aqueous solution of keratin-derived polypeptide with a concentration of 40%. The molecular weight of the keratin-derived polypeptide thus obtained was measured by gel filtration and found to have an average molecular weight of 1200. Reference Example 2-3 (Enzyme Hydrolysis) 500 g of feathers was treated with superheated steam at 200° C. at 10 kg/cm ² in a high-pressure container for 30 minutes, and then released into the atmosphere to obtain a porous puffed feather product. 3 kg of water was added to this, 30 g of papain was added, and hydrolysis was carried out at 40°C for 24 hours. After hydrolysis, the reaction mixture is filtered,
The filtrate was concentrated under reduced pressure to obtain keratin-derived polypeptide with a concentration of 40%. The molecular weight of the keratin-derived polypeptide thus obtained was measured by gel filtration and found to have an average molecular weight of 600. Reference Example 3 Production of Silk Protein-Induced Polypeptide Reference Example 3-1 (Alkaline Hydrolysis) Place 1.5 liters of 2N sodium hydroxide in 2 beakers and add 500 g of dried silkworm cocoons (wash them in advance to remove silkworm feces and dirt). Add as much of the remaining cocoon as possible, heat to 80°C, and while stirring, dissolve the cocoon by hydrolysis, and add the remaining cocoon. After adding the entire amount of cocoon for 30 minutes, the mixture was further heated to 80°C and stirred for 1 hour to complete hydrolysis. The reaction product was diluted by adding 1 part of water, and then filtered under reduced pressure. The filtrate was treated with weakly acidic cation exchange resin Amberlite IRC-50 (mentioned above).
The solution was neutralized by passing through a 1300 ml resin tower, concentrated under reduced pressure, and filtered to obtain an aqueous solution of silk protein-derived polypeptide with a concentration of 30%. The molecular weight of the silk protein-derived polypeptide thus obtained was measured by gel filtration, and the average molecular weight was found to be
It was 500. Reference example 3-2 (Acid hydrolysis) 1.0 kg of commercially available 55% lithium bromide aqueous solution
After adding and dissolving 200 g of unspun silk fiber at 50°C, this solution was diluted with ion-exchanged water to a total of 2.0 kg. This liquid was heated to 80° C. and stirred in two three-necked flasks, and 25 g of concentrated hydrochloric acid was added thereto for hydrolysis for 2 hours. After cooling, 48 g of a 20% aqueous sodium hydroxide solution was added to neutralize the mixture, followed by filtration under reduced pressure. The filtrate was subjected to electrodialysis, desalted, concentrated under reduced pressure and filtered to obtain an aqueous solution of silk protein-derived polypeptide with a concentration of 35%. The molecular weight of the silk protein-derived polypeptide thus obtained was measured by gel filtration and found to have an average molecular weight of 1800. Reference example 3-3 (enzymatic hydrolysis) 300g of washed silkworm cocoon was placed in a high-pressure container for 10 minutes.
Kg/cm ² , treated with superheated steam at 200°C for 1 hour to swell, then placed in two beakers, added 1 part of 0.1N sodium acetate buffer (PH6), and brought to 40°C.
20 mg of papain, a neutral proteolytic enzyme, was added. 40℃
Hydrolysis was carried out for 12 hours. After the reaction mixture was filtered to remove undecomposed residues, the filtrate was concentrated under reduced pressure to obtain an aqueous solution of silk protein-derived polypeptide with a concentration of 30%. The molecular weight of the silk protein-derived polypeptide thus obtained was measured by gel filtration and found to have an average molecular weight of 1050. Reference Example 4 Production of quaternary trimethylammonium-derived collagen polypeptide Reference Example 4-1 700 g of the 40% concentration collagen-derived polypeptide aqueous solution obtained in Reference Example 1-1 (average molecular weight of collagen-derived polypeptide 900, amino form) A total amount of nitrogen (310 mmol) was placed in a reaction vessel, and 35
103 g of CTA aqueous solution with a concentration of 51% while stirring at °C.
(0.9 equivalent of amino titanium of collagen-derived polypeptide) was added dropwise over a period of 30 minutes, and during that time, a 20% aqueous sodium hydroxide solution was appropriately added dropwise to maintain the pH of the reaction solution at 10.0. After finishing dropping CTA,
Stirring was continued for 2 hours while maintaining the pH at 10.0, and then the amino nitrogen was measured after being left for 24 hours. The total amount of amino nitrogen was 42 mmol, and 84% of the amino nitrogen had reacted. Was. Next, 170 ml of weakly acidic cation exchange resin Amberlite IRC-50 (mentioned above) was added to the reaction solution to neutralize it to pH 6.5, and the sodium ions in the reaction solution and the slight remaining unreacted CTA were removed. It is adsorbed onto an ion exchange resin, and then the ion exchange resin is removed to reduce the concentration.
A 30% aqueous solution of quaternary trimethylammonium-derived collagen polypeptide was obtained. When the obtained aqueous solution was subjected to a characteristic reaction of quaternary ammonium salt, a white precipitate was produced by sodium tetraphenylboronate, and a red precipitate was produced by Dragendorff's reagent, which showed a positive result. In addition, collagen-induced polypeptides and
