JPS60243010A - Hair protecting agent - Google Patents

Abstract

PURPOSE:A hair protecting agent, consisting of a specific quaternary trimethylammonium-derived polypeptide, capable of exhibiting improved hair protecting action, and preventing hair damage by cosmetics, e.g. permanent waving agent or shampoo, etc. CONSTITUTION:A hair protecting agent consisting of a compound expressed by formula I (R is side chain of amino acid constituting polypeptide derived from animal proteins; n is 3-20). The above-mentioned compound is obtained by reacting a compound expressed by formula II with a compound expressed by formula III, and has polypeptide part derived from animal proteins, e.g. collagen, keratin or silk protein, and chemical structure similar to that of the hair, and action of adsorbing on the hair by the action of the amino groups, carboxyl groups and further side chains of various amino acids to protect the hair and regenerate damaged hair. The quaternization improves the adsorbability of the agent on the hair greatly to impart flexibility of high order and natural gloss to the hair.

Description

[Detailed description of the invention] 〔Technical field〕 The present invention relates to a novel hair protection agent.

[Background technology]

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.

For example, when a permanent waving agent is used, a part of the keratin protein that makes up the hair is eluted, and the remaining part of the hair is also subjected to physical and chemical changes, causing the hair to feel strange and dry. In addition, since the surfactants contained in shampoos have a strong surfactant ability, even the sebum and constituent proteins of the hair are eluted, damaging the hair and making it feel dry or coarse after drying. Become. The conditioner is used after washing the hair with shampoo to give the hair flexibility and natural shine.The main ingredients used in the conditioner are long-chain alkyl trimethylammonium chloride with 16 to 18 carbon atoms, Dialkyltrimethylammonium chloride, alkyldimethylbenzylammonium chloride, etc. have strong surfactant properties, so if they are used in large quantities, the sebum and constituent proteins of the hair will be eluted, as in the case of shampoo, and the hair will become damaged. It starts to feel dry or rough.

[Purpose of the invention]

In view of the above-mentioned circumstances, it is an object of the present invention 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 provides quaternary This invention relates to a hair protection agent comprising trimethylammonium-derived polypeptide.

The quaternary trimethylammonium-derived polypeptide represented by the above general formula (1) 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. It adsorbs to the hair through the action of its amino groups, carboxyl groups, and side chains of various amino acids, and has the effect of protecting the hair and regenerating damaged hair. It has greatly improved adsorption properties, giving hair a high degree of flexibility and natural shine.

The hair protection agent made of the quaternary trimethylammonium-derived polypeptide represented by the general formula (I) is obtained by dissolving the quaternary trimethylammonium-derived polypeptide in water or a base mainly composed of water, and adding an emulsifier if necessary. , wetting agents, preservatives, fragrances, coloring agents, chelating agents, and various anionic, cationic, and nonionic surfactants may be appropriately added to the composition for 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, hair conditioner, etc.
It may be added to various hair cosmetics such as hair blowouts and permanent wave preparations. The above-mentioned water-based bases include ethyl alcohol, ethylene glycol,
It refers to a product to which alcohols or polyhydric alcohols such as propylene glycol, butylene glycol, glycerin, and polyol are added to the extent that it does not inhibit the dissolution of the quaternary trimethylammonium-derived polypeptide represented by the general formula (1). The amount is 50% by weight or more based on the total weight. When used, the concentration of the quaternary trimethylammonium-derived polypeptide represented by the general formula (1') is preferably about 2 to 20% by weight.

The polypeptide moiety in the general formula (I) is derived from animal proteins such as collagen, keratin, proteins constituting silk (silk protein), elastin, actin, and myosin; 1
), the amino acids whose side chains are represented by R are:
Alanine, glycine, valine, leucine, isoleucine, proline, phenylalanine, tyrosine, serine, threonine, methionine, arginine, histidine, lysine, aspartic acid, asparagine, glutamic acid, glutamine, cystine, cystic acid, tryptophan,
Examples include hydroxyproline and hydroxylysine. Table 1 shows an example of the composition ratio of these amino acids.

