JPH11240821A - Hair treating agent - Google Patents

Abstract

PROBLEM TO BE SOLVED: To obtain the subject agent capable of imparting rich gloss and smoothness to hair, preventing damage to the hair such as spirit hair or broken hair, having even restorative effects on the split hair and useful as a hair rinse, or the like," by including a specific decomposition derivative of a keratinous substance and a specified silylated peptide therein. SOLUTION: This agent is obtained by including (A) one or more kinds of compounds selected from a hydrolyzate of a keratinous substance, an alkali salt of an oxidative decomposition product of the keratinous substance and an alkali salt of a derivative at the thiol group of a reductive decomposition product of the keratinous substance and (B) a silylated peptide represented by formula I or II R<1> to R<3> are each a 1-3C alkyl or the like; R<4> is a residue except the terminal amino group of a basic amino acid having amino group at the side-chain terminal; R<5> is an amino acid side chain other than R<4> ; (a) is 1 or 3; (m) and (n) are each 0-200; [(m)+(n)] is 1-200, with the proviso that (m) and (n) denote each only the number of the amino acids without denoting the order of the amino acid sequence}. The respective amounts of the ingredient. A and B are preferably 0.05-10.0 wt.% ingredient A and 0.05-30.0 wt.% ingredient B.

Description

DETAILED DESCRIPTION OF THE INVENTION

[0001]

BACKGROUND OF THE INVENTION 1. Field of the Invention The present invention relates to a hair treatment agent which imparts excellent luster and smooth feel to hair and has an effect of repairing split ends.

[0002]

2. Description of the Related Art Conventionally, hydrolyzed proteins and hair cosmetics such as shampoos, hair rinses, hair treatment agents, hair styling agents, agents for permanent waving, and hair dyes have been used.
High molecular substances such as cationized cellulose and silicone are blended to prevent physical damage to the hair due to washing, brushing, drying with a hair dryer, etc., and damage to the hair due to chemical treatments such as permanent wave treatment and hair dyeing treatment. Attempts have been made to prevent and restore damaged hair.

[0003]

However, polysaccharides such as cationized cellulose are effective in improving hair fingering during shampooing and increasing the volume of hair after drying, but are not effective in shampooing and chemical treatment. When the protein components of the hair elute and damage the hair, the moisture retention of the hair is reduced, and when the hair becomes dry, it cannot be eliminated, and after drying, There is a problem that burns out or the combability deteriorates.

[0004] Silicone is useful for imparting gloss and improving combability, but silicone is originally a lipophilic (hydrophobic) substance, and hair with little damage, that is, strong hydrophobicity. It is easy to adsorb to hair, but it is said that it is difficult to adsorb to damaged hair, that is, hair whose hydrophilicity has become stronger due to exposure of hydrophilic groups to the surface due to damage. There has been a problem that the characteristics cannot be sufficiently exhibited.

[0005] In order to prevent such damage to the hair, a hair rinse agent and a hair treatment agent containing a quaternary ammonium salt have been used. However, although this method has the effect of softening the hair and preventing electrification, it does not restore the protein lost from the hair, so that only a temporary effect can be expected. Met.

[0006]

Under the present circumstances, the present inventors have conducted intensive studies to obtain a hair treatment agent having an excellent hair protection effect, and found that a specific keratin substance-decomposing derivative and an amino acid having an amino acid side chain were used. A hair treatment agent is prepared by blending a silylated peptide in which a functional group containing only one silicon atom is covalently bonded to the amino group of the peptide containing a group to prevent damage to the hair, The present inventors have found that an excellent hair treatment agent which gives moisture and flexibility, prevents split ends and improves combability of hair can be obtained, and has completed the present invention.

That is, the present invention is a hair treatment agent containing the following (A) and (B).

(A) a kind of a keratin substance-decomposing derivative selected from the group consisting of a hydrolyzate of a keratin substance, an alkali salt of an oxidative decomposition product of a keratin substance, and an alkali salt of a derivative in the thiol group of a reduced decomposition product of the keratin substance Or two or more. (B) A silylated peptide in which a functional group containing only one silicon atom is covalently bonded to an amino group of a peptide containing an amino group in an amino acid side chain represented by the following general formula (I) or (II).

[0009]

Embedded image

[Wherein R ¹ , R ² and R ³ represent an alkyl group having 1 to ³ carbon atoms or a hydroxyl group, and these R ¹ , R ² and R 3
All ^three may be the same or different. R ⁴
Represents a residue excluding a terminal amino group of a basic amino acid having an amino group at a terminal of a side chain, R ⁵ represents an amino acid side chain other than R ⁴ , a represents 1 or 3, m represents 0 to 200, n is 0
-200 and m + n are 1-200. (However, m and n only indicate the number of amino acids, and do not indicate the order of the amino acid sequence.)]

[0011]

Embedded image

Wherein R ¹ , R ² and R ^{3 each} have 1 to ³ carbon atoms.
Represents an alkyl group or a hydroxyl group of R ¹ , R 2
² and R ³ may be the same or different. R ⁴ represents a residue excluding a terminal amino group of a basic amino acid having an amino group at a terminal of a side chain, R ⁵ represents an amino acid side chain other than R ⁴ , a represents 1 or 3, and m represents 0 to 0. 20
0 and n are 0 to 200, and m + n is 1 to 200. (However, m and n only indicate the number of amino acids, and do not indicate the order of the amino acid sequence.)]

(A) Keratin substance-decomposing derivative The keratin substance-decomposing derivative which is the component (A) of the present invention hydrolyzes a keratin substance, oxidizes and decomposes a keratin substance, and converts the keratin substance into an alkali salt. After the substance is reductively decomposed, the thiol group is chemically modified into a derivative, and the derivative is converted into an alkali salt.
Examples of the keratin material as a raw material include animal hair, hair, feathers, nails, horns, hooves, scales, and the like, and wool, hair, and feathers are particularly preferable. These keratin substances can be directly subjected to an oxidation or reduction reaction, but if necessary, cut or crushed to an appropriate size, or washed,
Pretreatment such as degreasing may be performed.

The decomposition of the keratin substance is performed by any of the following methods. (1) Hydrolysis Reaction Hydrolysis by Acid Examples of the acid include inorganic acids such as hydrochloric acid, sulfuric acid, phosphoric acid, nitric acid, and hydrobromic acid, and organic acids such as acetic acid, formic acid, and oxalic acid. These are generally used at a concentration of 3 to 85%, but it is desirable that the hydrolysis reaction always has a pH of 4 or less. The reaction temperature is preferably from 40 to 100 ° C, but can be increased to 160 ° C under pressure. The reaction time is preferably 2 to 24 hours. The reaction product is neutralized with an alkali such as sodium hydroxide, sodium carbonate, ammonia or the like, and can be used as it is. However, it can be further purified by gel filtration, ion exchange resin or the like before use. The product obtained by such acid hydrolysis does not cause any change other than hydrolysis to the polypeptide chain of keratin as compared with the product obtained by alkaline hydrolysis, so that good results can be obtained.

Hydrolysis by alkali As the alkali, sodium hydroxide, potassium hydroxide, lithium hydroxide, barium hydroxide, sodium carbonate, potassium carbonate, lithium carbonate, sodium silicate,
An inorganic alkali such as borax is used. These are generally suitable in concentrations of 1 to 20%. If the alkali is used more than necessary, the color of the hydrolyzate solution becomes brown to black, which is not preferable. The reaction is carried out at room temperature to 100 ° C. for 3 hours.
It is preferable to carry out the reaction for 0 minute to 24 hours, and it is necessary not to raise the temperature too much or to lengthen the reaction time more than necessary. Hydrolysis with alkali has the advantage that the hydrolyzate of keratin dissolves with the progress of the reaction, and the progress of the reaction is visible. The reaction may be terminated when the reaction mixture becomes a homogeneous solution.

As the enzyme, there may be used an acidic protease such as pepsin, protease A and protease B, and a neutral protease such as papain, promelain, thermolysin, trypsin, pronase and chymotrypsin. The pH at the time of hydrolysis is preferably adjusted to a range of pH 1 to 3 for an acidic protease such as pepsin, and to a range of pH 5 to 8 for a neutral protease such as papain. The pH is generally conveniently adjusted appropriately with a buffer such as an ammonium acetate / ammonia buffer or a phosphate buffer. Reaction temperature is 30 ~
45 ° C. is desirable, and the reaction time is generally 3 to 24.
Time is appropriate. In the hydrolysis reaction using an enzyme, the molecular weight of the hydrolyzate is greatly affected by the amount of the enzyme used, the reaction temperature, and the reaction time. Therefore, in order to obtain a keratin hydrolyzate having a target molecular weight, the molecular weight distribution of the obtained hydrolyzate was examined by a gel filtration method for each of the conditions of the amount of the enzyme used, the reaction temperature, and the reaction time. Optimal conditions need to be determined. Enzymatic hydrolysis products include acids,
Compared to an alkali hydrolyzate, it has a narrower molecular weight distribution and produces less free amino acid, and thus is suitable for use in cosmetic formulations.

