JP2010285401A - Hair care agent and method for treating hair - Google Patents

Abstract

<P>PROBLEM TO BE SOLVED: To provide a hair care agent suitable for the improvement of the initial elastic modulus of the hair. <P>SOLUTION: The hair care agent comprises a peptide and the peptide has a group represented by formula (I): -S-S-(CH<SB>2</SB>)<SB>n</SB>COO- (wherein n is 1 or 2) as a side chain. The side chain is preferably at least one kind selected from a carboxymethyl disulfide group, a salt of the carboxymethyl disulfide group, a carboxyethyl disulfide group, and a salt of the carboxyethyl disulfide group. The hair care agent may be shampoo, rinse, a treatment agent or a conditioner. Further, the peptide preferably has hair permeability. <P>COPYRIGHT: (C)2011,JPO&INPIT

Description

  The present invention relates to a hair care agent used in shampoos, conditioners and the like, and a hair treatment method using the hair care agent.

  Physical treatments such as brushing, hand dryers, hot irons, and chemical treatments such as hair coloring and permanent wave damage the hair. Damaged hair has worse hair properties, such as hair feel (for example, beam, strain, softness), appearance (for example, gloss, cohesion), strength (for example, tensile strength) compared to before being damaged. Will be. In order to improve deteriorated hair properties, it is known to incorporate a peptide derived from a natural product and / or a modified peptide into which a cationic group, a silyl group, an acyl group, or an ester group is introduced into a hair care agent. .

Patent Document 1 discloses one type of modified peptide, which is obtained by converting a protein disulfide group (—S—S—) into a carboxymethyl disulfide group (—S—S—CH ₂ COOH). The obtained water-soluble one. Patent Document 1 discloses forming a film from a modified peptide as a specific application mode of the modified peptide.

  As described above, it is known that a modified peptide is blended in a hair care agent, and various modified peptides are being searched for in order to develop a hair care agent suitable for improving hair characteristics.

JP-A-7-126296

  The present invention has been made in view of the circumstances where improvement in properties of damaged hair is required, and a hair care agent suitable for improving the initial elastic modulus, which is one factor affecting hair tension, and hair using the hair care agent. The purpose is to provide a processing method.

  As a result of intensive studies, the present inventor has found that the initial elastic modulus of hair can be improved by blending a peptide having a predetermined side chain group into a hair care agent and treating the damaged hair with this hair care agent, The present invention has been completed.

That is, the hair care agent according to the present invention is a hair care agent containing a peptide, wherein the peptide includes a group having a group represented by the following formula (I) as a side chain group. .
_{-S-S- (CH 2) n} COO- (I)
(In the formula (I), n is 1 or 2.)

  The hair care agent contains a peptide having a side chain group having the group of the above formula (I), thereby improving the initial elastic modulus as one factor that affects the elasticity of the hair, hair color, permanent wave It is possible to improve the properties of damaged hair. The “peptide” here is a general term for compounds formed by binding two or more amino acids by peptide bonds, and is a concept including protein.

  The side chain group of the peptide blended in the hair care agent has one or more selected from carboxymethyl disulfide group, carboxymethyl disulfide group salt, carboxyethyl disulfide group, and carboxyethyl disulfide group salt. It is preferable. The initial elastic modulus of the hair can be effectively improved by the hair care agent in which the peptide having these side chain groups is blended. The cation constituting the “salt” here is not particularly limited as long as it is a cation that can be substituted with a hydrogen ion of a carboxy group and does not inhibit the above effect.

  The hair care agent can be used as a shampoo, rinse, treatment, or conditioner.

  It is preferable that the molecular weight of the peptide mix | blended with the said hair care agent is 22000 or less. By using such a low molecular weight peptide, it is possible to effectively recover the damage even for hair that has been greatly damaged.

  The dosage form at the time of use of the hair care agent may be liquid, emulsion, cream, ointment, gel, solid, foam, or mist. Depending on the user's preference and purpose, it is possible to use hair care agents in these dosage forms.

  The hair treatment method according to the present invention is characterized by using the above hair care agent.

  If the hair is treated with a hair care agent containing the predetermined peptide according to the present invention, the initial elastic modulus of the hair damaged by hair color, permanent wave or the like can be improved.

The present invention will be described below based on embodiments.
The hair care agent according to the present embodiment is a blend of a peptide having a group having a group represented by the above formula (I) as a side chain group (hereinafter, the peptide is referred to as “CAD peptide”). is there. When the group represented by the formula (I) is dissociated (ionized) to become a carboxylate anion, it is called a carboxylatoalkyl disulfide group.

(CAD peptide)
The CAD peptide has a main chain formed by peptide bonds of a plurality of amino acids and a side chain group bonded to the main chain.

  The main chain of the CAD peptide is not particularly limited. Examples of this main chain include the same main chain of peptides having cysteine as one of the constituent amino acids. Examples of peptides having cysteine as one of the constituent amino acids include keratin and casein. Keratin is known as having a high cysteine ratio among peptides derived from natural products, and is a raw material from which a CAD peptide can be efficiently obtained. Therefore, the main chain of the CAD peptide is preferably the same as the main chain of keratin.

The side chain group of the CAD peptide is a group having a group represented by the following formula (I). In this side chain group, the disulfide group is arranged on the main chain side of the CAD peptide. It is preferable that a plurality of side chain groups exist in the CAD peptide.
_{-S-S- (CH 2) n} COO- (I)
(In the formula (I), n is 1 or 2.)

Suitable as the chemical structure of the side chain group is a carboxymethyl disulfide group represented by the following formula (IA), a salt of the carboxymethyl disulfide group represented by the following formula (IB) or (IC), the following formula It is 1 type, or 2 or more types selected from the salt of the carboxyethyl disulfide group represented by (IIA), and the carboxyethyl disulfide group represented by the following formula (IIB) or (IIC). By using a hair care agent containing a peptide having a side chain group having such a chemical structure, the initial elastic modulus of hair can be improved.
_{-S-S-CH 2 COOH (} IA)
^{_{-S-S-CH 2 COOR 1}} (IB)
(R ¹ represents ammonium such as NH _4. )
^{_{-S-S-CH 2 COOM 1}} (IC)
(M ¹ represents a metal atom such as Na or K.)
_{-S-S-CH 2 CH 2} COOH (IIA)
^{_{-S-S-CH 2 CH 2}} COOR 2 (IIB)
(R ² represents ammonium such as NH _4. )
^{_{-S-S-CH 2 CH 2}} COOM 2 (IIC)
(M ² represents a metal atom such as Na or K.)

A preferable group as the side chain group is one or more selected from the following formulas (Ia), (Ib), (Ic), (IIa), (IIb), and (IIc) (in the following formula R ¹ , M ¹ , R ² and M ² are the same as above.)
—CH ₂ —S—S—CH ₂ COOH (Ia)
—CH ₂ —SS—CH ₂ COOR ¹ (Ib)
—CH ₂ —S—S—CH ₂ COOM ¹ (Ic)
—CH ₂ —S—S—CH ₂ CH ₂ COOH (IIa)
—CH ₂ —SS—CH ₂ CH ₂ COOR ² (IIb)
_{-CH 2 -S-S-CH 2} CH 2 COOM 2 (IIc)

  If the hair is treated with a hair care agent containing a CAD peptide, the CAD peptide crosslinks thiol groups constituting the hair, and as a result, the initial elastic modulus of the hair is considered to be improved. This improvement is caused by the presence of thiol groups in the hair, and since the thiol groups in damaged hair are increasing, hair care agents formulated with CAD peptides are used for chemical treatment and physical treatment on the hair. Suitable for treatment of hair damaged by treatment.

The cross-linking mechanism between thiol groups in hair is represented as follows using a CAD peptide having _two —CH ₂ —SS—CH ₂ COOH as side chain groups as an example.

Further, the cross-linking mechanism between thiol groups in the hair, if indicated the CAD peptide having two _{-CH 2 -S-S-CH 2} CH 2 COOH as side groups in the examples are as follows.

  Although the molecular weight of CAD peptide is not specifically limited, It is good in it being 63000 or less (63 kDa or less). Confirmation that the molecular weight of the CAD peptide is 63000 or less is confirmed by a sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) method using “Protein Molecular Weight Marker (Low)” manufactured by Takara Bio Inc. as a reference substance. be able to.

  The CAD peptide preferably has hair permeability. The molecular weight of the CAD peptide having hair permeability is, for example, 10,000 or less. This CAD peptide having hair permeability is considered to be able to crosslink thiol groups in the hair, so that the above-mentioned improvement effect is expected to the inside of the hair, and the characteristics of damaged hair can be improved. Here, “hair permeability” means the property that the peptide penetrates into portions other than the surface of the hair when the hair is treated with the hair care agent.

  Although the minimum of the CAD peptide compounding quantity to a hair care agent is not specifically limited, 0.05 mass% is good and 0.1 mass% is preferable. The upper limit of the amount of the CAD peptide is not particularly limited, but is preferably 15% by mass, preferably 10% by mass, more preferably 5% by mass, from the viewpoint of suppressing an increase in cost due to a large amount of formulation. Is more preferable.

(Method for producing CAD peptide)
As a method for manufacturing CAD peptide, the manufacturing method (A)-(C) demonstrated below is mentioned, for example.

[Production Method (A)]
The production method (A) comprises a reduction step of converting a protein disulfide group into a thiol group; and a thiol group generated in a protein molecule in the reduction step, a thiol group of mercaptoalkylcarboxylic acid, and / or a mercaptoalkylcarboxylate. A modification step of forming a group represented by the above formula (I) with a thiol group is provided. This production method (A) is suitable for production of a high molecular weight water-soluble CAD peptide having a molecular weight of 40,000 to 63,000 (40 kDa to 63 kDa) (hereinafter, the “high molecular weight water-soluble CAD peptide” is referred to as “CAD”). Sometimes referred to as "Peptide A").

  In the reduction step, the disulfide group (—S—S—) of the protein is reduced to two thiol groups (—SH HS—) by mixing the production raw material containing protein, water, and a reducing agent.

  Examples of the raw material for production include wool (merino wool, lincoln wool, etc.), human hair, animal hair, feathers, nails and the like containing keratin as a constituent protein. Among them, it is preferable to use wool as a raw material in order to obtain it inexpensively and stably. About a manufacturing raw material, it is good to process beforehand combining sterilization, degreasing, washing | cleaning, cutting | disconnection, grinding | pulverization, and drying suitably.

  Although the quantity of water is not specifically limited, For example, it is good in it being 20 to 200 mass parts with respect to 1 mass part of manufacturing raw materials. By setting the amount of water in the above range, the reduction reaction is favorably performed.

  A reducing agent has the effect | action which converts the disulfide group of protein into a thiol group. As the reducing agent, mercaptoalkylcarboxylic acid and / or a salt thereof is used. In addition to the mercaptoalkylcarboxylic acid and / or salt thereof, any other compound may be used as the reducing agent. Examples of such an optional reducing agent include thiolactic acid and / or a salt thereof, dithiothreitol, 2-mercaptoethanol, glutathione, thiourea and the like. These optional reducing agents can be used alone or in combination of two or more.

  The mercaptoalkylcarboxylic acid and / or salt thereof also serves as a modifier that forms the group represented by the above formula (I) in the modification step. As the mercaptoalkylcarboxylic acid and / or salt thereof, one or more selected from the group consisting of thioglycolic acid, thioglycolate, 3-mercaptopropionic acid, and 3-mercaptopropionic acid are used. The Examples of the thioglycolate include sodium thioglycolate, potassium thioglycolate, lithium thioglycolate, and ammonium thioglycolate. Of these, sodium thioglycolate and potassium thioglycolate are preferable, and sodium thioglycolate is more preferable from the viewpoint of efficiently forming a carboxylatomethyl disulfide group. Examples of 3-mercaptopropionate include sodium 3-mercaptopropionate, potassium 3-mercaptopropionate, lithium 3-mercaptopropionate, and ammonium 3-mercaptopropionate. Of these, sodium 3-mercaptopropionate and potassium 3-mercaptopropionate are preferable, and sodium 3-mercaptopropionate is more preferable from the viewpoint of efficiently forming a carboxylatoethyl disulfide group.

  The amount of the mercaptoalkylcarboxylic acid and its salt used is preferably 0.0050 mol or more and 0.02 mol or less, particularly preferably 0.0075 mol or more and 0.01 mol or less, based on 1 g of the production raw material. Further, the amount used is preferably 0.10 mol / L or more and 0.40 mol / L or less, particularly 0.15 mol / L or more and 0.25 mol / L or less, based on the total capacity of the production raw material, water and the reducing agent. preferable. By making the usage-amount of this mercaptoalkylcarboxylic acid and its salt into the said range, progress of a protein reduction reaction becomes favorable.

  In the reduction step, it is preferable to mix one or more alkaline compounds. An alkaline compound is a compound that can be made alkaline by adding it to water. Examples of the alkaline compound include lithium hydroxide, sodium hydroxide, potassium hydroxide, barium hydroxide, sodium carbonate, potassium carbonate, ammonia and the like, and other basic compounds such as monoethanolamine, diethanolamine, arginine, and lysine. Amino acids, sodium bicarbonate, ammonium bicarbonate and the like are also included. Among these, sodium hydroxide and potassium hydroxide are preferable from the viewpoint of efficiently performing protein reduction, and sodium hydroxide is particularly preferable.

  The mixing amount of the alkaline compound is not particularly limited, but it may be blended so that the pH of the reduction reaction system is adjusted to the following range. As the lower limit of the pH, 9 is preferable and 10 is particularly preferable. On the other hand, as an upper limit of pH, 13 is good, 12 is preferable, and 11 is particularly preferable. By adjusting the pH to be equal to or higher than the above lower limit, protein can be reduced efficiently. On the other hand, the main chain cleavage of the protein molecule can be suppressed by adjusting the pH to be not more than the above upper limit.

  As a temperature minimum of the reaction system in a reduction process, 20 ° C is preferred, 30 ° C is more preferred, and 40 ° C is still more preferred. On the other hand, the upper temperature limit is preferably 60 ° C. When the temperature is lower than the lower limit, the reduction time for converting the disulfide group of the protein into a thiol group becomes long, and there is a possibility that sufficient reduction cannot be performed. On the other hand, when the temperature upper limit is exceeded, the main chain of the protein molecule may be cleaved. The set time of the reduction reaction system is set longer as the temperature is lower, and is set shorter as the temperature is higher. The set time is, for example, 20 minutes to 120 minutes.

  In the denaturation step, an oxidant and an acid are mixed with the liquid obtained in the reduction step, thereby introducing the group represented by the above formula (I) into the protein and generating a CAD peptide. The acid may be mixed before the oxidant is mixed or after the oxidant is mixed.

  The oxidizing agent is used for promoting the introduction of the group represented by the above formula (I) into the protein. One or more oxidizing agents may be used, and an aqueous oxidizing agent solution and / or a gaseous oxidizing agent may be used.

  Examples of the oxidizing agent include sodium bromate, potassium bromate, sodium perborate, hydrogen peroxide, and the like. Moreover, oxygen etc. are mentioned as a gaseous oxidizing agent. When a gaseous oxidant is used, it may be supplied to the protein-containing solution by bubbling.

  The amount of the non-gaseous oxidant used is not particularly limited, but is preferably 0.001 mol or more and 0.02 mol or less based on 1 g of the manufacturing raw material, and is 0 based on the volume of the liquid in which the oxidant is mixed. 0.02 mol / L or more and 1 mol / L or less is preferable. When the amount of the oxidizing agent used is larger than the above upper limit, by-products such as cystine monooxide, cystine dioxide and cysteic acid may be produced. On the other hand, when the amount of the oxidizing agent used is less than the above lower limit, the introduction of the group represented by the formula (I) may be insufficient. In the mixing of the non-gaseous oxidant, in order to avoid locally increasing the oxidant concentration in the liquid, an oxidant aqueous solution of about 1 mol / L or more and 5 mol / L or less is gradually added over, for example, 30 minutes to 6 hours. Mix well.

  Although the temperature at the time of mixing an oxidizing agent is not specifically limited, For example, it sets to below the temperature in a reduction process.

  The acid is used for lowering the pH of the reaction system in the denaturation step and sufficiently introducing the group represented by the above formula (I) into the protein. One or two or more of these acids are used.

  Examples of the acid include organic acids such as citric acid, lactic acid, succinic acid, and acetic acid; and inorganic acids such as hydrochloric acid. If acetic acid is used, the specific odor from CAD peptide may be a problem, but if citric acid or the like is used, the specific odor can be suppressed.

  The mixing amount of the acid is not particularly limited, but it may be blended so that the pH of the reaction system in the modification step is adjusted to the following range. The final pH is preferably from 5 to 9, and particularly preferably from 6 to 8. In this way, by adjusting the final pH of the keratin mixture to the above range, introduction of the group represented by the above formula (I) into the protein can be promoted, and at the same time, disulfide group generation by thiol groups of the protein can occur. Can be suppressed. In addition, when pH in a reaction system falls locally, since there exists a possibility that the thiol group of protein may become a disulfide group, it is preferable to mix an acid into a reaction system gradually.

  The temperature in the reaction system when mixing the acid is preferably 10 ° C. or more and 60 ° C. or less, and particularly preferably 20 ° C. or more and 40 ° C. or less. By controlling within this temperature range, the production of by-products such as cystine monooxide can be suppressed. The standing time after the acid mixing is completed is, for example, 1 to 48 hours. With this standing time, the introduction of the group represented by the above formula (I) is sufficient.

  Through the denaturation step, the group represented by the above formula (I) is introduced into the protein. For example, when wool is used as a production raw material and thioglycolic acid is used as a reducing agent, the mechanism by which a carboxymethyl disulfide group, which is one of the groups represented by the above formula (I), is introduced into a protein molecule is as follows. It is as follows.

  In addition, when wool is used as a production raw material and 3-mercaptopropionic acid is used as a reducing agent, the mechanism by which a carboxyethyl disulfide group, which is one of the groups represented by the above formula (I), is introduced into a protein molecule is It is as follows.

  The protein into which the group represented by the formula (I) is introduced by the treatment in the denaturation step includes a protein that is soluble in water and a protein that is insoluble in water. When the former water-soluble protein is CAD peptide A and the latter insoluble protein needs to be removed, known solid-liquid separation means such as filtration, centrifugation, squeezing separation, sedimentation separation, and flotation separation are employed. be able to. About CAD peptide A aqueous solution, it is good to perform desalting etc. by ion exchange, electrodialysis, etc. as needed. In order to obtain solid CAD peptide A, (1) freeze drying of CAD peptide A solution, (2) spray drying of CAD peptide A solution, and (3) acid such as hydrochloric acid is added to CAD peptide A solution. A method such as recovery of CAD peptide A precipitate generated by adding and lowering the pH of the solution from about 2.5 to about 4.0 can be employed. About the collect | recovered solid CAD peptide A, it is good to perform washing | cleaning by water, acidic aqueous solution, drying, etc. as needed.

[Production Method (B)]
The production method (B) includes a reduction process, a modification process, and a hydrolysis process. The reduction process and the modification process in the production method (B) are the same as the reduction process and the modification process in the production method (A). The production method (B) including a hydrolysis step is suitable for the production of a water-soluble CAD peptide having a molecular weight of 40000 or less (40 kDa or less) (hereinafter referred to as “water-soluble CAD peptide having a molecular weight of 40000 or less”). ").

  In the hydrolysis step, the protein introduced with the group represented by the above formula (I) obtained by the treatment in the denaturation step is hydrolyzed. Known hydrolysis methods include (b1) enzymatic hydrolysis, (b2) acid hydrolysis, and (b3) alkali hydrolysis. In the hydrolysis method (b3), since the β elimination reaction of the group represented by the above formula (I) introduced into the protein may proceed, among the hydrolysis methods (b1) to (b3), an enzyme or Hydrolysis with acid is particularly preferred.

(B1) Hydrolysis by enzymes Examples of enzymes include acidic proteolytic enzymes such as pepsin, protease A, and protease B; neutral proteolytic enzymes such as papain, promelain, thermolysin, pronase, trypsin, and chymotrypsin. . Moreover, as a commercially available proteolytic enzyme, “Proteizer A” manufactured by Daiwa Chemical Industry Co., Ltd. is preferably used in the hydrolysis with an enzyme. The pH at the time of hydrolysis is preferably adjusted to 1 or more and 3 or less in the case of acidic proteolytic enzymes, and is adjusted to 5 or more and 9 or less in the case of neutral proteolytic enzymes. The reaction temperature during hydrolysis is preferably 30 ° C. or more and 60 ° C. or less, and the reaction time is preferably 10 minutes or more and 24 hours or less. In order to stop the hydrolysis, it is preferable to deactivate the enzyme at a temperature of 70 ° C. or higher.

(B2) Hydrolysis with acid Hydrolysis is performed using an inorganic acid such as hydrochloric acid, sulfuric acid, phosphoric acid, nitric acid, hydrobromic acid; and an acid appropriately selected from organic acids such as formic acid and oxalic acid. The hydrolysis conditions are, for example, pH 4 or less, reaction temperature 40 ° C. or more and 100 ° C. or less, and reaction time 2 hours or more and 24 hours or less.

(B3) Hydrolysis with alkali Hydrolysis is performed using alkali such as sodium hydroxide, potassium hydroxide, lithium hydroxide, barium hydroxide, sodium carbonate, potassium carbonate, lithium carbonate, sodium silicate, sodium borate, etc. Do. The hydrolysis conditions are, for example, alkali 1% by mass to 20% by mass, reaction temperature 15 ° C. to 100 ° C., and reaction time 30 minutes to 24 hours with respect to the total mass of the reaction system.