To make sure it is combined with the CTA,
Using the obtained aqueous solution, gel filtration (G-25, manufactured by Fumarmacia) was performed, and the above-mentioned characteristic reaction was performed for each molecular weight fraction, and each fraction was found to be a characteristic reaction of quaternary ammonium salt. was positive, confirming that collagen-induced polypeptide and CTA were bound together. Reference Example 4-2 1 kg of the collagen-derived polypeptide aqueous solution with a concentration of 35% obtained in Reference Example 1-2 (average molecular weight of collagen-derived polypeptide 500, total amount of amino nitrogen 697 mmol) was placed in a reaction vessel and stirred. At the same time, 228 g of CTA aqueous solution with a concentration of 49% (0.85 g of amino nitrogen of collagen-derived polypeptide)
equivalent amount) over 30 minutes, and during that time 20%
Add an appropriate amount of sodium hydroxide aqueous solution to the reaction solution.
PH was maintained at 9.5. After dropping CTA, adjust the pH to 9.5.
Stirring was continued for 5 hours while maintaining the temperature, and then after being left for 24 hours, the amount of amino titanium was measured, and the total amount of amino titanium was 147 mmol.
79 of the amino-form titanium reacted. Next, the reaction solution was added to the strongly acidic cation exchange resin Diamond SK-
1B (product name, Mitsubishi Chemical Industries, Ltd.) is passed through a 320 ml resin column, neutralized to pH 6.9, and the sodium ions in the reaction solution and the slight remaining unreacted CTA are transferred to the ion exchange resin. The ion exchange resin was then removed to obtain an aqueous solution of quaternary trimethylammonium-derived collagen polypeptide with a concentration of 30%. When the obtained aqueous solution was subjected to a quaternary ammonium salt characteristic reaction in the same manner as in Reference Example 4-1, all results were positive. In addition, using the obtained aqueous solution, gel filtration was performed in the same manner as in Reference Example 4-1, and a quaternary ammonium salt characteristic reaction was performed on each molecular weight fraction. It was confirmed that the and CTA were combined. Reference Example 4-3 800 g of the collagen-induced polypeptide aqueous solution with a concentration of 35% obtained in Reference Example 1-3 (average molecular weight of collagen-induced polypeptide 1700, total amount of amino nitrogen 140 mmol) was placed in a reaction vessel,
CTA aqueous solution with a concentration of 49% while stirring at 63.1 °C.
g (1.0 equivalent of amino titanium of collagen-derived polypeptide) was added dropwise over 1 hour, and
During that time, a 20% aqueous sodium hydroxide solution was appropriately added dropwise to maintain the pH of the reaction solution at 11.0. After dropping CTA, stirring was continued for 3 hours while maintaining the pH at 11.0, and then after being left for 24 hours, the amount of amino nitrogen was measured, and the total amount of amino nitrogen was 14 mmol. 90% of the elements were reacting. Next, 120 ml of a weakly acidic cation exchange resin Amberlite IRC-50 (mentioned above) was added to the reaction solution, and the sodium ions in the reaction solution and the slight remaining unreacted CTA were adsorbed onto the ion exchange resin, and then the ion exchange resin The exchange resin was removed to obtain an aqueous solution of quaternary trimethylammonium-derived collagen polypeptide with a concentration of 30%. When the obtained aqueous solution was subjected to a quaternary ammonium salt characteristic reaction in the same manner as in Reference Example 4-1, all results were positive. In addition, using the obtained aqueous solution, gel filtration was performed in the same manner as in Reference Example 4-1, and a quaternary ammonium salt reaction was performed on each molecular weight fraction. It was confirmed that the and CTA were combined. Reference Example 5 Production of Quaternary Trimethylammonium-Derived Keratin Polypeptide Reference Example 5-1 900 g of the 40% concentration keratin-derived polypeptide aqueous solution obtained in Reference Example 2-1 (average molecular weight of keratin-derived polypeptide 800, amino form) A total of 430 mmol of nitrogen) was placed in a reaction vessel, and while stirring, 148 g of a 49% CTA aqueous solution (0.9 equivalent of amino nitrogen of keratin-derived polypeptide) was added.
was added dropwise over 30 minutes, and during that time, 20% sodium hydroxide aqueous solution was added dropwise to bring the pH of the reaction solution to 10.0.
maintained. After dropping CTA, stirring was continued for 2 hours while maintaining the pH at 10.0, and then after being left for 24 hours, the amount of amino nitrogen was measured, and the total amount of amino nitrogen was 52 mmol. 88% of the base reacted. Next, add a weakly acidic cation exchange resin Amberlite IRC-50 to the reaction solution.
