JPH0460088B2 - - Google Patents

Description

[Detailed description of the invention]

[Technical Field] The present invention relates to a novel first agent for permanent waves that can impart excellent waving effects without damaging the hair or scalp. [Background Art] Conventional permanent waving agents are made by adding ammonia, monoethanolamine,
Adding a basic substance such as triethanolamine
The first agent is one whose pH is adjusted to 8 to 10, and the second agent is an aqueous solution of an oxidizing agent such as sodium bromate or hydrogen peroxide. The mechanism of waving hair with this permanent waving agent is to fix the hair to a rod or the like and curl the hair, and then use the first agent to remove cystine disulfide contained in the keratin protein in the hair. By reducing the bonds, they are cut into mercapto groups to loosen the protein chains in the hair, and then the mercapto groups are oxidized by a second agent to generate disulfide bonds at new positions in the hair, resulting in waves. It is intended to be fixed. However, in permanent waves using such conventional drugs, the disulfide bonds of cystine that are cleaved by the reducing agent of the first agent are completely restored to their original state by oxidation by the second agent, and the cystine is then oxidized. Some of the mercapto groups generated from cystine by treatment with the first agent may be overoxidized by the second agent, or may be oxidized by the thioglycolic acid or cysteine remaining in the hair. Side reactions occur such as reacting with mercapto groups to form disulfide bonds, which causes part of the keratin protein in the hair to elute, and the remaining part of the hair to undergo physical and chemical changes and other damage. arise. As a result, not only does the hair feel strange and dry, but the hair is also severely damaged. The degree of hair damage is related to the waving effect; for example, the first agent containing thioglycolic acid or its salt as a main ingredient has an excellent waving effect, but it also causes significant hair damage. The first agent, which is large and mainly contains cysteine, causes less hair damage but does not have a very large waving effect. In addition, in the past, first agents for permanent waves based on sulfite or bisulfite were used, but the reduction reaction with these was as shown below: keratin-S-S-keratin + HSO ₃ ^-keratin -SH + keratin - SSO ₃ ^- , and the disulfide bond is cleaved to a mercapto group on one side and an SSO ₃ ^- group on the other, so it is difficult to regenerate the disulfide bond by oxidation, and the above reduction-oxidation reaction is slow. , which generally heats the hair, causing more damage to the hair. [Object of the Invention] In view of the above-mentioned circumstances, an object of the present invention is to provide a first agent for permanent waving that can impart excellent waving effects without damaging the hair or scalp. [Structure of the Invention] The present invention has been made in order to eliminate the drawbacks of the conventional first agent for permanent waves as described above. (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) with at least one reducing agent selected from the group consisting of thioglycolic acid, thioglycolate, cysteine, sulfite, and bisulfite. It is designed to be used in combination with The quaternary trimethylammonium-derived polypeptide represented by the above general formula () is one whose polypeptide portion is derived from animal proteins such as collagen, keratin, and proteins constituting silk (silk protein). It has a chemical structure similar to that of hair, and has the effect of adsorbing to hair through the action of its amino groups, carboxyl groups, and side chains of various amino acids, protecting hair, and regenerating damaged hair. In addition, due to the quaternization, the adsorption to the hair is greatly improved, giving the hair a high degree of softness and natural luster. Therefore, when this quaternary trimethylammonium-derived polypeptide is blended into the first agent for permanent waves, the quaternary trimethylammonium-derived polypeptide is adsorbed to the hair, and the quaternary trimethylammonium-derived polypeptide is adsorbed to the hair.
The grade trimethylammonium-derived polypeptide remains on the hair without being washed away even by gentle rinsing before the second agent treatment, suppressing excessive oxidation caused by the second agent and side reactions with reducing agents such as thioglycolic acid. and greatly reduce hair damage. The polypeptide moiety in the general formula () is derived from animal proteins such as collagen, keratin, silk protein, elastin, actin, myosin, etc., and its side chain is represented by R in the general formula (). Amino acids include alanine, glycine, valine, leucine, isoleucine, proline, phenylalanine, tyrosine, serine, threonine, methionine, arginine, histidine, lysine, aspartic acid, asparagine, glutamic acid, glutamine, cystine, cysteic acid, tryptophan, Examples include hydroxyproline and hydroxylysine.
An example of the composition ratio of these amino acids is shown in Table 1.