  When it is necessary to separate CAD peptide B, which is a water-soluble protein, from water-insoluble protein after the treatment in the hydrolysis step, it may be separated by a known solid-liquid separation means. In order to obtain solid CAD peptide B, methods such as (1) freeze-drying of CAD peptide B solution and (2) spray drying of CAD peptide B solution can be employed. About the collect | recovered solid CAD peptide B, it is good to perform washing | cleaning with water, acidic aqueous solution, drying, etc. as needed.

[Production Method (C)]
The production method (C) is a method in which a water-insoluble protein obtained in the same reduction step and denaturation step as in the production method (A) is treated in the hydrolysis step. The hydrolysis step in the production method (C) is the same as the hydrolysis step in the production method (B). Moreover, as a means for obtaining a solid CAD peptide, the means of the production method (B) may be employed.

  The production method (C) is suitable for the production of a water-soluble CAD peptide having a molecular weight of 22000 or less (22 kDa or less) (hereinafter, “water-soluble CAD peptide having a molecular weight of 22000 or less” may be referred to as “CAD peptide C”). is there.). That is, keratin, which is a constituent protein of wool, contains microfibrils having a molecular weight of 45000 to 63000 and a matrix having a molecular weight of 10,000 to 22000, and the main hydrolysis target in the hydrolysis step in the production method (C) is sulfur rather than microfibrils. Since it is a matrix-derived protein with a high content, the production method (C) is suitable for the production of CAD peptide C with a high sulfur content.

(Hair care agent)
The “hair care agent” in the present embodiment is a treatment agent for performing care and care for hair. For example, shampoos, rinses, conditioners, treatments (e.g. non-washing treatments, flushing treatments, combined hair treatments, multi-component treatments, pre-treatments for perms, post-treatments for perms, Treatments for pre-treatment of coloring, treatments for post-treatment of coloring, treatments for pre-treatment of bleach, and treatments for post-treatment of bleach) fall under such hair care agents.

  The dosage form at the time of use of a hair care agent is not specifically limited, For example, liquid form, emulsion, cream form, ointment form, gel form, solid form, foam form (foam form), and mist form are mentioned.

  As long as CAD peptide is mix | blended as one component of a hair care agent, it corresponds to the hair care agent of this embodiment. For example, a hair care agent in which a CAD peptide is blended as an additional blending component of a known hair care agent, and a hair care agent in which a CAD peptide is blended as an alternative component of the blending component of a known hair care agent correspond to the hair care agent of this embodiment.

  An appropriately selected known hair care agent raw material can be employed as the hair care agent raw material according to the present embodiment blended in addition to the CAD peptide. The known hair care raw materials include, for example, anionic surfactants, cationic surfactants, amphoteric surfactants, nonionic surfactants, alcohols, polyhydric alcohols, sugars, fats and oils, ester oils, fatty acids, ethers, hydrocarbons, Wax, silicone, synthetic polymer compound, semi-synthetic polymer compound, natural polymer compound, protein, amino acid, animal and plant extract, microorganism-derived material, inorganic compound, fragrance, preservative, sequestering agent, UV absorber, dye Etc.

Examples of the anionic surfactant include
Fatty acid soaps such as sodium salts, potassium salts, amine salts of fatty acids such as lauric acid, myristic acid, palmitic acid, stearic acid, coconut oil fatty acid;
Sodium polyoxyethylene lauryl ether sulfate, ammonium polyoxyethylene lauryl ether sulfate, polyoxyethylene lauryl ether triethanolamine sulfate, polyoxyethylene alkyl (C12-13) sodium ether sulfate, polyoxyethylene alkyl (C12-13) ether ammonium sulfate Polyoxyethylene alkyl ether sulfates such as polyoxyethylene alkyl (C12-13) ether sulfate triethanolamine;
Alkyl sulfates such as sodium lauryl sulfate, ammonium lauryl sulfate, triethanolamine lauryl sulfate;
Olefin sulfonates;
Coconut oil fatty acid ethyl ester sulfonate;
Alkyl benzene sulfonates such as dodecyl benzene sulfonate and para-toluene sulfonate;
Polyoxyethylene alkyl ether carboxylates such as sodium polyoxyethylene alkyl ether acetate (sodium polyoxyethylene tridecyl ether acetate, sodium polyoxyethylene lauryl ether acetate, sodium polyoxyethylene coconut oil fatty acid acetate, etc.);
Dialkyl sulfosuccinic acid, polyoxyalkylene alkyl sulfosuccinate, dioctyl sodium sulfosuccinate, disodium lauryl sulfosuccinate, disodium lauryl polyoxyethylene sulfosuccinate, polyoxyethylene alkyl (C12-13) disodium sulfosuccinate, polyoxyethylene alkyl (C12-14) alkylsulfosuccinates such as disodium sulfosuccinate and disodium polyoxyethylene lauroylethanolamide sulfosuccinate;
Polyoxyethylene fatty acid amide ether sulfate such as polyoxyethylene coconut oil fatty acid sodium monoethanolamide sulfate;
Taurine salts such as coconut oil fatty acid methyl taurine sodium, lauroyl methyl taurine sodium, myristoyl methyl taurine sodium, palmitoyl methyl taurine sodium, stearoyl methyl taurine sodium, coconut oil fatty acid taurine sodium, lauric acid taurine sodium, acylmethyl taurine;
Sarcosine salts such as coconut oil fatty acid sarcosine sodium, lauroyl sarcosine sodium, coconut oil fatty acid sarcosine potassium, lauroyl sarcosine potassium, coconut oil fatty acid sarcosine triethanolamine, lauroyl sarcosine triethanolamine;
Lauryl phosphate, oleyl phosphate, polyoxyethylene lauryl ether phosphate, polyoxyethylene alkyl (C12-15) ether phosphate, polyoxyethylene cetyl ether phosphate, polyoxyethylene stearyl ether phosphate, dipolyoxyethylene alkyl ether Phosphate that is a salt of sodium, potassium, ammonium, triethanolamine, etc. such as phosphoric acid, tripolyoxyethylene alkyl ether phosphoric acid, polyoxyethylene oleyl ether phosphoric acid, polyoxyethylene coconut oil fatty acid monoethanolamide phosphate ;
N-acyl-L-aspartate, N-acyl glutamate (N-coconut oil fatty acid acyl glutamate, N-lauroyl glutamate, N-myristoyl glutamate, N-palmitoyl glutamate, N-stearoyl glutamate, N -Oleoyl glutamate, etc.), N-acylmethylalanine salt (N-coconut oil fatty acid methylalanine salt, N-lauroylmethylalanine salt, N-myristoylmethylalanine salt), N-acylsarcosine salt (N-coconut oil) Salts of amino acid derivatives such as fatty acid sarcosine salts, N-lauroyl sarcosine salts, N-myristoyl sarcosine salts, N-oleoyl sarcosine salts), N-acyl silk amino acid salts (N-lauroyl silk amino acid salts, etc.); .

Examples of the cationic surfactant include ammonium salts. Examples of the ammonium salt include trimethylammonium salts such as cetyltrimethylammonium bromide, stearyltrimethylammonium bromide, stearyltrimethylammonium chloride;
And dimethylammonium salts such as dimethyldistearylammonium chloride, dicocoyldimethylammonium chloride, and ethyl sulfate lanolin fatty acid aminopropylethyldimethylammonium. Other examples of the cationic surfactant include benzalkonium chloride and laurylamine oxide.

Examples of the amphoteric surfactant include
Imidazoline-based amphoteric surfactants such as 2-cocoyl-2-imidazolinium hydroxide-1-carboxyethyloxy disodium salt;
Betaine surfactants such as imidazolinium betaine, alkyl betaine, amide betaine, sulfobetaine;
And acylmethyl taurine.