The quaternary trimethylammonium-derived polypeptide represented by the general formula (I) can be obtained by reacting 3-chloro-2-hydroxypropyltrimethylammonium chloride with an animal protein-derived polypeptide.

3-chloro-2-hydroxypropyltrimethylammonium chloride (hereinafter referred to as CTA) used in the above reaction
) is known as existing chemical substance (2)-181, and an aqueous solution with a concentration of about 50% (weight %, hereinafter the same) is commercially available and can be easily obtained. On the other hand, animal protein-derived polypeptides are obtained by hydrolyzing animal proteins such as collagen, keratin, silk protein, elastin, actin, and myosin using acid, alkali, or protease. Then, during hydrolysis, by appropriately selecting the amount of acid, alkali, or enzyme added, reaction temperature, and reaction time, the obtained animal protein derivative □ polypeptide n
The value of 3 to 2o, that is, the molecular weight of about 300 to about 2,00
The preferred value can be 0.

The details of the hydrolysis of animal protein to obtain animal protein-derived polypeptide are as follows.

Raw animal proteins include collagen, keratin,
Examples include silk protein, elastin, actin, and myosin. These are all proteins of animal origin, and unlike vegetable proteins, they do not suffer from impurities such as carbohydrates and lipids, and can be obtained in large quantities.

Animal polypeptides derived from these raw materials are
It has the property of adsorbing to hair, and as a safe cosmetic raw material derived from natural products, it can prevent hair damage, restore hair damage,
It is applied to moisturize the skin and prevent denaturation of skin proteins caused by surfactants.

Raw materials such as collagen include animal skin, elbows, bones, etc., and it is convenient to use gelatin, which is an extract of collagen from these materials. Gelatin comes in powder, plate, and granule forms, all of which dissolve easily in hot water.
There are also few impurities.

Examples of raw material keratin include animal hair, hair, feathers,
Examples include nails, horns, hooves, scales, etc., but especially wool, hair,
Feathers are preferred. These keratins can be subjected to hydrolysis as they are, but if necessary, they may be cut or crushed into appropriate sizes, or pretreated such as washing, degreasing, and high-temperature pressure treatment.

Silk protein raw materials include silkworm cocoons,
Examples include silk thread and silk cloth, but since no particular processing is required, it is economically advantageous to use silkworm cocoons or cotton-like or rough brown-like materials before spinning. As with keratin, which is the same fibrous protein, it may be cut or crushed into appropriate sizes, or may be washed or subjected to high-temperature pressure treatment, if necessary. Furthermore, silk protein can be dissolved in a highly concentrated aqueous solution of 40% or more of an alkali metal halide or alkaline earth metal salt such as lithium bromide or calcium chloride. Hydrolysis can also be carried out.

In addition, elastin, a protein that exists in the skin along with collagen and is known to give skin elasticity, and muscle proteins actin and myosin can also be used.

Acid hydrolysis, alkaline hydrolysis, and enzymatic hydrolysis of animal proteins are carried out as follows.

(1) Hydrolysis with acids Examples of acids include inorganic acids such as hydrochloric acid, sulfuric acid, phosphoric acid, nitric acid, and hydrobromic acid, and organic acids such as acetic acid and formic acid. Alternatively, a mixture of hydrochloric acid, acetic acid, etc. may be used. These are generally used at a concentration of 5 to 85%, but it is desirable to ensure that the hydrolysis reaction always takes place at a pH of 4 or less. It is not preferable to use more acid than necessary because the hue of the hydrolyzate solution becomes brown. The reaction temperature is 40-1
00°C is preferred, but it can also be raised to 160°C under pressure. The reaction time is preferably 2 to 24 hours.

The reactant can be neutralized with an alkali such as sodium hydroxide, calcium hydroxide, or sodium carbonate and used as is, but the reactant or neutralized product can be used by gel filtration, ion exchange resin, etc.
It can also be used after being purified by ultrafiltration, dialysis, electrodialysis, etc.