(Previous) Add 200 ml, neutralize to pH 6.5, adsorb sodium ions in the reaction solution and a slight amount of unreacted CTA to the ion exchange resin, then remove the ion exchange resin to reduce the concentration. A 30% aqueous solution of quaternary trimethylammonium-derived keratin polypeptides was obtained. The obtained aqueous solution was subjected to a quaternary ammonium salt characteristic reaction in the same manner as in Reference Example 4-1, and all results were positive. In addition, using the obtained aqueous solution, gel filtration was performed in the same manner as in Reference Example 4-1, and a quaternary ammonium salt reaction was performed on each molecular weight fraction. It was confirmed that the and CTA were combined. Reference Example 5-2 900 g of the 40% concentration keratin-derived polypeptide aqueous solution obtained in Reference Example 2-2 (average molecular weight of keratin-derived polypeptide 1200, total amount of amino nitrogen 272 mmol) was placed in a reaction container and stirred. Meanwhile, 88.7 g of CTA aqueous solution with a concentration of 49 ((0.85 equivalent of amino titanium of keratin-derived polypeptide) was added dropwise over 30 minutes, and during that time, 20% sodium hydroxide aqueous solution was added dropwise as needed to dilute the reaction solution. PH
was maintained at 10.5. After dropping CTA, reduce the pH to 10.5
Stirring was continued for 2 hours while maintaining the temperature, and then after being left for 24 hours, the amino nitrogen was measured, and the total amount of amino nitrogen was 61 mmol.
78% of amino titanium reacted. Next, add the strongly acidic cation exchange resin Diaion SK to the reaction solution.
Add 200 ml of -1B (described above), neutralize to pH 6.9, adsorb sodium ions in the reaction solution and a small amount of unreacted CTA to the ion exchange resin, and then remove the ion exchange resin. An aqueous solution of quaternary trimethylammonium-induced keratin polypeptides with a concentration of 30% was obtained. When the obtained aqueous solution was subjected to a quaternary ammonium salt characteristic reaction in the same manner as in Reference Example 4-1, all results were positive. In addition, using the obtained aqueous solution, gel filtration was performed in the same manner as in Reference Example 4-1, and a quaternary ammonium salt reaction was performed on each molecular weight fraction. It was confirmed that the and CTA were combined. Reference Example 5-3 700 g of the 40% concentration keratin-derived polypeptide aqueous solution obtained in Reference Example 2-3 (average molecular weight of keratin-derived polypeptide 600, total amount of amino nitrogen 431 mmol) was placed in a reaction container and stirred. Meanwhile, 165 g of CTA aqueous solution with a concentration of 49% (1.0 equivalent of amino nitrogen of keratin-derived polypeptide)
was added dropwise over 1 hour, and during that time, 20% sodium hydroxide aqueous solution was added dropwise to adjust the pH of the reaction solution.
I kept it at 11.0. After dropping CTA, stirring was continued for 2 hours while maintaining the pH at 11.0, and then left to stand for 24 hours. Amino titanium was measured.
The total amount of amino titanium was 40 mmol, and 93% of the amino titanium was reacted. Next, add a weakly acidic cation exchange resin Amberlite IRC- to the reaction solution.
50 (mentioned above) to adsorb the sodium ions in the reaction solution and a small amount of unreacted CTA to the ion exchange resin, then remove the ion exchange resin to obtain quaternary trimethyl at a concentration of 30%. An aqueous solution of ammonium-induced keratin polypeptides was obtained. When the obtained aqueous solution was subjected to a quaternary ammonium salt characteristic reaction in the same manner as in Reference Example 4-1, all results were positive. In addition, using the obtained aqueous solution, gel filtration was performed in the same manner as in Reference Example 4-1, and a quaternary ammonium salt reaction was performed on each molecular weight fraction. It was confirmed that the and CTA were combined. Reference Example 6 Production of quaternary trimethylammonium-derived silk polypeptide Reference Example 6-1 1.2 kg of the 30% concentration silk protein-derived polypeptide aqueous solution obtained in Reference Example 3-1 (average molecular weight of silk protein-derived polypeptide 500) , total amount of amino-form titanium (730 mmol) was placed in a reaction vessel, heated to 40°C, and mixed with a 50% concentration CTA aqueous solution 247 while stirring.
g (0.9 equivalents of amino nitrogen of silk protein-derived polypeptide) was added dropwise over 30 minutes, and during that time, 20% aqueous sodium hydroxide solution was appropriately added dropwise to maintain the pH of the reaction solution at 10.0. After finishing dropping CTA,
Stirring was continued for 2 hours while maintaining the pH at 10.0, and then the amino nitrogen was measured after being left for 24 hours. The total amount of amino nitrogen was 81 mmol, and 89% of the amino nitrogen had reacted. Was. Next, 100 ml of weakly acidic cation exchange resin Amberlite IRC-50 (mentioned above) was added to the reaction solution to neutralize the pH to 6.7, removing the sodium ions and slightly remaining unreacted CTA in the reaction solution. Adsorb onto ion exchange resin, then remove ion exchange resin to a concentration of 30