Examples of nonionic surfactants include
Sorbitan fatty acid esters such as sorbitan monostearate and sorbitan sesquioleate;
Glycerin fatty acids such as glyceryl monostearate;
Glycerol fatty acid esters such as glycerol monostearate, glycerol monoisostearate, glycerol triisostearate;
Propylene glycol fatty acid esters such as propylene glycol monostearate;
Hardened castor oil derivative;
Glycerin alkyl ether;
POE sorbitan fatty acid esters such as POE sorbitan monooleate and polyoxyethylene sorbitan monostearate;
POE glycerol fatty acid esters such as POE glycerol monoisostearate;
POE fatty acid esters such as polyethylene glycol monooleate and POE distearate;
POE alkyl ethers such as POE lauryl ether, POE cetyl ether, POE oleyl ether, POE stearyl ether, POE2-octyldodecyl ether;
POE alkyl phenyl ethers such as POE nonyl phenyl ether;
Pluronic type;
POE · POP alkyl ethers such as POE · POP2-decyltetradecyl ether;
Tetronic type;
POE castor oil and POE castor oil derivatives;
POE hydrogenated castor oil and POE hydrogenated castor oil derivative;
Other examples include sucrose fatty acid esters, alkyl glucosides, decyl glucosides, coconut oil fatty acid monoethanolamide, coconut oil fatty acid diethanolamide, tetraoleic acid POE sorbitol, and the like. In the above compounds, “POE” means “polyoxyethylene”, and “POP” means “polyoxypropylene”.

Examples of the alcohol include
Lower monohydric alcohols having 6 or less carbon atoms, such as ethanol, propanol, and isopropanol;
Higher monohydric alcohols such as cetyl alcohol, stearyl alcohol, isostearyl alcohol, behenyl alcohol, octyldodecanol, myristyl alcohol and the like can be mentioned.

As an example of the polyhydric alcohol,
Ethylene glycol, propylene glycol, diethylene glycol, dipropylene glycol, glycerin, diglycerin, 1,3-butylene glycol, erythritol, isoprene glycol, 1,2-pentanediol, 2,4-hexanediol, 1,2-hexanediol, 1,2-octanediol and the like can be mentioned.

Examples of the saccharide include
Examples include sorbitol, trehalose, glucose, sucrose, xylitol, maltitol and the like. Examples of the oils and fats include macadamia nut oil, avocado oil, corn oil, olive oil, rapeseed oil, sesame oil, castor oil, safflower oil, cottonseed oil, jojoba oil, palm oil, palm oil, hardened palm oil, hardened oil, Examples include hardened castor oil and shea fat.

Examples of the ester oil include
Capryryl eicosenoate, cetyl ethylhexanoate, alkyl octanoate, isotridecyl isononanoate, isopropyl myristate, isopropyl myristate, octyl isononanoate, isotridecyl isononanoate, PEG-3 glyceryl trioleate, PEG-3 glyceryl triisostearate, myristine PPG-3 benzyl acid, dioctyldodecyl lauroyl glutamate, PEG-5 glyceryl trioleate, PEG-5 glyceryl triisostearate, PEG-5 glyceryl triisostearate, dioctyl succinate, lanolin fatty acid cholesteryl, dipentaerythritol fatty acid ester, etc. Can be mentioned.

Examples of the fatty acids include
And higher fatty acids such as oleic acid, isostearic acid, lauric acid, myristic acid, palmitic acid, stearic acid, and undecylenic acid.

Examples of the ether include
Examples include ethylene glycol monomethyl ether and ethylene glycol monoethyl ether.

Examples of the hydrocarbon include
Examples thereof include liquid paraffin, squalane, pristane, ozokerite, paraffin, ceresin, petrolatum, and microcrystalline wax.

Examples of the wax include
Examples include beeswax, mole, candelilla wax, carnauba wax, ibota wax, lanolin, hydrogenated reduced lanolin, jojoba wax and the like.

Examples of the silicone include
Dimethiconol, methylphenylpolysiloxane, decamethyltrisiloxane, methylpolysiloxane, cross-linked methylpolysiloxane, highly polymerized dimethylpolysiloxane, decamethylcyclopentasiloxane, polyoxyethylene / methylpolysiloxane copolymer, dimethylsiloxane / methylstea Roxysiloxane copolymer, amino-modified silicone (aminoethylaminopropylsiloxane / dimethylsiloxane copolymer, aminoethylaminopropylmethylsiloxane / dimethylsiloxane copolymer, highly polymerized dimethylsiloxane / methyl (aminopropyl) siloxane copolymer, etc. ), Trimethylsiloxysilicic acid, methyl hydrogen polysiloxane and the like.

Examples of the synthetic polymer compound include
Examples thereof include carboxyvinyl polymer, polyvinyl alcohol, polyvinyl pyrrolidone, polyacrylic acid, methacryloylethylbetaine / methacrylic acid ester copolymer, and the like.
Examples of the semi-synthetic polymer compound include
Examples include methyl cellulose, hydroxyethyl cellulose, hydroxypropyl cellulose, carboxymethyl cellulose, and soluble starch.
Examples of the natural polymer include
Examples include sodium alginate, xanthan gum, aluminum oxalate, quince seed extract, tragacanth gum, starch and the like.

Examples of the protein include
Examples include hydrolyzed soy protein, (dihydroxymethylsilylpropoxy) hydroxypropyl hydrolyzed soy protein, (dihydroxymethylsilylpropoxy) hydroxypropyl hydrolyzed sesame protein, hydrolyzed rice protein, and the like.

Examples of the amino acids include
Examples thereof include glycine, alanine, valine, leucine, isoleucine, phenylalanine, tryptophan, cystine, cysteine, methionine, proline, hydroxyproline, aspartic acid, glutamic acid, arginine, histidine, lysine and derivatives thereof.