(2) Hydrolysis with alkali Examples of alkali include sodium hydroxide, potassium hydroxide, lithium hydroxide, barium hydroxide, sodium carbonate,
Inorganic alkalis such as potassium carbonate and lithium carbonate are used. A concentration of 1 to 20% is generally suitable for these. If more alkali is used than necessary, the hue of the hydrolyzate solution will become brown to black, which is not preferable. The reaction is preferably carried out at a temperature of room temperature to 100°C for 30 minutes to 24 hours, and care must be taken not to raise the temperature too much or make the reaction time longer than necessary. After the reaction, it is preferable to neutralize with the above-mentioned acid or purify by gel filtration, ion exchange resin, ultrafiltration, dialysis, electrodialysis, etc.

(3) As the enzymatic hydrolysis enzyme, acidic proteolytic enzymes such as pepsin, proctase A1 and protase B, and neutral proteolytic enzymes such as papain, promelain, thermolysin, trypsin, pronase, and chymotrypsin are used. In addition, occlusive proteolytic enzymes such as subtilin and staphylococcal protease can also be used. The pH during hydrolysis is adjusted to a pH range of 1 to 4 in the case of acidic proteolytic enzymes such as pepsin, and a range of pH 4 to 10 in the case of neutral proteolytic enzymes such as papain. The pH is generally preferably adjusted appropriately with a buffer such as an acetic acid/sodium acetate buffer, a phosphate buffer, or by the addition of a certain acid, alkali, or the like. The reaction temperature is preferably 30 to 45°C, and the reaction time is generally 3 to 24 hours.

In hydrolysis reactions using enzymes, the molecular weight of the hydrolyzate is greatly influenced by the amount of enzyme used, reaction temperature, and reaction time. Therefore, in order to obtain an animal protein hydrolyzate with the desired molecular weight, the molecular weight distribution of the obtained hydrolyzate must be determined by gel filtration under each condition of the amount of enzyme used, reaction temperature, and reaction time. It is necessary to investigate thoroughly and determine the optimal conditions empirically.

Enzyme-based hydrolysates have a narrower molecular weight distribution and less free amino acids are produced than acid- or alkali-based hydrolysates, so they are very suitable for use in cosmetic formulations.

The average molecular weight of the hydrolyzate obtained by these hydrolysis reactions is preferably 300 or more and 2,000 or less. This is because the adsorption ability of animal protein hydrolyzate to hair is determined by its molecular weight, and the molecular weight is 300 to 60.
This is because those with a molecular weight of about 0 are the easiest to adsorb, are easily soluble in water, and are easy to handle, while those with a molecular weight of more than 2,000 have little adsorption to hair and are difficult to handle.

In the present invention, n is 3 to 2 in the quaternary trimethylammonium-derived polypeptide represented by general formula (I).
The reason for setting 0 is that when n is less than 3, adsorption to hair is insufficient, and when n exceeds 20, adsorption to hair becomes weak.
This is because handling becomes difficult due to gelation and the like.

The reaction between animal protein-derived polypeptide and CTA is carried out by adding CT' to an aqueous solution of animal protein-derived polypeptide.
This is carried out by dropping an aqueous solution of A to bring the animal protein-derived polypeptide and CTA into contact with each other in water.

During the reaction, the pH in the reaction system should be adjusted to 8 to 12, especially 9 to 12.
It is desirable to maintain the temperature at a temperature of 11, and therefore an aqueous alkaline solution such as sodium hydroxide or potassium hydroxide is added dropwise into the reaction solution as necessary. During the reaction, the pH within the reaction system is maintained within the above range; in order for the amino groups of the animal protein-derived polypeptide to react with CTA, it is desirable that the pH be on the alkaline side, at pH 8 or above; This is because if the amount exceeds CTA and animal protein-derived polypeptides, hydrolysis will occur. The reaction proceeds even at room temperature, but the higher the temperature, the faster the reaction. However, when the pH is high and the temperature increases, the hydrolysis of animal protein-derived polypeptides and CTA is promoted, and only products with low molecular weight can be obtained. During the reaction, animal protein-derived polypeptides become viscous and difficult to react uniformly when the concentration is high, so it is preferable to use an aqueous solution with a concentration of about 30 to 50%.CTA uses a commercially available aqueous solution with a concentration of 50%. You can use it as is.