The average molecular weight of the hydrolyzate obtained by these hydrolysis reactions is preferably 200 or more and 5000 or less. The adsorptivity of the keratin hydrolyzate to hair is determined by its molecular weight. A substance having a molecular weight of about 1000 is most likely to be adsorbed, and a substance having a molecular weight exceeding 5,000 is hardly adsorbed. In addition, it is preferable that as many disulfide bonds as possible remain in the keratin substance-decomposing derivative. For this purpose, it is necessary to use a keratin substance having high purity and to carry out the hydrolysis reaction under mild conditions.

(2) Oxidative degradation reaction Oxidation of keratin is carried out by various methods known per se [NHLeon; Tex
tile Progress, Vol. 7, page 1 (1975)]. As the oxidizing agent, a disulfide bond (S
-S bond) is preferably an organic or inorganic oxidizing agent which acts electrophilically, for example, organic peracids, inorganic peroxo acids or salts thereof, permanganic acids or salts thereof, chromic acids or related compounds. , Halogens, peroxides, oxyacids or salts thereof, and organic peracids such as peracetic acid, formic acid and perbenzoic acid are particularly preferred.

The oxidizing reaction is carried out in a liquid medium by using an excess amount of the oxidizing agent relative to the disulfide bond in the keratin substance, usually at least 2 times equivalent, preferably 4 to 10 times equivalent relative to one disulfide bond. Do. The reaction can be carried out under any of acidic or alkaline conditions, but is preferably carried out under acidic conditions, particularly weakly acidic conditions. Conditions such as reaction temperature and pressure are as follows:
The oxidizing agent to be used depends on the kind of the keratin substance, etc., and is not particularly limited. The temperature is generally room temperature, but it can be heated as needed, and the pressure is normal pressure. It may be performed under pressure or under pressure. When thus, disulfide bonds keratin materials is cleaved to generate a sulfonic acid (-SO ₃ H).

(3) Reductive decomposition and chemical modification reaction As the reducing agent used for reducing the keratin substance, one that cleaves a disulfide bond in the structure to give a thiol group (—SH), generally a disulfide Organic or inorganic reducing agents of the type which act nucleophilically on the bond are preferred. Specifically, organic reducing agents such as mercaptoethanol, thioglycolic acid, benzyl mercaptan, 1,4-dithiothreitol, and tributylphosphine;
Inorganic reducing agents such as sulfides such as sodium hydrogen sulfite and metal hydrides such as lithium aluminum hydride are exemplified.

The amount of the reducing agent is generally 2 to 10 times equivalent to the disulfide bond in the keratin substance. The pH of the reaction system is preferably in the range of 2 to 12, and particularly preferably in the range of 6 to 11. If the pH is out of this range, hydrolysis is undesirably caused. Although the reaction temperature is sufficient at room temperature, the reaction time can be shortened by heating. The reaction time usually requires 2 to 3 hours or more. It is also necessary that the thiol groups generated by this reduction are not substantially oxidized, so that it is better to carry out the operation in an inert gas atmosphere.

The keratin substance thus obtained is subjected to a chemical modification of the thiol group of the reductively decomposed product to obtain a derivative thereof (hereinafter referred to as a “keratin substance reduced derivative”).
Examples of the derivative in the thiol group include the following.

--SCH ₂ COOH, --SCH ₂ CH ₂ C
_{OOH, -SCH (CH 2 COOH)} COOH, -SC
_{H (CH 3) CH 2 COOH} , -SCH 2 CH (CH 3) C
_{OOH, -SO 3 H, -SSO 3} H, -SCH 2 CH 2 SO
₃ H,

[0024]

Embedded image

--SCH ₂ CH ₂ CONHC (CH ₃ ) ₂ CH
_{2 SO 3 H, -SCH 2 CH} 2 SO 2 CH 2 COOH. Among _{these, -SCH 2 COOH, -SCH (CH} 2 COO
H) COOH is particularly preferred.

The thiol group can be chemically modified by a method known per se, for example, NHLEON; Textile Progress, Vol. 7, page 1 (1
975), `` Organic Sulfur Compounds '' by Daigemo, published by Kagaku Doujin (1
968) and Masami Oku, "Experimental Course on Polymer Experiments", Vol. 12, Kyoritsu Shuppan (1957). The following are typical methods.

A method utilizing a nucleophilic substitution reaction of an SH group K-SH + RL → KSR + HL (where K is a keratin compound residue, R is a chemical modifying group to be introduced, L is a halogen atom , Represents a leaving atom or group such as an acid residue.) Examples of the compound that reacts by this method include halogen compounds such as iodoacetic acid, bromoacetic acid, and chloroacetic acid.

A method utilizing a nucleophilic addition reaction of a SH group to a carbon-carbon double bond

[0029]

Embedded image K-SH + (R ¹ ) (R ² ) C = C (R ³ ) (R ⁴ ) → K−S
−C (R ¹ ) (R ² ) −C (R ³ ) (R ⁴ ) H

(Wherein at least one of R ¹ , R ² , R ³ and R ⁴ represents a group having a carboxyl group or a sulfonic acid group therein, and the remainder represents an alkyl group or a hydrogen atom. Has the above-mentioned meaning.) Examples of the compound reacted by this method include acrylic acid, methacrylic acid, crotonic acid, maleic acid, fumaric acid, vinyl carboxymethyl sulfonic acid, vinyl sulfonic acid, styrene sulfonic acid, -Acrylamide-
Examples thereof include 2-methylpropanesulfonic acid. Method using substitution reaction between SH group and sulfite compound

[0031]

## STR7 ## K-SH + NaHSO ₃ → K-S-SO ₃ H K-SH + Na ₂ SO ₃ → K-S-SO ₃ H (reaction in air)

(Where K has the meaning described above)

A method for oxidizing an SH group to a sulfonic acid group K-SH → K-SO ₃ H (oxidation reaction) (where K has the above-mentioned meaning) As an oxidizing agent used in this reaction, for example, , Halogens and permanganates.

The alkali salts of oxidative decomposition of keratin substances and reduced derivatives of keratin substances include inorganic alkali metal salts such as sodium and potassium, ammonium salts, ethanolamine, diethanolamine, triethanolamine, 2-amino-2-methylpropanol. And salts with organic bases such as aminomercaptopropanediol, triisopropanolamine, glycine, histidine and arginine. These can be prepared in another system and blended into the hair treatment agent.However, an oxidized decomposition product of a keratin substance or a reduced derivative of a keratin substance and an alkali substance are blended in the hair treatment agent to form a salt in the system. You can also. Examples of the alkali substance in this case include inorganic alkali substances such as sodium hydroxide, potassium hydroxide, sodium carbonate, and potassium carbonate, and ammonia, ethanolamine, diethanolamine, triethanolamine, and 2-amino-2-methyl-1-. Propanol, 2-
Amino-2-methyl-1,3-propanediol, 2-
Examples include organic alkaline substances such as amino-1-butanol, triisopropanolamine, diisopropanolamine, monoisopropanolamine, arginine, histidine, and hydroxylysine, and these include carboxyl groups in oxidized decomposition products of keratin substances or reduced derivatives of keratin substances or It is preferable to add and blend 0.1 to 8 equivalents to the sulfonic acid group. The component (A) thus obtained is used alone or as a mixture of two or more thereof in the hair treatment composition of the present invention.

The preferred amount of the keratin substance-decomposing derivative used in the present invention is 0.05 to 10.0% by weight.
More preferably, the content is 0.1 to 1.0% by weight. When the amount is less than the above range, the effect of imparting gloss and moisture to the hair, protecting the hair, and improving the combability is not sufficiently exhibited, and also, the hair treating agent of the keratin substance-decomposed derivative is not used. This is because, even if the amount of the compound is larger than the above range, no increase in the effect due to the increase in the amount of the compound is observed, and stickiness occurs when the amount of the compound is extremely large.