Examples of the animal and plant extracts and microorganism-derived extracts are:
Ascorbic acid and its alkali metal salt or alkaline earth metal salt, L-ascorbic acid alkyl ester, L-ascorbic acid phosphate and its salt, L-ascorbic acid-2-sulfate and its salt, L-ascorbic acid glucoside Ascorbic acid derivatives such as;
Alkoxysalicylic acid and its salts;
Hydroquinone glycosides and derivatives thereof;
Kojic acid and its derivatives;
Others, ellagic acid, chamomile extract, altea extract, licorice extract, scorpion extract, raspberry extract, apple flavonoid, bran extract, vitamin E and its derivatives, hinokitiol, placenta extract, lucinol, chamomile ET, glutathione, clove extract, tea extract, Astaxanthin, bovine placenta extract, tranexamic acid and its derivatives, derivatives of resorcin, azulene, γ-hydroxybutyric acid, ashitaba extract, avocado extract, achacha extract, arnica extract, aloe extract, apricot extract, ginkgo biloba extract, ginkgo biloba extract , Turmeric extract, Oolong tea extract, Ages extract, Echinacea leaf extract, Ogon extract, Oat extract, Auren extract, Barley extract, Hypericum extract, Licorice extract, Dutch mustard extract, orange extract, seawater dried product, seaweed extract, hydrolyzed elastin, hydrolyzed wheat powder, hydrolyzed silk, chamomile extract, carrot extract, Chinese mugwort extract, licorice extract, oil-soluble licorice extract, calcade extract Extract Fermented extract, Rice germ oil, Comfrey extract, Cowberry extract, Saishin extract, Psycho extract, Saitai extract, Salvia extract, Soap extract, Sasa extract, Hawthorn , Salamander extract, Shiitake extract, Giant extract, Shikon extract, Perilla extract, Linden extract, Shimotake extract, Peonies extract, Pepper root extract, Birch extract, Horsetail extract, Kizuta extract, Hawthorn extract, Elderflower extract, Yarrowworm extract, Mint extract, sage extract, mallow extract, nematode extract, senbu extract, soybean extract, taisu extract, thyme extract, tea extract, chigaya extract, chimpi extract, clove extract, cassava extract, tonin extract, spruce extract, dokudami extract, tomato extract, natto Extract, carrot extract, garlic extract, wild rose extract, hibiscus extract, bacmond extract, parsley extract, hammamels Kiss, Parietalia extract, toad extract, bisabolol, loquat extract, dandelion extract, fuquito extract, butterfly extract, butcher bloom extract, grape extract, propolis, loofah extract, safflower extract, peppermint extract, body extract, button extract, hop extract, pine extract , Maronnier extract, Citrus extract, Mukuroji extract, Melissa extract, Peach extract, Cornflower extract, Eucalyptus extract, Yukinoshita extract, Yuzu extract, Yakuinin extract, Artemisia extract, Lavender extract, Apple extract, Lettuce extract, Lemon extract, Forsythia extract, Rose extract, Examples include rosemary extract, Roman chamomile extract, royal jelly extract, and honey.

Examples of the inorganic compound include
Metal oxides such as titanium oxide, zirconium oxide, zinc oxide, cerium oxide, magnesium oxide;
Metal sulfates such as barium sulfate, calcium sulfate, magnesium sulfate;
Metal carbonates such as calcium carbonate and magnesium carbonate;
Silicic acid and silicic acid derivatives such as anhydrous silicic acid, aluminum silicate, magnesium silicate, magnesium aluminum silicate, calcium silicate, barium silicate, strontium silicate;
In addition, tungstic acid metal salt, hydroxyapatite, vermiculite, hydrite, bentonite, montmorillonite, hectorite, zeolite, ceramic powder, dicalcium phosphate, alumina, aluminum hydroxide, boron nitride, silica and the like can be mentioned.

Examples of the preservative include
Examples include benzoic acid, sodium benzoate, salicylic acid, methyl paraoxybenzoate, propyl paraoxybenzoate, benzene paraoxybenzoate, phenoxyethanol, and hinokitiol.

Examples of the sequestering agent include:
Examples include alanine (also classified as the aforementioned amino acids), edetic acid, edetate disodium, diethylenetriaminepentaacetic acid, and the like.

  The hair treatment method using the hair care agent of the present invention typically includes a step of applying the hair care agent to the hair, and a step of washing the hair on which the hair care agent has been applied. Moreover, you may perform well-known pre-processing and post-processing with respect to hair before and after such a hair treatment.

  Hereinafter, the present invention will be described more specifically with reference to examples. However, the present invention is not limited to the following examples unless departing from the gist of the present invention.

[Example 1]
A 3% by mass aqueous solution of CAD peptide A was prepared as the hair care agent of Example 1.

  CAD peptide A used in Example 1 was recovered from an aqueous CAD peptide A solution produced according to the following reduction and denaturation steps.

(Reduction process)
Merino wool, washed with neutral detergent and dried, was cut to about 5 mm. 5 g of this wool, 15.4 g of a 30% by mass sodium thioglycolate aqueous solution and 8.5 g of a 6 mol / L sodium hydroxide aqueous solution were mixed, and ion-exchanged water was further mixed to prepare a mixture of 150 ml in total volume and pH 11. The mixture was stirred at 45 ° C. for 1 hour. Subsequently, water was further mixed to make a total volume of 200 ml, left under conditions of 45 ° C. for 2 hours, and then naturally cooled until the liquid temperature reached room temperature.

(Modification process)
While stirring the mixed solution after the reduction step, 25 g of an aqueous solution containing 2.05 g of sodium bromate was mixed with the mixed solution over about 60 minutes. Thereafter, stirring of the mixed solution was continued throughout, and 100 g of an aqueous solution containing 7.08 g of citric acid was mixed with the mixed solution over about 85 minutes to obtain a CAD peptide A aqueous solution. The pH after mixing with citric acid was 7.

  The solid part was separated by filtration from the CAD peptide A aqueous solution obtained by the treatment in the denaturing step. Thereafter, precipitation of CAD peptide A was caused by adding 36 mass% hydrochloric acid aqueous solution to bring the pH of CAD peptide A aqueous solution to 3.8. This precipitate was recovered and washed with water to obtain a solid CAD peptide A.

  The molecular weight of CAD peptide A was confirmed by a sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) method using “Protein Molecular Weight Marker (Low)” manufactured by Takara Bio Inc. as a reference substance. As a result, the molecular weight of CAD peptide A was confirmed to be in the range of 40,000 to 63,000 (40 kDa to 63 kDa).

[Example 2]
A 3% by mass aqueous solution of CAD peptide C was prepared as the hair care agent of Example 2.

  CAD peptide C used in Example 2 is a product obtained by hydrolyzing the solid portion filtered and separated from the aqueous solution of CAD peptide A used in Example 1. The hydrolysis procedure was as follows. 100 parts by mass of the solid part separated by filtration, 1 part by mass of a proteolytic enzyme (“Proteerizer A” manufactured by Daiwa Chemical Co., Ltd.), and an appropriate amount of sodium bicarbonate and water were mixed so that the pH would be 8.0 to 8.5. The hydrolysis reaction was allowed to proceed for 20 minutes in water at 50 ° C. Thereafter, the proteolytic enzyme was inactivated at 80 ° C. for 5 minutes. After the deactivation, an aqueous solution of CAD peptide C was obtained by filtration. When the molecular weight of the CAD peptide of Example 2 was confirmed by the same SDS-PAGE method, a CAD peptide having a molecular weight exceeding 22,000 could not be confirmed. That is, it was confirmed that the molecular weight of the CAD peptide of Example 2 was within the range of 22000 or less (22 kDa or less).

[Reference Example 1]
“Now Road Pro Hikeratin” manufactured by Milbon, containing 17% by mass of hydrolyzed keratin, was prepared as a hair care agent of Reference Example 1.

[Test Example 1]
Using the hair care agent of Example 1, Example 2 or Reference Example 1, hair treatment was performed according to the following.

  The slow-waved black hair was washed with shampoo ("Deceths Aufé Base Aqua A" manufactured by Milbon), dried with warm air, and then left overnight in an atmosphere at a temperature of 25 ° C and a humidity of 50%. Using this black hair as a hair sample, the hair sample was immersed in the hair care agent of Example 1, Example 2 or Reference Example 5 for 5 minutes, washed with water, and then dried with warm air.

  About the said processed hair sample, the initial stage elastic modulus and breaking strength per unit cross-sectional area were measured. In this test example, the average value of the measured values for the three hair samples was taken as the initial elastic modulus and breaking strength. The measuring machine used was "TENSILON UTM-II-20" manufactured by Orientec. Measurement conditions were such that the hair sample was immersed in water for 24 hours before the measurement, the hair sample was immersed in water at the time of measurement, the temperature was 25 ° C., the pulling speed was 2 mm / min, and the tension interval of the hair sample was 20 mm.