Dripping CTA onto animal protein-derived polypeptide is 3
It is preferable to complete the process in 0 minutes to 6 hours. When CTA is added dropwise, the reaction shown in the formula below proceeds, hydrogen chloride is generated and the pH of the reaction solution is lowered. Therefore, alkali is added dropwise at the same time as CTA is added and stirred to reduce the pH in the solution.
It is preferable to keep H dropwise into the reaction at p) 1, so that it is preferred to allow the dropwise addition to take at least 30 minutes. After dropping CTA, continue stirring for about 2 to 6 hours,
It is preferable to keep 9 to 1 liters of PL (1°) and then leave it for a day and night or heat it to about 60°C to complete the reaction. It is confirmed by measuring the amino nitrogen in polypeptide using the VanSlyke) method.

[Example] Next, the present invention will be described in further detail by reference examples (manufacturing example of animal protein-derived polypeptide and manufacturing example of quaternary trimethylammonium-derived polypeptide) and examples.

Reference Example 1 Production of Collagen-Induced Polypepquid 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 add water with stirring for 1 hour. After decomposition, the reaction mixture was filtered, the filtrate was diluted to 2e with water, and a weakly basic anion exchange resin Diaion WA20 (trade name, Mitsubishi Chemical Industries, Ltd.) was added.
The solution was passed through a 290 ml resin tower for neutralization. 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) 500 g of plate gelatin was dissolved while heating 700 g of a 6% aqueous sodium hydroxide solution, hydrolysis was performed for 1 hour while stirring at 80"C, and the reaction mixture was filtered. death,
The filtrate was diluted with water to 21 V and neutralized by passing it through a 500 ml resin column containing weakly acidic cation exchange resin Amberlite IRC-50 (trade name, 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 a gel filtration method and found to be an average molecular weight of 500.

Reference Example 1-3 (enzymatic degradation) Add 650 g of water to 350 g of granular gelatin,
After heating to ℃ to dissolve gelatin, 1 g of neutral proteolytic enzyme papain 20II was added and hydrolysis was carried out for 3 hours with stirring at 50 ℃.The reaction mixture was filtered to obtain collagen-derived polypeptide with a concentration of 35%. An aqueous solution of was obtained. 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 2 of manufacturing keratin-derived polypeptide
-1 (Acid hydrolysis) 35% salt 1145 to 500 g of wool in a three-solo flask
0 g was added and hydrolysis was carried out at 80°C for 16 hours with stirring. After hydrolysis, the reaction mixture is filtered and the filtrate is treated with a weakly basic anion exchange resin Diaion WA20 (described above) 1.
After neutralizing with 400 ml, the solution was concentrated and filtered to remove the ion exchange resin 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 800.

Reference example 2-2 (alkaline hydrolysis) 500 g of pig hair, 100 g of sodium hydroxide and 3 kg of water
was added and allowed to stand at 40°C for 24 hours to perform hydrolysis, then the reaction mixture was filtered, and the filtrate was neutralized with 600 mβ of a weakly acidic cation exchange resin Amberlite IRC-50 (described above). 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 1.200.

Reference Example 2-3 (Enzyme Hydrolysis) 500g of feathers was placed in a high pressure container at a rate of 10kg/ai! , 200
After being treated with superheated steam at ℃ for 30 minutes, it was discharged 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 performed at 40° C. for 24 hours. After hydrolysis, the reaction mixture was filtered and 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 be an average molecular weight of 600.

Reference Example 3 Production Reference Example 3 of silk-covered white matter-induced polypeptide
-1 (Alkaline hydrolysis) Pour 1.51 g of 2N sodium hydroxide into a 2x beaker, and add a portion of 500 g of dried silkworm cocoons (washed in advance to remove silkworm feces and dirt). 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 further added. After adding the whole cocoon for 30 minutes, keep at 80℃ for another 1 hour.
The mixture was heated and stirred to complete the hydrolysis. The reaction product was diluted by adding 1β of water, and then filtered under reduced pressure.

The filtrate was treated with a weakly acidic cation exchange resin Amberlite IRC-
50 (mentioned above) After neutralizing by passing the liquid through a 1,300 ml resin tower, it was concentrated under reduced pressure and filtered to a concentration of 3.
A 0% aqueous solution of silken white matter-derived polypeptide was obtained. The molecular weight of the thus obtained silky white matter-derived polypeptide was measured by gel filtration, and the average molecular weight was 50.
It was 0.