((B) Silylated peptide) The silylated peptide used in the present invention is represented by the above-mentioned general formula (I) or (II). The silylated peptide represented by the general formula (I) is, for example, a compound represented by the following general formula (III)

[0037]

Embedded image

Wherein R ⁶ , R ⁷ and R ^{8 each} have 1 to 3 carbon atoms.
, An alkoxy group having 1 to 3 carbon atoms, a hydroxyl group or a halogen atom, wherein R ⁶ , R ⁷ and R ⁸ may be the same or different. a represents 1 or 3, and X represents a halogen atom such as Cl, Br, F, and I. A silyl compound represented by the following general formula (IV):

[0039]

Embedded image

[Wherein, R ⁴ represents a residue excluding a terminal amino group of a basic amino acid having an amino group at a terminal of a side chain;
R ⁵ represents an amino acid side chain other than R ⁴ , m is 0 to 200,
n is 0 to 200 and m + n is 1 to 200. And a peptide represented by the following formula:

The silylated peptide represented by the general formula (II) is, for example, a compound represented by the following general formula (V):

[0042]

Embedded image

Wherein R ⁶ , R ⁷ and R ⁸ have 1 to 3 carbon atoms.
, An alkoxy group having 1 to 3 carbon atoms, a hydroxyl group or a halogen atom, wherein R ⁶ , R ⁷ and R ⁸ may be the same or different. a is 1
Or 3 is indicated. And a peptide represented by the above general formula (IV) by a condensation reaction.

(Characteristics of Silylated Peptide) Formula (I)
The silylated peptide represented by the general formula (II) and the silylated peptide represented by the general formula (II) are, as apparent from their chemical structural formulas, respectively. ), And a silyl functional group containing a silicon atom based on the silyl compound represented by formula (IV), and a peptide moiety based on the peptides represented by the general formula (IV). Excellent extensibility, friction reduction, gloss and gloss imparting effects, water repellency imparting effects, etc. of the part, as well as the adsorptive action on the hair of the peptide part, resulting in increased hair volume, firmness, and film formation Can simultaneously exert a protective action, a moisturizing action, and the like. Moreover, since peptides have good adsorptivity to damaged hair, the silylated peptide can adsorb a silyl functional group to the damaged hair, which is difficult to be adsorbed by high-molecular-weight silicone, via the peptide moiety. It can improve the feel of the hair and contribute to the recovery of strength.

Therefore, when a hair treating agent is prepared by blending the silylated peptide, the silylated peptide imparts luster and moisture to the hair, smoothes the hair, and improves the combability of the hair. Prevents split ends and broken hairs and restores the strength of damaged hair.

The silylated peptide represented by the general formula (I) and the silylated peptide represented by the general formula (II) are those in which a low molecular weight silyl functional group is bonded to the peptide portion, Since the hair is adsorbed to the hair by an ordinary peptide adsorption mechanism, the silylated peptide can be reversibly desorbed from the hair by washing with a detergent containing no peptide.

In the silylated peptide represented by the general formula (I) or the silylated peptide represented by the general formula (II),
R ¹ , R ² and R ³ are specified as described above because the silylated peptide represented by the general formula (I) or the silylated peptide represented by the general formula (II) has a water solubility. This is for maintaining good storage stability in a water-soluble hair treating agent. Also, a is specified as 1 or 3 because
When a is 2, the storage stability of the silyl compound represented by the general formula (III) or the silyl compound represented by the general formula (V) is poor. In this case, the proportion of the silyl functional group occupies a small area, and the properties possessed by the silyl functional group cannot be sufficiently exhibited.

(Peptide portion in silylated peptide) In the silylated peptide represented by the general formula (I) or the silylated peptide represented by the general formula (II), R ⁴ has an amino group at a terminal of a side chain. Although it is a residue excluding the terminal amino group of the basic amino acid, examples of the basic amino acid having an amino group at the terminal of the side chain as described above include lysine, arginine, and hydroxyline. Further, R ⁵ represents a side chain of an amino acid other than R ^4, but as such acids, e.g., glutamic acid, aspartic acid, alanine, serine, threonine, valine, methionine, leucine, isoleucine, tyrosine, phenylalanine, proline , Hydroxyproline and the like.

In the silylated peptide represented by the general formula (I) or the silylated peptide represented by the general formula (II),
m is 0 to 200, preferably more than 0 and 50 or less (0
<M ≦ 50), more preferably greater than 0 and 10 or less (0 <m ≦ 10), n is 0 to 200, preferably 1 to 100, more preferably 2 to 40, and m + n is 1 to 200. , Preferably 2-100, more preferably 3
５０50 for the following reason. That is, when m is larger than the above range, the number of silyl functional groups bonded to the amino group of the side chain increases, and the adsorptive action on the original hair of the peptide decreases. When n becomes larger than the above range, the silyl functional group for the peptide moiety becomes larger. When the ratio of the moieties is small, the properties possessed by the silyl functional group moieties cannot be sufficiently exhibited, and when m + n is larger than the above range, the adsorptivity and permeability to hair as a peptide are lower than those of a low molecular weight peptide. In addition, it is easy to aggregate during storage, and storage stability is reduced.

The above-mentioned m, n and m + n are theoretically integers. However, when the peptide portion is a hydrolyzed peptide as described later, the hydrolyzed peptide is obtained as a mixture of those having different molecular weights. Therefore, the measured value is an average value.

The peptides represented by the general formula (IV) include amino acids, peptides, and esters of amino acids or peptides. Examples of the above amino acids include alanine, glycine, valine, leucine, isoleucine, proline, phenylalanine, tyrosine, serine, threonine, methionine, arginine, histidine, lysine, asparagine, aspartic acid, glutamine, glutamic acid, cystine, cysteine, cysteic acid, Tryptophan, hydroxyproline, hydroxylysine, O-
Examples include phosphoserine and citrulline.

The above peptides include natural peptides, synthetic peptides, hydrolyzed peptides obtained by partially hydrolyzing proteins (proteins) with acids, alkalis or enzymes. Examples of the natural peptide include glutathione, bacitracin A, insulin, glucagon, oxytocin, vasopressin, and the like, and examples of the synthetic peptide include polyglycine, polylysine, polyglutamic acid, and polyserine. Examples of the hydrolyzed peptide include collagen (including gelatin as a denatured product thereof), keratin, silk fibroin, sericin,
Egg yolk protein, egg white protein, egg white protein, egg protein such as casein, conchiolin, elastin, chicken and duck, soy protein, wheat protein, corn protein, rice (rice bran) protein, potato protein and other animal and plant-derived proteins,
Alternatively, yeast proteins of the genera Saccharomyces, Candita and Endomycopsis, yeast proteins decomposed from so-called beer yeasts, sake yeasts, proteins extracted from mushrooms (basidiomycetes), proteins isolated from chlorella, and the like. Peptides obtained by partially hydrolyzing a protein derived from a microorganism with an acid, an alkali or an enzyme are exemplified. As the ester of the amino acid or peptide, an ester with a hydrocarbon alcohol having 1 to 20 carbon atoms in the carboxyl group of the amino acid or peptide, for example, methyl ester, ethyl ester, propyl ester, isopropyl ester, lauryl ester, cetyl ester, 2-ethylhexyl ester, 2
-Hexyldecyl ester, stearyl ester and the like.

(Synthesis of Silylated Peptide) The silylated peptide represented by the general formulas (I) and (II) is a compound represented by the general formula (III) or the general formula (V). Is obtained by contacting a silyl compound represented by the general formula (IV) with a peptide represented by the general formula (IV). The silyl compound represented by the general formula (III) or the compound represented by the general formula (V) As the silyl compound to be used, those commercially available as silane coupling agents can be used.
Examples of such a silane coupling agent include TSL8390 and TSL821 manufactured by Toshiba Silicone Co., Ltd.
9, TSL8395, TSL8326, TSL832
5, TSL8320, TSL8355, TSL8350
(Both are trade names), SH60 manufactured by Nippon Unicar Co., Ltd.
40, SH6076 (all trade names), KMB403, KMB402, KMB70 manufactured by Shin-Etsu Silicone Co., Ltd.
3 (all are trade names).

The reaction between the silyl compound represented by the general formula (III) or the silyl compound represented by the general formula (V) and the peptide represented by the general formula (IV) is carried out by, for example, The compound is stirred and hydrolyzed in water at 30 to 50 ° C. for 5 to 20 minutes to convert an alkoxy group or a halogen atom bonded to a silicon atom into a hydroxyl group.
This is carried out by dropping the hydroxylated silyl compound into a solution of the peptide represented by the general formula (IV) and bringing them into contact with each other. In the above reaction, 30 kinds of peptides were used.
It is preferable to prepare an aqueous solution of about 50% by weight, and the dropping of the hydroxylated silyl compound is preferably completed in 30 minutes to 5 hours.