  The results of Test Example 1 are shown in Table 1. “Untreated” in Table 1 indicates an example in which the initial elastic modulus and the breaking strength were measured for slow-waved black hair that was not treated with a hair care agent. As shown in Table 1, it can be confirmed that the values of the initial elastic modulus and the breaking strength of Examples 1 and 2 are higher than those of the Reference Examples and untreated values.

[Test Example 2]
The hair damaged greatly as described later was used as a hair sample, the hair sample was immersed in the hair care agent of Example 1 or Example 10 for 10 minutes, washed with water, and then dried with warm air. Thereafter, the initial elastic modulus and breaking strength of each of the five hair samples were measured in the same manner as in Test Example 1, and the average value was obtained. Similarly, the damaged hair was used as a hair sample, and the initial elastic modulus and breaking strength were measured without performing treatment with a hair care agent (referred to as “untreated” as in Test Example 1).

  The hair sample in Test Example 2 is obtained by treating straight black hair as follows. Straight hair black hair was processed by the procedures of bleaching, perm treatment, color treatment, hair washing treatment, color treatment, hair washing treatment, perm treatment, color treatment, hair washing treatment, color treatment, hair washing treatment, and drying treatment.

  In the bleaching treatment, the first agent and the second agent of “Promatis Flave-Ad” manufactured by Milbon were mixed in a ratio of about 1 part by mass: 2 parts by mass, and this was applied to the hair. The coating amount was twice the hair mass. The coated hair was covered with a film, washed with shampoo after 15 minutes, and dried with warm air.

  In the perm treatment, hair wound around a perm rod with a diameter of 12 mm is dipped in the first agent of “Pre-Cum C / T” manufactured by Milbon for 10 minutes, washed with water, and then second of “Pre-Cum C / T”. It was immersed in the agent for 10 minutes and washed with water. Thereafter, the hair was dried with warm air.

  In the color treatment, the first and second agents of “Oldive” manufactured by Milbon were mixed at a ratio of about 1 part by mass to about 1 part by mass, and this was applied to the hair. The coating amount was 10 times the mass of the hair, and was allowed to stand for 10 minutes after coating.

  In the hair washing treatment, hair shampooing, treatment, and warm air drying were defined as one cycle, and these 60 cycles were performed. In the shampoo, shampoo (“Lux Super Rich Shine” manufactured by Unilever Co., Ltd.) 5 times the mass of the sample hair was applied to the hair, allowed to stand for 3 minutes and then washed with water. In the treatment, 5 times the sample hair mass (Unilever “Luxe Super Rich Shine”) was applied to the hair, allowed to stand for 3 minutes and then washed with water.

  The results of Test Example 2 are shown in Table 2. As shown in Table 2, it can be confirmed that the initial elastic modulus is improved in both Example 1 and Example 2 as compared with the case of no treatment. Moreover, although the breaking strength of Example 1 is falling rather than untreated, it can confirm that the breaking strength of Example 2 was improving rather than untreated. That is, according to the hair care agent of Example 2 in which the CAD peptide C having a molecular weight of 22000 or less is blended, it can cope with hair properties that are greatly damaged.

[Examples 3-4, Comparative Example 1 and Reference Examples 2-3]
Stearyltrimethylammonium chloride 0.8% by mass, isopropanol 0.2% by mass, cetanol 3% by mass, behenyl alcohol 0.8% by mass, propylene glycol 0.02% by mass, dipropylene glycol 2% by mass, soft lanolin fatty acid cholesteryl 4% by mass, 2% by mass of shea fat, 0.06% by mass of hydroxyethylcellulose, 0.2% by mass of tamarind seed gum, 1% by mass of dimethiconol, 16% by mass of decamethylcyclopentasiloxane, 2% by mass of methylpolysiloxane, cross-linked type 0.2% by weight of methylpolysiloxane, 2% by weight of amino-modified silicone, 0.1% by weight of highly polymerized dimethylsiloxane / methyl (aminopropyl) siloxane copolymer, cocamidopropyldimethylammoniohydroxypropyloxypropylsiloxane Polypolysiloxane copolymer acetate 0.5% by mass, acrylamide-2- (acryloyloxy) ethyltrimethylammonium chloride copolymer 0.03% by mass, antioxidant 0.05% by mass, preservative 0.2% by mass % And fragrance 0.2% by mass were prepared in a cream 1 for a non-washed treatment (a type of treatment that was not washed away) prepared by blending in water (Comparative Example 1). In addition, by blending 4% by mass aqueous solution of CAD peptide A adjusted to pH 8.72 with arginine in the above cream 1 at a ratio of 5% by mass and 1% by mass, respectively, Cream 2 (Example 3) having a ratio of 0.2% by mass and Cream 3 (Example 4) having the same ratio of 0.04% by mass were prepared. On the other hand, a 5% by weight aqueous solution of keratin (“Keratec IFP-HMW” manufactured by Croda Japan Co., Ltd.) is blended in Cream 1 at a ratio of 4% by weight and 0.8% by weight, respectively, so that the ratio of keratin is 0. Cream 4 (Reference Example 2) having a content of 2% by mass and Cream 5 (Reference Example 3) having the same ratio of 0.04% by mass were prepared.

[Test Example 3]
After applying each of the above creams 1 to 5 (Examples 3 to 4, Comparative Example 1 and Reference Examples 2 to 3) to human hair, a sensory evaluation was performed on the order of thickness feeling (thickness feeling was the most). The best one was ranked first and the worst one was ranked fifth). Moreover, it applied also to the hair of the wig and the same evaluation was performed.

  Here, the “thickness” means a feeling that a certain substance is coated on the surface of the hair. The results of sensory evaluation of the feeling of thickness after treatment with each cream are shown in Table 3. From the results in Table 3, Example 3 and Example in which CAD peptide A was blended compared to the cream in Comparative Example 1 in which neither CAD peptide A nor keratin was blended or the cream in Reference Examples 1 and 2 in which keratin was blended were used. The cream of No. 4 was found to have a greater sense of thickness.

[Example 5 and Reference Example 4]
A 4% by mass aqueous solution of CAD peptide A adjusted to pH 8.72 with arginine was diluted with water to give a 1% by mass aqueous solution (Example 5; this aqueous solution is referred to as “mist 1”). In addition, a 5% by mass aqueous solution of keratin (“Keratech IFP-HMW” manufactured by Croda Japan Co., Ltd.) was diluted with water to give a 1% by mass aqueous solution (Reference Example 4; this aqueous solution is referred to as “mist 2”).

[Test Example 4]
Each of the mists 1 and 2 (Example 5 and Reference Example 4) was sprayed on human hair, and then the degree of firmness and firmness was subjected to sensory evaluation.

  Table 4 shows the results of sensory evaluation of elasticity and firmness after the treatment with each mist. From the results of Table 4, it was found that the firmness and firmness of the mist of Example 5 containing CAD peptide A was greater than that of Reference Example 4 containing keratin.