Reference Example 3-2 (Acid Hydrolysis) 5.0 kg of commercially available 55% lithium bromide aqueous solution
After adding and dissolving 200 g of unspun silk fiber at 0°C, this solution was diluted with ion-exchanged water to a total of 2.0 kg. This liquid was heated to 80'C in a 2β three-dimensional solo flask and stirred, and 25 g of concentrated hydrochloric acid was added thereto for 2 hours of hydrolysis. After cooling, 48 g of 20% aqueous sodium hydroxide solution was added to neutralize the mixture, and then filtered 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 total protein-induced polypeptide thus obtained was measured by gel filtration and found to have an average molecular weight of 1,800.

Reference Example 3-3 (Enzyme Hydrolysis) 300 g of washed silkworm cocoon was placed in a high-pressure container at 10 kg.
g/oa, 27! Put it in a beaker and add 0. IN sodium acetate buffer (pH 6) lj! was added, the temperature was adjusted to 40"C, and 20 mg of the neutral proteolytic enzyme papain was added.
Hydrolysis was carried out at 0°C for 12 hours. After filtering the reaction mixture to remove undecomposed residue, the filtrate was concentrated under reduced pressure to a concentration of 30
An aqueous solution of % total protein-derived polypeptide was obtained. The molecular weight of the total protein-induced polypeptide thus obtained was measured by gel filtration, and the average molecular weight was 1.
It was 050.

Reference Example 4 Production of quaternary trimethylammonium-derived collagen polypeptide A total of 310 mmol of nitrogen) was placed in a reaction vessel, and while stirring at 35°C, 103 g of CT'A aqueous solution with a concentration of 51% (equivalent to 0.8 g of amino nitrogen in collagen-derived polypeptide) was added.
was added dropwise over 30 minutes, and during that time a 20oA sodium hydroxide aqueous solution was added dropwise to adjust the pH of the reaction solution to 10.0.
maintained. After the completion of dropping CTA, stirring was continued for 2 hours while maintaining the pH at 10.0, and then after being left for 24 hours, amino nitrogen was measured, and the total amount of amino nitrogen was 42 mmol. 84 of nitrogen
% were responding. Next, a weakly acidic cation exchange resin Amberlite IRC-50 (mentioned above) 170+nj was added to the reaction solution.
! was added to neutralize the pH to 6.5, the sodium ions in the reaction solution and the slightly remaining CTA of the East reaction were adsorbed onto the ion exchange resin, and then the ion exchange resin was removed to give a solution with a concentration of 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 tetraphenylboron, and a red precipitate was produced by Dragendorff's reagent, indicating a positive result.

Furthermore, in order to confirm that the collagen-derived polypeptide and CTA were bound together, the resulting aqueous solution was subjected to gel filtration (G-25, manufactured by Pharmacia), and each molecular weight fraction had the above-mentioned properties. When the reaction was carried out, each fraction was positive for the quaternary ammonium salt reaction, and it was confirmed that the collagen-derived 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 molecule of collagen-derived polypeptide N500, total amount of amino thiosine 697
millimoles) into a reaction vessel, and while stirring, reduce the concentration to 49 mmol.
% CTA aqueous solution (0°85 equivalent of amino nitrogen of collagen-derived polypeptide) was added dropwise over 30 minutes, and during this period, a 20% sodium hydroxide aqueous solution was added dropwise to adjust the pH of the reaction solution to 9. It was kept at 5.

After the completion of dropping CTA, stirring was continued for 5 hours while maintaining the pH at 9.5, and then after being left for 24 hours, amino nitrogen was measured, and the total amount of amino nitrogen was 14
7 mmol, and 79% of the amino nitrogen had reacted. Next, the reaction solution was mixed with a strongly acidic cation exchange resin Diaion 5K-IB (trade name, Mitsubishi Chemical Industries, Ltd.) 3
20 mj! The solution is passed through a resin tower, neutralized to pH 6.9, the sodium ions in the reaction solution and the slightly remaining unreacted CTA are adsorbed onto the ion exchange resin, and then the ion exchange resin is removed to adjust the concentration. A 30% aqueous solution of quaternary trimethylammonium-derived collagen polypeptide was obtained.