In the case of using the silyl compound represented by the general formula (III), during the reaction, hydrogen halide is generated by the reaction and the pH after the reaction is lowered. PH of the reaction system is adjusted to 8 to 11, particularly 9 to 10
Is preferably maintained. When the silyl compound represented by the general formula (V) is used, the pH does not decrease due to the reaction, but since the reaction proceeds in a basic manner, the pH of the peptide solution is adjusted to 8 to 11, particularly 9 to 10. It is preferably set to 10. The reaction proceeds at room temperature, but the higher the temperature, the faster the reaction rate. However, when the temperature is increased in a state where the pH is high, the hydrolysis of the silyl compound is promoted. Therefore, the temperature is preferably set to 70 ° C. or less at most, particularly preferably at 40 to 60 ° C. The progress and completion of the reaction can be confirmed by measuring the amount of amino nitrogen in the peptides during the reaction by the Van Slyke method. After completion of the reaction, the reaction solution is neutralized, concentrated as appropriate, purified by ion exchange resin, dialysis membrane, electrodialysis, gel filtration, ultrafiltration, etc., and left as a liquid or powdered hair cosmetic Is prepared.

In the silylated peptide represented by the general formula (I), the introduction ratio of a silyl functional group (that is, a functional group containing only one silicon atom) to the amino group of the peptide is 50% or more and 85% or more. The following is preferred. When the introduction ratio of the silyl functional group is less than 50%, the properties based on the silyl compound may not be sufficiently exhibited.
If it exceeds 5%, the hydrophobicity may increase and the hydrophilicity may decrease. In the silylated peptide represented by the general formula (II), the introduction ratio of the silyl functional group to the amino group of the peptide is preferably 50% or more and 75% or less. When the introduction ratio of the silyl functional group is less than 50%, the properties based on the silyl compound may not be sufficiently exhibited,
If it exceeds 75%, the hydrophobicity may increase and the hydrophilicity may decrease.

The silylated peptide of the present invention is described in detail in, for example, JP-A-9-52821, JP-A-8-81338, JP-A-8-157340, and the like.

The amount of the silylated peptide represented by the general formula (I) or the silylated peptide represented by the general formula (II) in the hair treatment agent (content in the hair treatment agent) is as follows.
0.05 to 30.0% by weight is preferable, and in particular, 0.5 to
15.0% by weight is more preferred. That is, when the amount of the silylated peptide in the hair treating agent is less than the above range, the hair is given gloss or moisture, or the hair is protected, combability is improved, or the polymer silicone is used. The effect of improving the emulsification stability is not sufficiently exhibited, and even if the amount of the silylated peptide in the hair cosmetic is increased, the effect of the increase in the amount is not increased. If the amount is extremely large, stickiness will be caused. Then, when compounding into a hair treatment agent, the silylated peptide may be used alone,
Two or more kinds may be used as a mixture.

In the hair treatment composition of the present invention, the compounding ratio of the keratin substance-decomposed derivative to the silylated peptide is preferably 0.1 to 10.0 parts by weight, more preferably 0.1 to 10.0 parts by weight, per 1 part by weight of the keratin substance-decomposed derivative. Is 0.5 to 3.0
It is desirable to use parts by weight.

The hair treatment composition of the present invention contains, in addition to the above essential constituents, liquid paraffin, squalane, a lanolin derivative, and the like, within a quantitative and qualitative range that does not impair the effects of the present invention depending on the purpose. Higher alcohols, various ester oils, avocado oil, palm oil, tallow, jojoba oil, silicone oil, polyalkylene glycol polyethers and their carboxylic acid oligoester compounds, oils such as terpene hydrocarbon oils, ethylene glycol, propylene glycol, Water-soluble polyhydric alcohols such as 3,3-butylene glycol, glycerin, sorbitol, polyethylene glycol, etc., humectants such as hyaluronic acid, chondroitin sulfate, pyrrolidone carboxylate, ultraviolet absorbers, ultraviolet scattering agents, acrylic resins, silicone resins And resins such as polyvinylpyrrolidone Soybean protein, gelatin, collagen, silk fibroin, protein or protein hydrolyzate, such as elastin, ethyl paraben, preservatives such as butyl paraben, various amino acids, biotin, activators such as pantothenic acid derivatives, .gamma.-oryzanol, sodium dextran sulfate,
Blood circulation promoters such as vitamin E derivatives and nicotinic acid derivatives,
Antiseborrheic agents such as sulfur and thianthol, diluents such as ethanol, isopropanol and tetrachlorodifluoroethane, thickeners such as carboxyvinyl polymers, drugs, fragrances, coloring agents and the like may be appropriately compounded as necessary.

In particular, when the hair treatment agent is a cleaning agent, a cationic polymer substance incorporated for the purpose of improving usability, for example, a cation-modified cellulose ether derivative (trade name: Polymer JR (UCC)) Co., Ltd.), a quaternary ammonium polyvinylpyrrolidone derivative (trade name: Guffcoat (manufactured by GAF), etc.), and a polymer of diallyldimethylammonium chloride (trade name: Mercoat (Merc)
k), polyacrylic acid derivative quaternary ammonium (trade name: Cartex (National Star))
ch)), polyoxyethylene polyalkylene polyamine (trade name: Polycoat (manufactured by HENKEL))
) Is added in an amount that does not impair the effect of the present invention (to the extent that it does not cause stiffness or hair fly), the effect of imparting smoothness when rinsing the detergent is added to the effect of the present invention and is synergistic. To improve.

The hair treatment composition of the present invention may be in the form of an aqueous solution, an ethanol solution, an emulsion, a suspension, or a gel, and may be a shampoo, a hair rinse, a hair treatment, a pre-shampoo, a hair spray, or a hair brushing. It can be in the form of well-known hair treatment agents such as agents, hair setting agents, hair liquids, and hair tonics.

[0063]

Next, the present invention will be described with reference to examples. The present invention is not limited by these. All amounts are by weight. Prior to the examples, a method for synthesizing the keratin substance-decomposed derivative and silylated peptide of the present invention will be described.

1. Synthesis of Keratin Decomposition Derivative Synthesis Example 1-1 (Synthesis of Oxidation Decomposition Derivative of Keratin Substance) (a) 10 g of wool fiber is immersed in 700 g of an 8% aqueous solution of peracetic acid for 1 day at room temperature to cause an oxidation reaction. Was. The obtained oxidized wool was filtered, washed with water, and immersed in 700 g of 0.1 N ammonia water at room temperature for one day, so that about 90 g of wool was solubilized in the ammonia water. About 1 g of the insoluble portion was removed by filtration, and 2N hydrochloric acid was added to an aqueous ammonia solution of keratose, which was an oxidatively decomposed product of wool keratin, to obtain a pH 4.0 solution.
When it was set to 0, α-keratose was precipitated as a precipitate. This is filtered, washed with acetone and dried.
4 g of α-keratose were obtained.

(B) Wool fibers were weighed at 6 kg /
After heating under pressure for 6 minutes with saturated steam of cm ^2, the mixture was rapidly released into the atmosphere to obtain a porous expanded product. 10 g of the pulverized product, 250 g of formic acid, 30% hydrogen peroxide aqueous solution 5
0 g into a 500 ml three-necked flask,
Dipped for a day. At this time, there was no powder form, and a foamy lump was floating in the upper layer. The reaction mixture was filtered, the filtrate was poured into 1.5 l of water and adjusted to pH 4 with hydrochloric acid. The deposited precipitate was collected by filtration and washed with 500 ml of water to obtain 4.5 g of α-keratose. Further, 350 ml of water was added to the insoluble portion where the reaction product was collected by filtration, adjusted to pH 11 with aqueous ammonia, and immersed at room temperature for 1 day. This was filtered, hydrochloric acid was added to the filtrate to adjust the pH to 4, and the deposited precipitate was collected by filtration to obtain 0.7 g of α-keratose. 1.4 g of the insoluble portion was mainly β-keratose.

Synthesis Example 1-2 (Synthesis of Reductive Decomposition Derivative of Keratin Substance) (a) 10 g of wool fiber was immersed in 600 ml of an aqueous solution of 8 M urea and 0.01 M Tris buffer, and 6 ml of 2- After adding mercaptoethanol, 5N
The pH was adjusted to 10 with an aqueous potassium hydroxide solution, and a reduction reaction was performed at room temperature under a nitrogen stream. After about 3 hours, the wool was solubilized in the reaction by about 85%. Then, while adjusting the pH of the system with a 5N aqueous solution of potassium hydroxide so as not to become 7 or less, 16.5% g of iodoacetic acid was gradually added to finally adjust the pH of the system to 8.5, and the carboxymethylation reaction was carried out. Performed at room temperature for 2 hours. The reaction solution was filtered to remove insoluble portions, the obtained filtrate was placed in a cellulose tube, and dialyzed against ion-exchanged water to remove low molecular impurities such as urea.
As urea is dialyzed, HGT (a component having a high content of glycine and tyrosine), which is a water-insoluble component, precipitates in the cellulose tube and becomes cloudy. After completion of the dialysis, HGT is removed by centrifugation, and SCMKA becomes insoluble by isoelectric point precipitation from the resulting neutral transparent aqueous solution of S-carboxymethyl keratin (SCMKA), and precipitates as a precipitate. This was separated by filtration, washed with ethanol and dried to obtain 4.2 g of SCMKA.