% of quaternary trimethylammonium-derived silk polypeptide was obtained. When the obtained aqueous solution was subjected to a quaternary ammonium salt characteristic reaction in the same manner as in Reference Example 4-1, all results were positive. In addition, using the obtained aqueous solution, gel filtration was performed in the same manner as in Reference Example 4-1, and a quaternary ammonium salt characteristic reaction was performed on each molecular weight fraction. It was confirmed that the peptide and CTA were bound together. Reference Example 6-2 500 g of the 35% concentration silk protein-derived polypeptide aqueous solution obtained in Reference Example 3-2 (average molecular weight of silk protein-derived polypeptide 1800, total amount of amino nitrogen 95 mmol) was placed in a reaction vessel. , While stirring, 30.4 g of CTA aqueous solution with a concentration of 49% (0.85 equivalent of amino titanium of silk protein-derived polypeptide) was added dropwise over 1 hour, and during that time, 20% sodium hydroxide aqueous solution was added dropwise as appropriate. PH of reaction solution
was maintained at 10.0. After dropping CTA, adjust the pH to 10.0.
Stirring was continued for 2 hours while maintaining the temperature, and then after being left for 24 hours, the amount of amino titanium was measured, and the total amount of amino titanium was 17 mmol.
82% of amino titanium reacted. Next, add the strongly acidic cation exchange resin Diaion SK to the reaction solution.
Add 80 ml of -1B (described above), neutralize to pH 6.9, adsorb sodium ions in the reaction solution and a small amount of unreacted CTA to the ion exchange resin, and then remove the ion exchange resin. An aqueous solution of quaternary trimethylammonium-derived silk polypeptide with a concentration of 30% was obtained. When the obtained aqueous solution was subjected to a quaternary ammonium salt characteristic reaction in the same manner as in Reference Example 4-1, all results were positive. In addition, using the obtained aqueous solution, gel filtration was performed in the same manner as in Reference Example 4-1, and a quaternary ammonium salt characteristic reaction was performed on each molecular weight fraction. It was confirmed that the peptide and CTA were bound together. Reference Example 6-3 800 g of the 30% concentration silk protein-derived polypeptide aqueous solution obtained in Reference Example 3-3 (average molecular weight of silk protein-derived polypeptide 1050, total amount of amino titanium 226 mmol) was placed in a reaction vessel. While stirring, 87.7 g of CTA aqueous solution with a concentration of 49% (1.0 equivalent of amino titanium of silk protein-derived polypeptide) was added dropwise over 1 hour, and during that time, 20% sodium hydroxide aqueous solution was added dropwise as appropriate. PH of reaction solution
was maintained at 11.0. After dropping CTA, adjust the pH to 11.0.
Stirring was continued for 2 hours while maintaining the temperature, and then after being left for 24 hours, the amount of amino titanium was measured, and the total amount of amino titanium was 18 mmol.
92% of amino titanium reacted. Next, add the weakly acidic cation exchange resin Amberlite to the reaction solution.
Add 150 ml of IRC-50 (described above), and add sodium ions in the reaction solution and the slight remaining unreacted
CTA was adsorbed onto an ion exchange resin, and then the ion exchange resin was removed to obtain an aqueous solution of quaternary trimethylammonium-derived silk polypeptide with a dry residue of 30%. When the obtained aqueous solution was subjected to a quaternary ammonium salt characteristic reaction in the same manner as in Reference Example 4-1, all results were positive. In addition, using the obtained aqueous solution, gel filtration was performed in the same manner as in Reference Example 4-1, and a quaternary ammonium salt characteristic reaction was performed on each molecular weight fraction. It was confirmed that the peptide and CTA were bound together. Examples 1 to 9 Using the quaternary trimethylammonium-derived polypeptides obtained in Reference Examples 4 to 6, hair protection agents having the formulations shown in Table 2 were prepared. The blending amount is shown in parts by weight. The same applies hereafter. In addition, the fourth
Table 2 also shows the composition of Control Product 1, which does not contain grade trimethylammonium-derived polypeptide. A hair bundle weighing 1 g was immersed in 30 g of the hair protectant having each of the above compositions for 10 minutes, rinsed, and the hair bundle was separately prepared with the first agent 70 for permanent waves.
After rinsing, it was immersed in 100 g of the second agent for permanent wave for 15 minutes.
The gloss, suppleness, and combability of the hair after treatment were sensory evaluated. Furthermore, the amount of cysteic acid in the hair after treatment is shown in Table 3. Cysteic acid in hair is produced from cystine in hair during permanent wave treatment, and the amount of cysteic acid produced indicates the degree of damage to the hair, and it is said that the greater the amount produced, the greater the damage to the hair. The evaluation criteria used for the sensory evaluation are as follows. ◎: Particularly good ○: Good △: Fair ×: Poor An amino acid automatic analyzer was used to measure the amount of cysteic acid. The formulation composition of the first agent for permanent waves and the formulation composition of the second agent for permanent waves used are as shown in Table 4.