The resulting aqueous solution was subjected to a quaternary ammonium salt impact 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 each molecular weight fraction was subjected to a quaternary ammonium salt impact reaction. It was confirmed that they are connected.

Reference Example 4-3 800 g of the collagen-derived polypeptide aqueous solution with a concentration of 35% obtained in Reference Example 1-3 (average molecular weight of collagen-derived polypeptide 1,700, total amount of amino nitrogen 140 mmol) was placed in a reaction container, While stirring at 30°C, 63.1 g of CTA aqueous solution with a concentration of 49% (1.0 g of amino nitrogen of collagen-derived polypeptide) was added.
equivalent amount) was added dropwise over a period of 1 hour, and during that time, a 20% aqueous sodium hydroxide solution was appropriately added dropwise to adjust the pH of the reaction solution to 11.
．． It was maintained at 0. After dropping CTA, adjust the pH to 11.0.
Stirring was continued for 3 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 14 mmol, and 90% of the amino nitrogen had reacted. . Next, add 120 m of weakly acidic cation exchange resin Amberlite IRC-50 (mentioned above) to the reaction solution.
Add A to adsorb the sodium ions in the reaction solution and the slight remaining unreacted CTA 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 resulting aqueous solution was subjected to impact reaction with quaternary ammonium salt 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 each molecular weight fraction was subjected to a quaternary ammonium salt impact reaction. It was confirmed that they are connected.

Reference Example 5 Production of quaternary trimethylammonium-derived keratin polypeptide Total amount of elements 43
0 mmol) into a reaction vessel, and while stirring, reduce the concentration to 49.
% CTA aqueous solution (0.g equivalent of amino nitrogen of keratin-derived polypeptide) was added dropwise over 30 minutes, and during that time, a 20% aqueous sodium hydroxide solution was appropriately added dropwise to adjust the pH of the reaction solution to 10.0. maintained. CT
After the addition of A was completed, stirring was continued for 2 hours while maintaining the pH at 10, O, and then after being left for 24 hours, amino nitrogen was measured. 88% of the nitrogen was reacted. Next, add a weakly acidic cation exchange resin Amberlite ■RC-50 (mentioned above) to the reaction solution at 220 mj! Add
Neutralize to pH 6.5, adsorb sodium ions in the reaction solution and a small amount of unreacted CTA to an ion exchange resin, then remove the ion exchange resin to a concentration of 30.
% of quaternary trimethylammonium-derived keratin polypeptide was obtained.

The resulting aqueous solution was subjected to impaction reaction with quaternary ammonium salt 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 each molecular weight fraction was subjected to a quaternary ammonium salt impact reaction. It was confirmed that they are connected.

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 1,200, total amount of amino-tinogen 272 mmol) was placed in a reaction container, While stirring,
88 g of 8 liquids of CTA water/aqueous solution with a concentration of 49% (0.85 equivalent of amino thiiso of keratin-derived polypeptide) was added dropwise over a period of 30 minutes, and a 20% aqueous sodium hydroxide solution was appropriately added dropwise during the reaction. The pH of the solution was maintained at 10.5. 'After the completion of dropping CT A, stirring was continued for 2 hours while maintaining the pH at 10.5, and then after being left for 24 hours, amino nitrogen was measured, and the total amount of amino thiosine was 61 mmol. , amino nitrogen 7
8% responded. Next, 200 m of strongly acidic cation exchange resin Diamond 5K-IB (mentioned above) was added to the reaction solution.
12 was added to neutralize the pH to 6.9, the sodium ions in the reaction solution and the slightly remaining unreacted CTA were adsorbed onto the ion exchange resin, and then the ion exchange resin was removed and a 30% concentration solution was added. An aqueous solution of quaternary trimethylammonium-derived keratin polypeptide was obtained.

When the resulting aqueous solution was subjected to impact reaction with quaternary ammonium salt 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 each molecular weight fraction was subjected to a quaternary ammonium salt impact reaction. It was confirmed that they are connected.