[Examples 6 and 7 and Reference Example 5]
Treatment cream 6 (Example 6) was prepared by blending 2% by weight CAD peptide A, 2% by weight cetyltrimethylammonium bromide, 1% by weight ethanol, 3% by weight cetanol and 2% by weight stearyl alcohol in water. . Further, treatment cream 7 (Reference Example 5) was prepared by adding 2% by mass of cetyltrimethylammonium bromide, 0.05% by mass of stearyltrimethylammonium chloride, 0.08% by mass of dicocoyldimethylammonium chloride, polyoxyethylene cetyl ether (20E O.) 0.01% by mass, ethanol 1% by mass, cetanol 6% by mass, highly polymerized dimethylsiloxane 2% by mass, aminoethylaminopropylsiloxane / dimethylsiloxane copolymer 1% by mass, ethyl lanolin sulfate fatty acid aminopropylethyl Prepared by blending 0.01% by weight of dimethylammonium (2), 0.2% by weight of amino acid, 0.3% by weight of preservative and 0.3% by weight of perfume into water. Further, a two-component treatment was prepared in which the cream 6 was the first agent and the cream 7 was the second agent (Example 7).

[Test Example 5]
About the said cream 6 of Example 6, after applying the cream 6 to the hair bundle for evaluation and making it adjust to the whole hair bundle, it washed with water and dried with warm air. On the other hand, about the said cream 7 of the reference example 5, after apply | coating the cream 7 to the hair bundle for evaluation and making it adjust to the whole hair bundle, it washed with water and dried with warm air. For the two-component treatment consisting of the creams 6 and 7 in Example 7, apply cream 6 (first agent) and cream 7 (second agent) to the evaluation hair bundle in this order, After making it adjust to the whole bundle, it washed with water and dried with warm air. And sensory evaluation was performed about the grade of the thickness of the hair | bristle bundle after these processes.

  Table 5 shows the results of sensory evaluation of the feeling of thickness after treatment by each treatment. As shown in Table 5, in Examples 6 and 7, a strong thickness feeling was obtained.

[Examples 8 to 13, Comparative Examples 2 to 3, and Reference Examples 6 to 11]
Shampoo A (Comparative Example 2) and shampoos 1 to 6 (Examples 8 to 10 and Reference Examples 6 to 8) were prepared as follows. Preparation of shampoo A (Comparative Example 2) was prepared by 5% by weight of sodium polyoxyethylene lauryl ether sulfate, 4% by weight of triethanolamine lauryl sulfate, 2% by weight of sodium polyoxyethylene lauryl ether acetate, sodium lauroylmethyl-β-alanine 0 .9% by mass, lauric acid amidopropyl betaine 4% by mass, coconut oil fatty acid diethanolamide 3% by mass, coconut oil fatty acid monoethanolamide 0.1% by mass, 1,3-butylene glycol 0.2% by mass, o-chloride [2-Hydroxy-3- (trimethylammonio) propyl] hydroxyethylcellulose 0.4% by weight, chelating agent 0.3% by weight, preservative 0.3% by weight, antioxidant 0.1% by weight and perfume 0. It was carried out by blending 2% by mass with water. Preparation of shampoo 1 (Example 8) in which the proportion of CAD peptide A is 0.2% by mass, preparation of shampoo 2 (Example 9) in which the proportion is 0.12% by mass, and the proportion is 0.04 Preparation of the shampoo 3 (Example 10) which is mass% was performed by blending the CAD peptide A 4 mass% aqueous solution with water in addition to the blending raw material of shampoo A (Comparative Example 2). In addition, preparation of shampoo 4 (Reference Example 6) having a keratin ratio of 0.2% by mass, preparation of shampoo 5 (Reference Example 7) having the same ratio of 0.12% by mass, and the same ratio of 0.04%. Preparation of shampoo 6 (Reference Example 8), which is mass%, is carried out by adding an aqueous solution containing 5% by mass of keratin (“Keratech IFP-HMW” manufactured by Croda Japan Co., Ltd.) to the blended raw material of shampoo A (Comparative Example 2). It was carried out by blending.

  Treatment A (Comparative Example 3) and Treatments 1-6 (Examples 11-13 and Reference Examples 9-11) were prepared as follows. Preparation of Treatment A (Comparative Example 3) was performed using 2% by mass of cetyltrimethylammonium bromide, 3% by mass of alkyltrimethylammonium chloride, 0.8% by mass of ethanol, 0.7% by mass of isopropanol, 5% by mass of cetanol, and stearyl alcohol 2 Mass%, concentrated glycerin 4 mass%, polyoxyethylene stearyl ether 0.5 mass%, cetyl 2-ethylhexanoate 1 mass%, dipentaerythritol fatty acid ester 0.8 mass%, squalane 0.3 mass%, high It was carried out by blending 0.3% by mass of polymerized methylpolysiloxane, 0.2% by mass of dimethylsiloxane / methylstearoxysiloxane copolymer, 0.2% by mass of preservative and 0.3% by mass of perfume into water. Preparation of Treatment 1 (Example 11) in which the proportion of CAD peptide A is 0.2% by mass, Preparation of Treatment 2 (Example 12) in which the proportion is 0.12% by mass, and the same ratio is 0.04 Preparation of Treatment 3 (Example 13) in mass% was carried out by blending the above CAD peptide A 4 mass% aqueous solution with water in addition to the ingredients of Treatment A (Comparative Example 3). Also, the preparation of Treatment 4 (Reference Example 9) having a keratin ratio of 0.2% by mass, the preparation of Treatment 5 (Reference Example 10) having the same ratio of 0.12% by mass, and the same ratio of 0.04%. Preparation of Treatment 6 (Reference Example 11), which is mass%, is performed by adding an aqueous solution containing 5% by mass of keratin (“Keratech IFP-HMW” manufactured by Croda Japan Co., Ltd.) in addition to the ingredients of Treatment A (Comparative Example 3). And blended in water.

[Test Example 6]
A plurality of hair bundles obtained by combining 3 g of the bleached hair were prepared and used as evaluation hair bundles. Combinations of shampoos (Examples 8 to 10, Reference Examples 6 to 8 and Comparative Example 2) and Treatment A (Comparative Example 3) shown in Table 6 (a) below, and Shampoo A (Comparative Example 2) and Using a combination of treatments (Examples 11 to 13, Reference Examples 9 to 11 and Comparative Example 3) shown in Table 6 (b), shampoo application and water washing, and treatment application and water washing for each hair bundle Then, it was dried with warm air. And the sensory evaluation was performed on the basis of Comparative Example 2 or Comparative Example 3 with respect to the sense of thickness, smoothness and softness of the hair bundle after these treatments.

  Tables 6 (a) and 6 (b) show the results of sensory evaluation of the sense of thickness, smoothness and softness after the treatment with each shampoo and treatment (the evaluation "-" in the table was not evaluated) Is shown.)

As described above, since the hair care agent of the present invention can effectively improve the initial elastic modulus of damaged hair, it is preferably used for hair treatment for business use or home use.

Claims (6)

A hair care agent containing a peptide,
A hair care agent, wherein the peptide comprises a group having a group represented by the following formula (I) as a side chain group.
_{-S-S- (CH 2) n} COO- (I)
(In the formula (I), n is 1 or 2.)   The hair care agent according to claim 1, wherein the side chain group has one or more selected from carboxymethyl disulfide group, carboxymethyl disulfide group salt, carboxyethyl disulfide group and carboxyethyl disulfide group salt.   The hair care agent according to claim 1 or 2, which is a shampoo, rinse, treatment, or conditioner.   The hair care agent according to claim 1, 2 or 3, wherein the molecular weight of the peptide is 22,000 or less.   The hair care agent according to any one of claims 1 to 4, wherein the dosage form at the time of use is liquid, emulsion, cream, ointment, gel, solid, foam, or mist.   A hair treatment method using the hair care agent according to any one of claims 1 to 5.