(B) In Synthesis Example 1-2 (a), feathers were used instead of wool fibers in a high pressure vessel at 6 kg / cm ² ,
Synthetic Example 1-2 (except that after heating with superheated steam at 40 ° C. for 6 minutes, a porous expanded product obtained by rapid release into the atmosphere was used, and 17.5 g of maleic acid was used instead of iodoacetic acid). By the same operation as in b), 5.3 g of S-
(1,2-Dicarboxyethyl) -keratin was obtained.

(C) Synthesis Example 1-2 Synthesis Example 1 was the same as Example 1 (a) except that ground horse hooves were used instead of wool fibers and 11 g of acrylic acid was used instead of iodoacetic acid.
4.2 g of S- (2-
(Carboxyethyl) -keratin was obtained.

(D) 4.8 g by the same operation as in Synthesis Example 1-2 (A) except that 28 g of styrenesulfonic acid was used instead of iodoacetic acid in Synthesis Example 1-2 (A).
Of S- (sulfophenylvinyl) -keratin was obtained.

(E) 8 g of wool fiber was added to n-propanol 3
00 ml and 300 ml of 0.1 N Tris buffer, and after purging with nitrogen, tri-n-butylphosphine 3.2
Then, the mixture was stirred at room temperature for 24 hours. After this was collected by filtration, 400 ml of water, 9.28 g of maleic acid and about 30 ml of 5N potassium hydroxide were added to the insoluble portion to adjust the pH to 8.0, followed by stirring at room temperature for 6 hours. About 20 ml of a 28% aqueous ammonia solution was added to adjust the pH to 11.5, and the mixture was further stirred at room temperature for 18 hours. The reaction solution was filtered to remove insolubles, and the obtained filtrate was placed in a cellulose tube and dialyzed against ion-exchanged water to remove low molecular impurities.
After completion of the dialysis, the insoluble components in the cellulose tube were removed by centrifugation, the resulting neutral transparent aqueous solution was adjusted to pH 4.4 by adding about 5.5 ml of 1N hydrochloric acid, and the deposited precipitate was collected by filtration and ethanol. After washing and drying, 3.9 g of S-
(1,2-Dicarboxyethyl) -keratin was obtained.

(F) In Synthesis Example 1-2 (e), instead of wool fiber, wool was heated in a high-pressure vessel with 6 kg / cm ² of saturated steam for 6 minutes and then rapidly released into the atmosphere. Synthesis Example 1-2 except that the obtained porous expanded product was pulverized and 16.5 g of 2-acrylamido-2-methylpropanesulfonic acid was used instead of maleic acid.
By the same operation as in (e), 4.5 g of keratin-S-
(2-acrylamido-2-methylpropanesulfonic acid) was obtained.

Synthesis Example 1-3 (Synthesis of Hydrolyzed Derivative of Keratin Substance) (a) 10 g of wool fiber was immersed in 300 g of a 1% aqueous sodium bisulfite solution, and pH was adjusted with a 5N aqueous solution of sodium hydroxide.
Adjusted to 6.7. Furthermore, add 0.2 g of papain,
When the hydrolysis reaction was performed at 60 ° C. for 15 hours, about 80% of wool was solubilized. By removing the insolubles by filtration, the sulfite in the obtained filtrate was removed by ultrafiltration using a membrane having a molecular weight cut off of 500, and the aqueous hydrolyzate solution was concentrated and freeze-dried. , Molecular weight 500-
7.7 g of 2000 hydrolysates were obtained.

(B) 10 g of wool fiber was immersed in 300 g of a 75% phosphoric acid aqueous solution, and a hydrolysis reaction was carried out at 120 to 130 ° C. for 5 hours. After cooling, the insoluble portion was removed by filtration, 4 to 5 times the amount of water was added, and the insoluble portion was further removed by centrifugation. Next, after adding calcium carbonate or barium hydroxide to adjust the pH to 6.7, the precipitate is collected by filtration and dried to obtain a molecular weight of 500 to 200.
8.0 g of the hydrolyzate of the formula (1) were obtained. (Note) According to the production method of the above Synthesis Example 1-3 (a) or 1-3 (b), the amount of SS bond during hydrolysis is 50 mol per 105 g of the hydrolyzate, and It can be seen that cystine has not been destroyed.

(C) 100 g of feathers are placed in a high-pressure vessel at 6 kg.
After pressurized and heated with superheated steam at 240 ° C./cm ² for 6 minutes, the mixture was rapidly released into the atmosphere to obtain a porous expanded product. After the pulverized product was pulverized, 3 l of 0.3N caustic soda was added, a hydrolysis reaction was performed at 60 ° C. for 18 hours, and then neutralized with 1N hydrochloric acid, and the reaction solution was filtered. The salt in the obtained filtrate was removed by an ultrafiltration method using a membrane having a molecular weight cut off of 500, and the aqueous solution of keratin hydrolyzate was concentrated and lyophilized to give a keratin hydrolyzate 7.2.
g was obtained. Its molecular weight was 1,800 as measured by gel filtration.

(D) A ground horse hooves having a particle size of 0.25
100 g of the mixture adjusted to １1 mm was degreased with a 50% methanol / 50% chloroform solution, and then the soluble protein was removed with 1% ammonia water. Then, the mixture was transferred to a three-necked flask, and 20 g of sodium hydroxide and 400 g of ion-exchanged water were added. In addition, a hydrolysis reaction was performed at a temperature of 90 ° C. for 4 hours with stirring. After cooling, the pH was adjusted to 8 with hydrochloric acid, and the reaction solution was filtered. After the operation of removing the salt from the filtrate, 68 g of a keratin hydrolyzate was obtained in the same manner as in Synthesis Example 1-3 (c). The molecular weight of this product measured by gel filtration was 2,500.

2. Synthesis of Silylated Peptide Synthesis Example 2-1 Hydrolyzed Collagen (A hydrolyzate of collagen. In general formula (IV), average value of m = 2, average value of n = 1
8, average value of m + n = 20) A 20% aqueous sodium hydroxide solution was added dropwise to 50 g of a 30% aqueous solution (10.6 mmol as a stoichiometric mole obtained by measurement of amino nitrogen) to adjust the pH to 9 And heated to 55 ° C. On the other hand, as a silylating agent, in the general formula (V), R ⁶ =
2.3 g of a silyl compound (1.0 equivalent with respect to the amount of amino nitrogen of hydrolyzed collagen) in a mixture of CH ₃ , R ⁷ ＯOCH ₃ , R ⁸ ＯOCH ₃ and a = 3 is converted to a 15% aqueous solution in water. And adjust the pH to 3.5 with dilute hydrochloric acid.
In continued stirring for 15 minutes to convert the methoxy group (-OCH ₃₎ hydrolyzing the hydroxyl group.

While the above-mentioned hydrolyzed collagen solution was stirred at 55 ° C., an aqueous solution of a silyl compound converted to a hydroxyl group was dropped therein over 30 minutes. After dropping, 55
Stirring was continued at 5 ° C. for another 5 hours to complete the reaction. After the completion of the reaction, the introduction rate of the silyl functional group into the amino nitrogen was determined by measuring the amino nitrogen, and the introduction rate of the silyl functional group was 67%. After neutralizing the reaction solution with dilute hydrochloric acid, desalting with an electrodialysis device, adjusting the pH to 6.5, and concentrating the mixture to adjust the concentration, the concentration of the reaction product (silylated hydrolyzed collagen) is reduced. 63 g of a 20% aqueous solution was obtained.

Synthesis Example 2-2 Hydrolyzed wheat protein (a hydrolyzate of wheat protein,
In the general formula (IV), the average value of m = 1.2, the average value of n = 8.8, and the average value of m + n = 10) 30% aqueous solution 5
A 20% aqueous sodium hydroxide solution was added dropwise to 0 g (15 mmol as a stoichiometric mole obtained by measurement of amino nitrogen) to pH 9.5, and the mixture was heated to 55 ° C.
On the other hand, as a silylating agent, R ⁶ in the general formula (V)
= Cl, R ⁷ = CH ₃ , R ⁸ = Cl, a = 3 silyl compound 3.1 g (0.9 equivalent based on the amount of amino nitrogen of hydrolyzed wheat peptide) becomes a 15% aqueous solution in water. And stirring was continued for 15 minutes to convert Cl atoms directly bonded to silicon atoms into hydroxyl groups. While stirring the hydrolyzed wheat protein aqueous solution at 55 ° C., an aqueous solution of a silyl compound converted to a hydroxyl group was dropped therein over 1 hour. After completion of the dropwise addition, stirring was continued at 55 ° C. for further 5 hours to complete the reaction. After neutralizing the reaction solution with dilute hydrochloric acid, desalting by electrodialysis, concentration and concentration adjustment, the reaction product (silylated hydrolyzed wheat protein) concentration is 20%.
55 g of an aqueous solution of was obtained. Introduction rate of silyl functional group is 62%
Met.

Synthesis Example 2-3 In place of hydrolyzed collagen, hydrolyzed keratin (hydrolyzate of wool, average value of m in general formula (IV) =
Using 50 g of a 30% aqueous solution (average value of 0.6, n = 4.4, average value of m + n = 5) (42 mmol as a stoichiometric number of moles obtained by measurement of amino nitrogen), using silyl As an agent, in the general formula (V), R ⁶ ＣＨCH ₃ ,
In _{^{R 7 = OC 2 H 5,}} R 8 = OC 2 H 5, a silyl compound of a = 3 (with respect to amino nitrogen of hydrolyzed keratin, 0.8 eq) 75 g except using, Synthesis Example 2 In the same manner as in -1, 58 g of an aqueous solution having a reaction product (silylated hydrolyzed keratin) concentration of 20% was obtained. The introduction ratio of the silyl functional group was 59%, and in the silyl compound represented by the general formula (V), the ethoxy group (OC ₂ H ₅ ) directly bonded to the silicon atom became a hydroxyl group during the above reaction. Had been converted to.

Synthesis Example 2-4 In place of hydrolyzed collagen, hydrolyzed soybean protein (a hydrolyzate of soybean protein. In general formula (IV), average value of m = 0.5, average value of n = 5) .5, m + n
(Average value of 6) 50% of a 30% aqueous solution (stoichiometric number of moles obtained by measurement of amino nitrogen);
4 mmol) as a silylating agent using the general formula (V)
Wherein R ⁶ OCH ₃ , R ⁷ ＯOCH ₃ , R ⁸ ＯOCH
₃ , the reaction product was obtained in the same manner as in Synthesis Example 2-1 except that 3.4 g of the silyl compound of a = 1 (0.9 equivalents based on the amount of amino nitrogen of the hydrolyzed soybean protein) was used. (Silylated hydrolyzed soy protein) Aqueous solution 5 with 20% concentration
3 g were obtained. The introduction rate of the silyl functional group was 60%, and in the silyl compound represented by the general formula (V), the methoxy group directly bonded to the silicon atom was converted to a hydroxyl group during the above reaction.

Synthesis Example 2-5 In place of hydrolyzed collagen, hydrolyzed yeast protein (a hydrolyzate of yeast protein, in general formula (IV), average value of m = 1.2, average value of n = 6) .8, m + n
(Average value = 8) of a 30% aqueous solution (30 mmol as a stoichiometric mole obtained by measurement of amino nitrogen), and as a silylating agent, R ⁶ ＣＨCH in general formula (V) ₃ , R ⁷ = OC ₂ H ₅ , R ⁸ = OC ₂ H ₅ ,
The reaction product (silylation) was carried out in the same manner as in Synthesis Example 2-1 except that 5.3 g of the silyl compound of a = 3 (0.8 equivalents to the amount of amino nitrogen in the hydrolyzed yeast protein) was used. 48 g of an aqueous solution having a hydrolyzing yeast protein) concentration of 20% was obtained. The introduction ratio of the silyl functional group was 57%, and in the silyl compound represented by the general formula (V), the ethoxy group directly bonded to the silicon atom was replaced with a hydroxyl group during the above reaction.

Synthesis Example 2-6 10 g of L-lysine hydrochloride (molecular weight: 182.6, 54.7)
(Mmol) was dissolved in 100 ml of water, a 20% aqueous sodium hydroxide solution was added dropwise to adjust the pH to 9.5, and the mixture was heated to 55 ° C. On the other hand, as a silylating agent, in the general formula (V), R ⁶ ＯOCH ₃ , R ⁷ ＯOCH ₃ , and R ⁸ ＯOCH ₃
Then, 17.8 g (0.7 equivalents based on the amount of amino nitrogen of L-lysine hydrochloride) of the silyl compound having a = 3 was added to 15% of water in water.
The solution was dissolved in an aqueous solution, the pH was adjusted to 3.5 with dilute hydrochloric acid, stirring was continued at 50 ° C. for 15 minutes, and the methoxy group was hydrolyzed to be converted to a hydroxyl group. While stirring the L-lysine hydrochloride aqueous solution, an aqueous solution of a silyl compound converted to a hydroxyl group was dropped into the aqueous solution over 30 minutes. After completion of the dropwise addition, stirring was continued at 55 ° C. for further 5 hours to complete the reaction.

After completion of the reaction, the introduction rate of the silyl functional group was determined by measuring the amount of amino nitrogen, and the introduction rate of the silyl functional group was 65%. It was found that the amino group of the chain was also reacted. After neutralizing the reaction solution with dilute hydrochloric acid, desalting and purification with an electrodialysis device, adjusting the pH to 6.5, and concentrating the mixture to adjust the concentration, the concentration of the reaction product (silylated L-lysine) is increased. 118 g of a 15% aqueous solution was obtained.

Synthesis Example 2-7 Glycyl-L-alanine 1 was used instead of L-lysine hydrochloride
0 g (molecular weight 146.1, 68.4 mmol)
As a silylating agent, in the general formula (V), R ⁶ ＣC
H ₃ , R ⁷ ＣＨOCH ₃ , R ^{8 、} OCH ₃ , and 13.5 g of a silyl compound having a = 1 (0.9 equivalents based on the amount of amino nitrogen of glycyl-L-alanine) was used. In the same manner as in Synthesis Example 2-6, 104 g of an aqueous solution having a reaction product (silylated glycyl-L-alanine) concentration of 15% was obtained. The introduction ratio of the silyl functional group was 55%, and in the silyl compound represented by the general formula (V), the methoxy group directly bonded to the silicon atom was converted to a hydroxyl group during the above reaction.

A. Examples as Hair Restorative Example 1 (Treatment Lotion)% by weight (1) 1,3-butylene glycol 2.0 (2) Glycerin 1.0 (3) Stearyltrimethylammonium chloride 0.5 (4) Methylphenyl polysiloxane 1.0 (5) Derivative of keratin substance of Synthesis Example 1-1 (a) 1.0 (6) Silylated peptide of Synthesis Example 2-1 1.0 (7) Perfume Appropriate amount (8) Ultraviolet rays Appropriate amount of inhibitor (9) Preservative Appropriate amount (10) Ethanol 50.0 (11) Ion-exchanged water 43.5 <Production method> (5) to (11) are dissolved by stirring, and then (1) to
(4) is added sequentially.

Example 2 (treatment mousse)% by weight (1) Light liquid isoparaffin (C12 to C15) 22.0 (2) Dimethylpolysiloxane (20cs) 3.0 (3) Propylene glycol 6.0 (4) Poly Oxyethylene (80 mol) hydrogenated castor oil ester 2.0 (5) Cationized cellulose 0.2 [Product name: Polymer JR-400, manufactured by Union Carbide Co.] (6) Keratin substance of Synthesis Example 1-2 (e) Decomposed derivative 4.0 (7) Silylated peptide of Synthesis Example 2-2 6.0 (8) Deionized water 46.8 (9) Liquefied petroleum gas (LPG) 10.0 <Production method> (3), (4) The mixture of (1) and (2) is added to the mixture of (1) and emulsified. To this, the solutions (5) to (8) are added and mixed and stirred to obtain a stock solution. This stock solution is filled into an aerosol can,
Next, the propellant gas of (9) was filled to obtain an aerosol-type hair damage preventive / restorative agent.

Comparative Example 1 (treatment lotion)% by weight (1) 1,3-butylene glycol 2.0 (2) glycerin 1.0 (3) stearyltrimethylammonium chloride 0.5 (4) methylphenylpolysiloxane 0 (5) Collagen hydrolyzate 1.0 (6) Perfume proper amount (7) UV inhibitor proper amount (8) Preservative proper amount (9) Ethanol 50.0 (10) ion exchange water 44.5 <Production method> (5 )-(10) were dissolved by stirring, and then (1)-
(4) is added sequentially.

Comparative Example 2 (Treatment mousse)% by weight (1) Light liquid isoparaffin (C12 to C15) 0 (2) Dimethylpolysiloxane (20 MPa) 3.0 (3) Propylene glycol 6.0 (4) Polyoxyethylene (80 mol) hydrogenated castor oil ester 2.0 (5) Cationized cellulose 0.2 [Product name] : Polymer JR-400, manufactured by Union Carbide Co.) (6) Synthesis Example 1-2 Decomposition derivative of keratin substance of (e) 4.0 (7) Water-soluble elastin 6.0 (8) Deionized water 46.8 (9) ) Liquefied petroleum gas (LPG) 10.0 <Production method> A mixed solution of (1) and (2) is added to a mixture of (3) and (4) and emulsified. To this, the solutions (5) to (8) are added and mixed and stirred to obtain a stock solution. This stock solution is filled into an aerosol can,
Next, the propellant gas of (9) was filled to obtain an aerosol-type hair damage preventive / restorative agent.