Reference Example 5-3 700 g of the keratin-derived polypeptide aqueous solution with a concentration of 40% obtained in Reference Example 2-3 (average molecular weight of keratin-derived polypeptide 600, total amount of amino-thiisomine 43
1 mmol) into a reaction vessel, and while stirring, adjust the concentration to 4.
165 g of 9% CTA aqueous solution (1.0 equivalent of amino nitrogen of keratin-derived polypeptide) was added dropwise over 1 hour, during which time 20% hydroxide was added. The pH was maintained at 11.0. After the completion of dropping CTA, stirring was continued for 2 hours while maintaining the pH at 11.0, and then after being left for 24 hours, the amino nitrogen was measured, and the total amount of amino nitrogen was 40 mmol. 93% of the nitrogen was reacted. Next, 100 m Il 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 slightly remaining unreacted CTA were adsorbed onto the ion exchange resin. The ion exchange resin was then removed to obtain an aqueous solution of quaternary trimethylammonium-derived keratin polypeptide with a concentration of 30%.

When the resulting aqueous solution was subjected to impact reaction with quaternary ammonium salt 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 each molecular weight fraction was subjected to a quaternary ammonium salt impact reaction. It was confirmed that they are connected.

Reference Example 6 Production of quaternary trimethylammonium-derived silk polypeptide 500, total amount of amino thiosine 7
30 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% (total amount equivalent to 00 g of amino nitrogen of white matter-derived polypeptide) was added.
was added dropwise over a period of 30 minutes, and during this time, a 20% aqueous sodium hydroxide solution was appropriately added dropwise to maintain the pH of the reaction solution at 10.0. After the completion of dropping CTA, stirring was continued for 2 hours while maintaining the pH at 10.0, and then after being left for 24 hours, amino nitrogen was measured, and the total amount of amino nitrogen was 81 mmol. 89% of nitrogen
was reacting. Next, add 100 m of weakly acidic cation exchange resin Amberlite IRC-50 (mentioned above) to the reaction solution.
+2 was added to neutralize the pH to 6 or 7, and the sodium ions in the reaction solution and the slightly remaining unreacted CTA were adsorbed onto the ion exchange resin.Then, the ion exchange resin was removed and a 30% concentration An aqueous solution of quaternary trimethylammonium-derived silk polypeptide was obtained.

When the resulting aqueous solution was subjected to impact reaction with quaternary ammonium salt 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 each molecular weight fraction was subjected to a quaternary ammonium salt impact reaction. As a result, each fraction was positive, indicating that it was a silk protein-derived polypeptide. It was confirmed that it was bound to CTA.

Reference Example 6-2 500 g of the white matter-derived polypeptide aqueous solution with a total concentration of 35% obtained in Reference Example 3-2 (average molecular weight of the total white matter-derived polypeptide: 1,800, total amount of amino nitrogen 95 mmol) was placed in a reaction vessel. Add 30.4 g of CTA aqueous solution with a concentration of 49% (total amount: 0.85 equivalents of amino nitrogen of white matter-derived polypeptide) to 1 ml while stirring.
The reaction solution was added dropwise over a period of time, and a 20% aqueous sodium hydroxide solution was appropriately added dropwise during this period to maintain the pH of the reaction solution at 4-10.0. After the dropwise addition of CTA was completed, stirring was continued for 2 hours while maintaining I)H at 10°O, and then after being left for 24 hours, the amino nitrogen was measured, and the total amount of amino nitrogen was 17 mmol. , 82% of amino nitrogen
was reacting. Next, a strongly acidic cation exchange resin Diaion 5K-IB (mentioned above) 80mi was added to the reaction solution.
Neutralize to pH 6.9, adsorb sodium ions in the reaction solution and a small amount of unreacted CTA to an ion exchange resin, then remove the ion exchange resin to a concentration of 30.
% of quaternary trimethylammonium-derived silk polypeptide was obtained.

The resulting aqueous solution was subjected to a quaternary ammonium salt 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 characteristic reaction was performed on each molecular weight fraction. It was confirmed that it was bound to CTA.