【table】

【table】

【table】

【table】

[Table] Examples 10 to 18 Hair protection agents having the formulation shown in Table 5 were prepared,
The effect was confirmed as shown below. 20g of hair protectant of each composition above and 80g of bleaching solution prepared separately
A hair bundle weighing 1 g was immersed in the solution for 30 minutes, rinsed, and further dried to decolorize the hair. The shine and suppleness of the hair after treatment,
The combability was sensory evaluated. Furthermore, Table 6 shows the results of measuring the amount of cysteic acid in the hair after treatment. Cysteic acid in hair is produced from cystine in hair through oxidation due to bleaching, and the amount of cysteic acid produced indicates the degree of damage to the hair, and it is said that the greater the amount produced, the greater the damage to the hair. The evaluation criteria used for the sensory evaluation were the same as in Example 1.
Further, cysteic acid was measured in the same manner as in Example 1. Decolorizing agent composition 35% hydrogen peroxide 20.0 25% ammonia water 7.0 Polyoxyethylene 1.0 Cetyl ether EDTA 0.1 Purified water 71.9

【table】

[Table] Next, 70 parts of a separately prepared hair dye was mixed with 30 parts of a hair protectant having the composition shown in Table 5 of Examples 10 to 18, and dyed using a panel of 10 professional women. I did hair. A tensile test was conducted on the hair before and after treatment on each panel to determine the degree of damage to the hair, and the percentage decrease in tensile strength is shown in Table 7. Also, Example 1
Cysteic acid was determined in the same manner as above, and the results are shown in Table 7. Furthermore, a sensory test was conducted regarding hair gloss and dyeing (color, uneven dyeing, etc.), and the results are shown in Table 7. The evaluation method of the sensory test was the same as in Example 1. To measure the tensile strength, use a rheometer (manufactured by Mitsuwa Rikagaku Kogyo Co., Ltd.) to fix each 2 cm long hair, and pull at a pulling speed of 2 cm/min until the hair is completely cut. , the maximum load at the moment of cutting was measured. Ten hairs from each person were measured before and after treatment, and the rate of decrease in tensile strength was determined from the average value. Hair dye Sodium lauryl sulfate (30% aqueous solution) 25.0 Polyoxyethylene stearate (5) 8.0 Sorbitan ester 30%) Lecithin 1.5 25% ammonia water 8.0 1,3-butylene glycol 3.0 Isopropanol 2.5 Paraphenylene diamine 0.7 Para-aminophenol 0.15 4-Nitro-1,2-diaminobenzene 0.3 Pyrogallol 0.7 Resorcinol 0.2 Hydroquinone 0.1 Purified water 49.85

〔Effect of the invention〕

As explained above, the hair protection agent of the present invention exhibits an excellent hair protection effect and prevents hair damage.

Claims (1)

[Claims] 1 General formula () (In the formula, R is a side chain of an amino acid constituting a polypeptide derived from animal protein, and n
is 3 to 20).