Test Example 1 Measurement of Hair Smoothness A hair bundle was made from damaged hair collected from the same person, and the samples of Examples 1 and 2 and Comparative Examples 1 and 2 were applied to each hair bundle, and friction was measured. The coefficient of friction of the hair was measured with an instrument.
Thereafter, each of the hair tresses was washed twice with shampoo, sufficiently washed with water, and dried with a drier, and the friction coefficient of the hair was measured. Table 1 shows the results.

[0090]

[Table 1] 摩擦 Friction coefficient immediately after sample application Friction coefficient after shampoo ── ─────────────────────────────── Example 1 0.15 0.20 Example 2 0.20 0.25 Comparison Example 1 0.30 0.45 Comparative Example 2 0.25 0.35 Uncoated 0.45 0.45 ────────

From the results shown in Table 1, it can be seen that the use of the product of the present invention significantly reduced the coefficient of friction and maintained the smoothness of the hair after shampooing.

Test Example 2 Measurement of Effect of Preventing Split Hair Generation A hair bundle was prepared from healthy head hair collected from the same person, and the samples of Examples 1 and 2 and Comparative Examples 1 and 2 were applied to each hair bundle. The number of split ends generated when brushing was applied 10,000 times was counted. Each hair bundle consists of 1300 hairs. Table 2 shows the results.

[0093]

[Table 2] 試 料 Sample number of split ends generated ──────────────── Example 1 20 Example 2 50 Comparison Example 1 200 Comparative Example 2 100 Uncoated 300 ────────────────

From the results shown in Table 2, it can be seen that the product of the present invention has a remarkable effect in preventing the generation of split ends.

Test Example 3 Measurement of Splitting Hair Repair Effect Four treatment panels having many split hairs were used with the treatment lotion of Example 1, and the split hair repairing effect was observed. As a result, in each of the panels, the split ends became inconspicuous, and the repair effect of the product of the present invention was confirmed.

Example 3 (hair blow)% by weight (1) Decamethylcyclopentasiloxane 5.0 (2) Ammonium-modified high-molecular silicone (molecular weight 500,000) 1.0 (3) 1,3-butylene glycol 2.0 (4) Polyoxyethylene (60 mol) hydrogenated castor oil ester 2.0 (5) Ethanol 15.0 (6) Silylated peptide of Synthesis Example 2-3 5.0 (7) Synthesis Example 1-3 (b) Keratin substance decomposition derivative of 5.0 (8) Ion-exchanged water 65.0 (9) Perfume Appropriate amount <Production method> Dissolve (2) in (1), add to mixture of (3), (4), emulsify And mix with (5)-(9). The hair was blown into a dispenser container and sprayed on the hair in a mist.

Example 4 (Hair Foam) Weight% (1) Decamethylcyclopentasiloxane (6 Mpa · s) 20.0 (2) Dimethylpolysiloxane 5.0 (3) Dipropylene glycol 5.0 (4) Poly Oxyethylene-modified dimethylpolysiloxane 3.0 [trade name: SILWET 10-E, manufactured by Nippon Unicar Co., Ltd.] (5) Ethanol 10.0 (6) Deionized water 43.0 (7) Synthesis Example 2-4 4.0 (8) Keratin substance-decomposed derivative of Synthesis Example 1-3 (a) 4.0 (9) Perfume (10) Butane 4.0 (11) Dimethyl ether 2.0 <Production method> (1 ) Is dissolved in (2), and added to the mixture of (3) and (4) to emulsify. The emulsified product is added to a solution obtained by mixing (5) to (9), put in an aerosol solution, attached with a valve, and then filled with (10) and (11).

Example 5 (Hair Cream) Weight% (1) Isoparaffin 10.0 [trade name: Isosol 400, manufactured by Nippon Petrochemical Co., Ltd.] (2) Jojoba oil 3.0 (3) Dimethylpolysiloxane ( 5.0 (4) Glycerin tri-2-ethylhexanoate 8.0 (5) Vaseline 5.0 (6) Stearyl alcohol 2.0 (7) Sorbitan monooleate 2.0 (20 MPa · S / 25 ° C) 8) Polyoxyethylene (40 mol) hydrogenated castor oil ester 2.0 (9) Glycerin 5.0 (10) Hyaluronic acid 5.0 (11) Methylparaben proper amount (12) Ion exchange water 49.0 (13) Synthesis example 2-5 Silylated peptide 1.0 (14) Synthetic Example 1-2 Keratin substance-decomposed derivative of (b) 3.0 <Production method> (1) to (8) were stirred and dissolved at 70 ° C., and (9) (14) is added to the dissolved substance and emulsified to obtain a hair cream.

Example 6 (treatment lotion)% by weight (1) Isoparaffin 15.0 [trade name: Shellsol 71, manufactured by Shell Co.] (2) High molecular weight dimethylpolysiloxane (molecular weight 500,000) 3.0 (3) 1,3-butylene glycol 2.0 (4) Polyoxyethylene (60 mol) hydrogenated castor oil ester 2.0 (5) Silylated peptide of Synthesis Example 2-6 10.0 (6) Synthesis Example 1-1 ( Keratin substance-decomposing derivative of b) 3.0 (7) Ethanol 15.0 (8) Ion-exchanged water 50.0 (9) Perfume qs <Production method> Dissolve (2) in (1), (3), (3) The mixture was emulsified by adding to the mixture of 4), and the emulsified matter was added to and dissolved in the dissolution materials of (5) to (9) to obtain a treatment lotion.

B. Examples as Hair Rinse Effect Agents Examples 7 to 12, Comparative Examples 3 to 6 Hair rinses were prepared according to the usual methods using the compositions shown in Tables 3 and 4. Tables 3 and 4 also show the results of the evaluation of each preparation by the following methods.

(1) Hair protection effect 1 g of each sample was applied to a bundle of 500 to 600 hairs of 15 cm in length, and the hair was rinsed and shaken (100 cycles) twice in 300 ml of warm water at 40 ° C. Dry the bundle. The number of split ends and cuts generated after brushing the bundle of hair with a certain force is counted, and the incidence of split ends and cuts relative to the total number of hairs is calculated. The incidence Y% of each sample-treated hair was compared with the incidence X% of split ends and cut hairs of the untreated hair, and evaluated by the value of Y / X as follows.

Y / X <0.5 A (hair protection effect large) 0.5 ≦ Y / X <0.8 B (during hair protection effect) 0.8 ≦ Y / X <1.0 C (Small hair protection effect) 1.0 ≦ Y / X… D (no hair protection effect)

(2) Measurement of Adsorption Amount on Hair 2 g of each sample was applied to 4 g of the hair bundle after complete degreasing, and the hair bundle was shaken and rinsed (100 cycles) twice in warm water (40 ° C.). Allow to dry. The adsorbed material was extracted from each hair bundle by Soxhlet extraction (dichloromethane / methanol = 92/8 vol%, 5 hr extraction), and the amount of sample adsorbed per 1 g of hair was calculated from the weight. The adsorptivity of each sample to hair was evaluated as follows. 30 mg or more A (large adsorbability to hair) 10 mg or more and less than 30 mg B (during adsorbability to hair) Less than 10 mg C (small adsorbability to hair)

(3) Effect of Applying Gloss to Hair 1 g of each sample is applied to a hair bundle of 500 to 600 hairs of 15 cm in length and subjected to shaking and rinsing (100 cycles) twice in 300 ml of warm water at 40 ° C. The hair bundle is dried. Choose 10 hairs arbitrarily from this hair bundle,
The reflected light distribution of the hair with respect to the incident light was measured by a variable-angle photometer GP-IR [manufactured by Murakami Color Research Laboratory Co., Ltd.], and the glossiness (glossy) of the hair was determined by the following equation.