Reference Example 6-3 The total amount of white matter-inducing polypeptide aqueous solution with a concentration of 30% obtained in Reference Example 3-3 was 800. g (average molecular weight of white matter-derived polypeptides: 1,050, total amount of amino-type chinogens: 226 mmol) was placed in a reaction vessel, and while stirring, 87.7 g of CTA aqueous solution with a concentration of 49% (total amount of white matter-derived polypeptides of amino-tinols) was added to a reaction vessel. (1.0 equivalents of chlorine) 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 the completion of dropping CTA, stirring was continued for 2 hours while maintaining the pH at 11.0, and then after being left for 24 hours, the amino nitrogen was measured, and the total amount of amino nitrogen was 18 mmol. 92% of the nitrogen was reacted. Next, add 150 mI of the weakly acidic cation exchange resin Amberlite IRC-50 (mentioned above) to the reaction solution. The sodium ions in the reaction solution and the slightly remaining unreacted CTA are adsorbed onto the ion exchange resin, and then the ion exchange resin is removed to form a quaternary trimethylammonium-derived silk polyester with a dry residue of 30%. An aqueous solution of butide was obtained.

The resulting aqueous solution was subjected to a quaternary ammonium salt 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 characteristic reaction was performed on each molecular weight fraction. It was confirmed that it was bound to CTA.

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. The composition of Control Product 1, which does not contain quaternary trimethylammonium-derived polypeptide, is also shown in Table 2.

Add 1 hair strand weighing 1g to 30g of hair protectant of each composition above.
After immersion for 0 minutes and rinsing, the hair bundle was immersed in 70 g of a separately prepared first agent for permanent waves for 20 minutes, rinsed, and then immersed in 100 g of a second agent for permanent waves for 15 minutes. The gloss, suppleness, and combability of the hair after treatment were sensory evaluated. Furthermore, the amount of cystic acid in the hair after treatment is shown in Table 3. Cystic acid in hair is produced from cystine in hair during permanent waving, and the amount of cystic 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 Also, an automatic amino acid analyzer was used to measure the amount of cystic acid. The formulation composition of the first agent for permanent waving and the formulation composition of the second agent for permanent waving used are as shown in Table 4.

Table 4 Examples 10 to 1B Hair protection agents having the formulations shown in Table 5 were prepared, and their effects were confirmed as shown below. Mix 20 g of the hair protectant of each composition above and 80 g of a separately prepared bleaching solution,
A hair bundle weighing 1 g was immersed in the solution for 30 minutes, rinsed, and further dried to remove color. The gloss, suppleness, and combability of the hair after treatment were sensory evaluated. Furthermore, Table 6 shows the results of measuring the amount of cysteine in the hair after treatment. Cystic acid in hair is produced from cystine in hair through oxidation due to bleaching, and the amount of cystic 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, cystic acid was also measured in the same manner as in Example 1.

Five negative claw set bottom 35% hydrogen peroxide solution 20.0 25% ammonia solution 7.0 Polyoxyethylene 1.0 Cetyl ether EDTA 0.1 Purified ice 71.9 Next, Table 5 of Examples 10-18 70 parts of a separately prepared hair dye were mixed with 30 parts of a hair protectant having the composition shown in Figure 1, and the hair was dyed using a panel of 10 professional women.

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. Cystic acid was also determined in the same manner as in Example 1, 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, a rheometer (manufactured by Mitsuwa Rikagaku Kogyo Co., Ltd.) was used to fix each 2 cm long hair, and pull the hair at a pulling speed of 2 cm/min until the hair was 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 of each hair.

Togeki Sotrium lauryl sulfate (30% aqueous solution) 25.0 Polyoxyethylene stearate (5) 8.0 Sorbitan ester (30%) Citin 1.5 25% aqueous ammonia 8.0 1.3- Butylene glycol 3.0 Isopropatol 2.5 Paraphenylenediamine 0.7 Paraaminophenol 0.15 4-Nitro-1,2-diaminobenzene 0.3 Pyrogallol 0.7 Resorcinol 0.2 Hydroquinone 0.1 Purified water 49.85 [Effects 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) Quaternary trimethylammonium-derived polypeptide represented by general formula (1) (wherein R is a side chain of an amino acid constituting a polypeptide derived from animal protein, and n is 3 to 20) More hair protectants.