〔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 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 hydrolyze for 1 hour while stirring. After that, the reaction mixture was filtered, the filtrate was diluted to 2 with water, and the weakly basic anion 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, the filtrate was diluted to 2 with water, and the 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 be 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 Silk protein-derived polypeptide reference example 3-1 (alkaline hydrolysis) 2Pour 1.5 liters of 2N sodium hydroxide into a beaker, add 500g of dried silkworm cocoons (washed in advance to remove silkworm droppings and dirt) A portion of the cocoon) was added as much as possible, heated to 80°C, and stirred to dissolve the cocoon by hydrolysis, and the remaining cocoon was added. 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 column, 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 in two three-necked flasks and stirred, and 25 g of concentrated hydrochloric acid was added 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 is subjected to electrodialysis, desalted, and then concentrated under reduced pressure.
It was 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), heated to 40°C,
20 mg of papain, a neutral proteolytic enzyme, was added. 40℃
Hydrolysis was carried out for 2 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 was 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 and slightly remaining unreacted CTA in the reaction solution were ionized. Adsorb onto exchange resin, then remove ion exchange resin to reduce concentration to 30%
An 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 Pharmacia) 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 the 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 the amino nitrogen was measured after being left for 24 hours. The total amount of amino nitrogen was 147 mmol, and 79% of the amino nitrogen had reacted. Ta. Next, the reaction solution was mixed with a strongly acidic cation exchange resin, Diamond Ion.
SK-1B (trade 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 was adsorbed onto an ion exchange resin, and then the ion exchange resin was removed to obtain an aqueous solution of quaternary trimethylammonium-derived collagen polypeptide at 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-derived polypeptide aqueous solution with a concentration of 35.0% obtained in Reference Example 1-3 (average molecular weight of collagen-derived polypeptide 1700, total amount of amino nitrogen 140 mmol) was placed in a reaction container,
CTA aqueous solution with a concentration of 49% while stirring at 30℃
63.1 g (1.0 equivalent of amino titanium of collagen-derived polypeptide) was added dropwise over 1 hour, and during this time, 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 left for 24 hours. When the amino nitrogen was measured, the total amount of amino nitrogen was 14.
mmol, and 90% of the amino titanium was reacted. Next, 120 ml of 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.
Then, the ion exchange resin was removed and a fourth sample with a concentration of 30% was added.
An aqueous solution of grade trimethylammonium-derived collagen 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 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 to the reaction vessel.
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 left to stand for 24 hours. When the amino nitrogen was measured, the total amount of amino nitrogen was 52 mmol. 88% of the base reacted. Next, add the weakly acidic cation exchange resin Amberlite IRC-5 to the reaction solution.
(Previous) Add 220 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 a concentration of 30. % quaternary trimethylammonium-derived keratin polypeptide 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 reactor and stirred. Meanwhile, 88.7 g of CTA aqueous solution with a concentration of 49% (0.85 equivalent of amino nitrogen 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 200ml of -1B (previously), neutralize to pH 6.9, adsorb the sodium ions in the reaction solution and unreacted CTA remaining on the ion exchange resin, and then remove the ion exchange resin. An aqueous solution of quaternary trimethylammonium-derived keratin polypeptides having 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 as needed to dilute the reaction solution. PH
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 40 mmol.
93% of amino titanium reacted. Next, add the weakly acidic cation exchange resin Amberlite to the reaction solution.
Add 100 ml of IRC-50 (described above), and remove the sodium ions in the reaction solution and the slight amount of 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 keratin polypeptides 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 6 Production of quaternary trimethylammonium-derived silk polypeptide Reference Example 6-1 1200 g of silk protein-derived polypeptide obtained in Reference Example 3-1 with a concentration of 30% (average molecular weight of silk protein-derived polypeptide 500, amino Total amount of titanium
730 mmol) was placed in a reaction vessel, heated to 40°C, and while stirring, 247 g of CTA aqueous solution with a concentration of 50% (amino titanium of silk protein-derived polypeptide) was added to a reaction vessel.
0.9 equivalent) over 30 minutes, and during that time 20
% sodium hydroxide aqueous solution was added dropwise as appropriate to maintain the pH of the reaction solution at 10.0. After finishing dropping CTA, PH
Continue stirring for 2 hours while maintaining the temperature at 10.0, then
After standing for 24 hours, the amino titanium was measured, and the total amount of amino titanium was 81 mmol, indicating that 89% of the amino titanium had reacted. 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.
The sodium ions in the reaction solution and the slight remaining unreacted CTA are adsorbed onto the ion exchange resin.
The ion exchange resin was then removed to obtain an aqueous solution of quaternary trimethylammonium-derived polypeptide having 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 it binds to peptide and CTA. 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 nitrogen 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 at 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 peptide and CTA were bound together. Examples 1 to 9 Using the quaternary trimethylammonium-derived polypeptides obtained in Reference Examples 4 to 6, first agents for permanent waves having the formulations shown in Table 2 were prepared.
The amount of each component is shown in parts by weight. The same applies to the following. In the table, the type of quaternary trimethylammonium-derived polypeptide is indicated by reference example number. Comparative Example 1 For comparison, Example 1 except that the quaternary trimethylammonium-derived polypeptide was not used.
In the same manner as above, a first agent for permanent waves having the formulation shown in Table 2 was prepared. Using the first agents for permanent waving of Examples 1 to 9 and Comparative Example 1 prepared as described above, a panel of 10 professional women underwent permanent waving, and each item shown in Table 3 was applied. Stiff
A 10-level evaluation was conducted and the results are shown in Table 3. In the above permanent wave treatment, a 7% aqueous solution of sodium bromate was used as the second agent. In addition, amino acid analysis was performed on the hair that had been subjected to the permanent wave treatment, and cysteic acid produced by the permanent wave treatment was quantified. The amount of cysteic acid produced indicates the degree of damage to the hair, and it is said that the larger the amount produced, the more damaged the hair is. The results (average values) are shown in Table 3.