[0105]

G = s / d (G: glossiness, s: specular reflection light amount,
d: diffuse reflection light amount)

Using the gloss G obtained by the above method, the gloss imparting effect of each sample to the hair was evaluated as follows. G is 15 or more A (large gloss effect) G is 10 or more and less than 15 B (during gloss effect) G is 5 or more and less than 10 C (small gloss effect) G is less than 5 D (gloss effect) No effect)

(4) Uniform Coatability The uniform coatability was evaluated from a scanning electron microscope (SEM) photograph of a hair sample prepared in the same manner as in the measurement of gloss of hair. SEM photographs of hair treated with each sample (400-1
SEM of untreated hair by 15 judges
Compared with the photograph, the uniform coating property was evaluated in two stages of “good” and “same degree”. Evaluation was made as follows from the results of the determination. All 15 people answered "good" ... A 8-14 out of 15 people answered "good" ... B Out of 15 people, 7 or less answered "good" ... C

(5) Smoothness after Drying (Sensory Evaluation of Effect on Hair) As test subjects, 15 women aged 19 to 36 years old were selected. Each test subject applied 12 g of each sample to hair after washing with a commercially available hair shampoo (normal alkyl sulfate salt-based shampoo), rinsed with water at about 40 ° C., and then dried with a dryer. The feel of the hair was measured using a control sample (stearyltrimethylammonium chloride 2.0).
%, 3.0% of cetostearyl alcohol, 5.0% of propylene glycol and 90% of water), markedly excellent, "good", "same as" and "poor". It was evaluated on a scale. Evaluation was made as follows from the determination results of the 15 persons. 12 or more answered "significantly good" or "good" ... A 8 to 11 said "significantly good" or "good" ... B 4 to 7 said "significantly good" or "good" ... C 3 or less people answered "Notably good" or "Good" ... D

[0109]

[Table 3] {Example No. 7 8 9 10 11 12} ───────────────────────────────── Silylated peptide (Synthesis Example 2-7) 10.0 10.0 10.0 10.0 10.0 10.0 Chloride Stearyltrimethylammonium 2.0 1.0 0.8 0.5 2.0 2.0 Distearyldimethylammonium chloride-0.5----Cetostearyl alcohol 3.0 3.5 3.0 1.5 4.0 4.0 (C16 / C18 = 7/3) Decomposition derivative of keratin substance 2.0 1.0 1.0 0.2 5.0 2.5 (Synthesis Example 1-1 (A)) High molecular weight dimethylpolysiloxane-----2.5 (Molecular weight 400,000) Dimethylpolysiloxane (5cs) 10.0 10.0 10.0 10.0 5.0-Methylparaben Proper amount Proper amount Proper amount Proper amount Proper amount Proper amount Proper amount Proper amount Proper amount Proper amount Proper amount Flavor appropriate amount appropriate amount appropriate amount appropriate amount appropriate Appropriate amount Deionized water Residue Residual Residue Residual Residual ─────────────────────────────────── Hair protection effect A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A A ────────────────────────────────

[0110]

[Table 4] {Comparative Example No. 3 4 5 6} ───────────────────── Silylated peptide (Synthesis Example 2-7)---10.0 Stearyltrimethylammonium chloride 2.0 1.0 2.0 2.0 Distearyldimethylammonium chloride-- --Cetostearyl alcohol 3.0 2.0 3.0 3.0 (C16 / C18 = 7/3) Decomposition derivative of keratin substance-1.0--(Synthesis example 1-1 (a)) High molecular weight dimethylpolysiloxane 2.0---(Molecular weight 400,000) Dimethyl polysiloxane (5cs) 10.0 10.0 15.0 5.0 Methyl paraben qs qs qs qs qs qs qs qs qs qs perfume qs qs qs qs qs qs ion-exchanged water residue residue residue residue ────────────────── ───────── ── Hair protection effect C C DC C Adsorption to hair B B C B Gloss imparting effect to hair C C DC Uniform coatability C C C C Smoothness after drying B C D D ────── ────────────────────────

As can be seen from Tables 3 and 4, the hair treatment agent of the present invention has a hair protection effect, smoothness after drying, absorptivity to hair, a gloss imparting effect to hair, The coating was excellent.

Example 13 (hair rinse)% by weight (1) Silylated peptide (Synthesis Example 2-1) 3.0 (2) Keratin substance decomposed derivative (Synthesis Example 1-2 (b)) 12.0 (3) Cetyltrimethylammonium chloride 0.6 (4) Cetostearyl alcohol (C16 / C18 = 6/4) 2.0 (5) Dimethylpolysiloxane (100 MPa) 3.0 (6) Cyclic silicon pentamer 15.0 (7) ) Glycerol monostearate 1.0 (8) Stearic acid 0.5 (9) Glycerin 5.0 (10) Propylene glycol 5.0 (11) Yellow-4 No. (dye) Appropriate amount (12) Perfume Appropriate amount (13) Methylparaben proper amount (14) EDTA-3Na (chelating agent) proper amount (15) ion-exchanged water residue <Production method> (1), (2), (7), (9), (10), (11), (13) , (14), (15) were mixed and stirred at 70 ° C., and (3), (4), (5), (6), (7),
A mixture obtained by mixing and stirring (8) and (12) at 70 ° C. was added to obtain a hair rinse. The obtained hair rinse was prepared according to Examples 7 to 12 above.
The evaluation was performed in the same manner as described above. As a result, this hair rinse was excellent in stability, exhibited unprecedented smoothness even in the evaluation of sensory tests, and also provided an excellent protective effect to hair.

Example 14 (Hair treatment cream)% by weight (1) Behenyltrimethylammonium chloride 3.0 (2) Cetostearyl alcohol (C16 / C18 = 7/3) 6.5 (3) Behenyl alcohol 2.0 (4) Dimethylpolysiloxane (5cs) 20.0 (5) Liquid paraffin 6.0 (6) 2-octyldodecanol 2.0 (7) Polyoxyethylene hydrogenated castor oil derivative 0.3 (60 moles of ethylene oxide added (8) Polyoxyethylene stearyl ether 1.0 (4 mol ethylene oxide adduct) (9) Silylated peptide of Synthesis Example 2-2 0.5 (10) Glycerin 10.0 (11) Dipropylene glycol 5 0.0 (12) Yellow-4 (dye) proper amount (13) perfume proper amount (14) methyl paraben proper amount (15) EDTA-3Na (chelating agent) proper amount (16) ion exchange water residue (17) synthesis Keratin substance-decomposed derivative of Example 1-3 (a) 0.5 Preparation method> (1), (9) to (12), (14) to (17) were mixed and stirred at 70, and then (2) After mixing (8) and (13) at 70 ° C. and stirring, a hair treatment cream was obtained. The obtained hair treatment cream was used in Examples 7 to 12 described above.
The evaluation was performed in the same manner as described above. As a result, this hair treatment cream gave excellent smoothness, especially to damaged hair, and had a good hair protection effect.

[0114]

As described above, the hair treatment composition of the present invention imparts rich gloss and smoothness to hair,
It is a hair treatment agent having an effect of preventing damage to hair such as cut hair and repairing generated split ends to make them less noticeable. When the hair treatment agent of the present invention is used as a hair rinse, a hair treatment, and a hair rinse effect agent containing a rinsing step with a hair pack, the hair is not sticky and can impart excellent smoothness and luster to the hair. And a hair treating agent having a high effect of protecting the hair from physical stimuli such as brushing.

Claims (2)

[Claims] 1. A hair treatment agent comprising the following (A) and (B): (A) one or two keratin substance-decomposing derivatives selected from the group consisting of a hydrolyzate of a keratin substance, an alkali salt of an oxidative decomposition product of a keratin substance, and an alkali salt of a derivative at a thiol group of a reduction decomposition product of the keratin substance that's all. (B) A silylated peptide in which a functional group containing only one silicon atom is covalently bonded to an amino group of a peptide containing an amino group in an amino acid side chain represented by the following general formula (I) or (II). Embedded image [In the formula, R ¹ , R ² , and R ³ represent an alkyl group having 1 to ³ carbon atoms or a hydroxyl group, and these R ¹ , R ² , and R ³ may be the same or different. R ⁴ represents a residue excluding the terminal amino group of a basic amino acid having an amino group at the terminal of the side chain; R ⁵ represents an amino acid side chain other than R ⁴ ;
a is 1 or 3, m is 0 to 200, n is 0 to 200,
m + n is 1 to 200. (However, m and n only indicate the number of amino acids, and do not indicate the order of the amino acid sequence.)] [In the formula, R ¹ , R ² , and R ³ represent an alkyl group having 1 to ³ carbon atoms or a hydroxyl group, and these R ¹ , R ² , and R ³ may be the same or different. R ⁴ represents a residue excluding a terminal amino group of a basic amino acid having an amino group at a terminal of a side chain, R ⁵ represents an amino acid side chain other than R ⁴ , a represents 1 or 3, and m represents 0 to 0. 200, n is 0-20
0 and m + n are 1 to 200. (However, m and n
Indicates the number of amino acids, but does not indicate the order of the amino acid sequences. )] 2. The compounding amount of one or a mixture of two or more keratin substance-decomposing derivatives is 0.05 to 10.0% by weight.
The hair treatment composition according to claim 1, wherein the amount of the silylated peptide is 0.05 to 30.0% by weight.