【table】

[Table] Examples 10 to 12 Using the quaternary trimethylammonium-derived polypeptides obtained in Reference Examples 4 to 6, a first agent for permanent waves having the formulation shown in Table 4 was prepared. Comparative Example 2 The same procedure as in Example 10 was carried out except that the quaternary trimethylammonium-derived polypeptide was not used.
A drug was prepared. Using the first agents for permanent waving of Examples 10 to 12 and Comparative Example 2 prepared as described above, permanent waving was performed on a panel of 10 professional women in the same manner as in Example 1, and a comparative test was conducted. Ta.
The results are shown in Table 5. Additionally, the amount of cysteic acid in hair that had been subjected to permanent wave treatment was measured. The results are shown in Table 5.

【table】

〔Effect of the invention〕

As explained above, the first agent for permanent waving of the present invention can provide excellent waving effects without damaging the hair or scalp.

Claims (1)

[Scope of Claims] 1. At least one reducing agent selected from the group consisting of thioglycolic acid, thioglycolate, cysteine, sulfite, and bisulfite.
Contains weight% and has the general formula () (In the formula, R is a side chain of an amino acid constituting a polypeptide derived from animal protein, and n
0.2 to 20% by weight of a quaternary trimethylammonium-derived polypeptide represented by
A first agent for permanent waves characterized by containing the following: