JP2002121117A - Formulating agent for cosmetic - Google Patents

Abstract

PROBLEM TO BE SOLVED: To obtain a formulating agent for a cosmetic comprising a copolymer composition having excellent characteristics of both a polypeptide and a silicone compound, provided with characteristics based on a silane compound, forming a strong coating film by heating. SOLUTION: This formulating agent for a cosmetic comprises a silylated peptide-silane compound copolymer composition obtained by subjecting one or more kinds silylated peptides containing two or more hydroxy groups directly bonded to a silicon atom and one or more kinds of silane compounds to produce two or more hydroxy groups directly bonded to a silicon atom by hydrolysis in a composition ratio of 5:1 to 1:1 to condensation polymerization.

Description

DETAILED DESCRIPTION OF THE INVENTION

[0001]

TECHNICAL FIELD The present invention relates to a cosmetic compounding agent comprising a silylated peptide-silane compound copolymer composition, and more particularly to a cosmetic compound comprising a hydroxyl group directly bonded to a silicon atom.
And at least one hydrolyzate of a silane compound that produces two or more hydroxyl groups directly connected to a silicon atom by hydrolysis at a composition ratio of 5:
From a silylated peptide-silane compound copolymer composition obtained by condensation polymerization in an aqueous solution within a range of 1 to 1: 1 and further having properties based on a silane compound added to properties based on the silylated peptide. The present invention relates to a cosmetic compounding agent.

[0002]

2. Description of the Related Art Conventionally, polypeptides and silicone oils (organic silicone compounds) have been blended into cosmetics to sorb the hairs of the polypeptides, alleviate skin irritation, and protect and moisturize the skin by film formation. Attempts have been made to exert the effect of imparting gloss and gloss and water repellency by silicone oil.

[0003] However, silicone oil is originally a hydrophobic (lipophilic) substance, is hardly compatible with hydrophilic polypeptides, and is used in combination with an emulsifier in water-soluble cosmetics. There is a problem that the product lacks stability and its commercial value is easily lost.
When used in cosmetics, it is difficult for the polypeptide to adhere to the parts that first contacted the silicone oil, and conversely, the silicone oil did not easily adhere to the parts that contacted the polypeptide first, so that the properties of both were sufficient. There was a problem that it can not be exhibited in the.

For this reason, polyoxyalkylene-modified silicones having a polyoxyalkylene group introduced for the purpose of imparting hydrophilicity to silicones have been used in water-soluble cosmetics. However, unlike polypeptides, they have no ionic properties. There is a problem that it is difficult to be absorbed on hair and skin.

[0005] In order to solve these problems, the present inventors have prepared a silylated peptide in which an amino group of the peptide is covalently bonded to a functional group containing only one silicon atom in an aqueous solvent ( JP-A-8-59424 and JP-A-8-67608), and can be used as a compounding agent for a cosmetic base material and a fiber treatment agent.

[0006] However, this silylated peptide has good sorption properties to hair and skin, but is inferior to silicone oil in terms of the effect of imparting extensibility and smoothness due to the small number of silyl groups bonded to the peptide chain. There was a problem.

Accordingly, the present inventors have developed a silylated peptide-silane compound copolymer composition obtained by polycondensation of this silylated peptide and a silane compound which produces at least two hydroxyl groups directly bonded to silicon atoms by hydrolysis in an aqueous solution. (JP-A-11-286550, JP-A-200
No. 0-007785), and an improvement in the action of imparting extensibility and smoothness, which are disadvantages of silylated peptides, has been attempted.

[0008] However, this silylated peptide-silane compound copolymer composition is excellent in the action of imparting extensibility and smoothness, but has the problem that it is hardly soluble or insoluble in water and is difficult to be incorporated into transparent cosmetics. Was.

[0009]

SUMMARY OF THE INVENTION Accordingly, the present invention provides a silicone compound which has excellent properties in addition to the excellent properties of a polypeptide, can be incorporated in water-soluble transparent cosmetics, and can be used in an organic solvent. It is an object of the present invention to provide a silylated peptide-silane compound copolymer composition that can be easily produced in an aqueous system without using any of the above as a cosmetic compounding agent.

[0010]

Means for Solving the Problems The inventors of the present invention have conducted intensive studies to solve the above-mentioned problems, and as a result, have been hydrolyzed with one or more silylated peptides having two or more hydroxyl groups directly connected to silicon atoms. Silylated peptide-silane compound copolymer obtained by condensation polymerization of at least one silane compound having two or more hydroxyl groups directly bonded to silicon atoms in an aqueous solution at a composition ratio of 5: 1 to 1: 1 The composition is
This silylated peptide-silane compound copolymer composition has both the properties based on the silylated peptide and the properties based on the silane compound. Further, since the silylated peptide-silane compound copolymer composition has water solubility, it can be blended into a transparent cosmetic. The compound copolymer composition formed a strong film by heating, and was found to be excellent in a protective effect on skin and hair and a setting effect on hair, and completed the present invention.

[0011]

BEST MODE FOR CARRYING OUT THE INVENTION The silylated peptide having two or more hydroxyl groups directly bonded to a silicon atom has two hydroxyl groups directly bonded to a silicon atom from the time of its synthesis, and has the following general structural formula (I)

[0012]

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[Wherein at least two of R ¹ , R ² and R ³ are hydroxyl groups, the rest are alkyl groups having 1 to 3 carbon atoms, and R ⁴ is a base having an amino group at a terminal of a side chain. R ⁵ represents a residue of a side chain excluding a terminal amino group of a neutral amino acid;
⁴ represents an amino acid side chain other than ^4;
_{2 -, - (CH 2)} 3 - and - (CH _{2) 3} OCH ₂
CH (OH) CH ₂ — represents at least one group selected from the group consisting of: m is 0 to 500, n is 0 to 500,
m + n is from 1 to 500 (however, m and n only indicate the number of amino acids, and do not indicate the order of the amino acid sequence)), and the following general structural formula ( II)

[0014]

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[Wherein, R ^{6 to} R ⁸ each represent a hydroxyl group, an alkoxy group, a halogen group, a hydrogen atom or a carbon atom of 1 to 3;
Represents an alkyl group, R ⁶ to R ⁸ may be the same, may be different from each of at least two of R ⁶ to R ⁸ is an alkoxy group or a halogen group, R ^4,
R ⁵ , A, m and n are the same as those in the above-mentioned general structural formula (I)]. The silylated peptide represented by (II) is disclosed in
424, JP-A-8-67608, JP-A-7
223921, JP-A-7-228508, and the like, and can be easily synthesized in an aqueous solution.

In the silylated peptide represented by the above general structural formula (I), R ⁴ is a side chain residue excluding the terminal amino group of a basic amino acid having an amino group at the terminal of the side chain. Examples of the basic amino acid having an amino group at the terminal of the side chain as described above include lysine, arginine, and hydroxylysine. Further, R ⁵ represents an amino acid side chain 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 structural formula (I), m is 0 to 500, preferably more than 0 and 200 or less (0 <m ≦ 200), more preferably more than 0 and 50 or less (0 <m <200). m ≦ 50), more preferably more than 0 and 10 or less (0 <m ≦ 10), and n is 0
５００500, preferably more than 0 and 200 or less (0 <n
≦ 200), more preferably 1 to 100, further preferably 2 to 40, and m + n is 1 to 500, preferably 1 to 200, more preferably 2 to 100, and still more preferably 3 to 50.

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 sorption effect of the peptide on the original hair decreases. When the ratio of the silyl functional group portion to is small, the characteristics possessed by the silyl functional group portion cannot be sufficiently exhibited, and when m + n is larger than the above range, the sorption property and the permeability to the hair as a peptide become poor. In addition to the reduction compared to low-molecular-weight peptides, they tend to aggregate during storage and storage stability is reduced. The above m, n and m + n are theoretically integers. However, when the peptide portion is a hydrolyzed peptide as described below, the hydrolyzed peptide is obtained as a mixture of those having different molecular weights. The measured value will be the average value.

The peptides used for the silylated peptide represented by the general structural formula (I) include amino acids, peptides, and the like. Examples of the amino acids include alanine, glycine, valine, leucine, isoleucine, and proline. Phenylalanine, tyrosine, serine, threonine, methionine, arginine, histidine, lysine, asparagine, aspartic acid, glutamine, glutamic acid, cystine, cysteine, cysteic acid, tryptophan, hydroxyproline, hydroxylysine, O-phosphoserine, citrulline and the like. .

Examples of the above-mentioned peptides include natural peptides, synthetic peptides, hydrolyzed peptides obtained by partially hydrolyzing proteins (proteins) with acids, alkalis, enzymes or a combination thereof.

Examples of natural peptides include glutathione, bacitracin A, insulin, glucagon, oxytocin, vasopressin, and the like, and examples of synthetic peptides include polyglycine, polylysine, polyglutamic acid, and polyserine.

Examples of the hydrolyzed peptide include collagen (including its denatured gelatin), keratin, silk fibroin (silk), sericin, casein,
Egg yolk protein (protein), egg white protein, egg white protein, soy protein, wheat protein, corn protein, rice (rice bran) protein, animal and plant-derived proteins such as potato protein in eggs such as conchiolin, elastin, chicken, and duck.
Alternatively, yeasts of the genera Saccharomyces, Candida and Endomycopsis, yeast proteins isolated from so-called beer yeasts, sake yeasts, proteins extracted from mushrooms (basidiomycetes), proteins isolated from chlorella, and the like. And a peptide obtained by partially hydrolyzing a protein derived from the microorganism with an acid, an alkali, an enzyme or a combination thereof.

The silylated peptide-silane compound copolymer composition, which is a cosmetic compound of the present invention, is directly bonded to one or more silylated peptides represented by the above general structural formula (I) to a silicon atom by hydrolysis. Can be obtained by condensation polymerization of one or more silane compounds having two or more hydroxyl groups. The silane compound having two or more hydroxyl groups directly bonded to a silicon atom by hydrolysis is, for example, the following general structure Formula (III) R ⁹ pSiX (4-p) (III) wherein p is an integer of 0 to 2, and R ⁹ is an organic group or a hydrogen atom in which a carbon atom is directly bonded to a silicon atom;
R ⁹ may be the same or different. (4-
p) Xs are at least one group selected from the group consisting of a hydroxyl group, an alkoxy group and a halogen group], and the silane compound is hydrolyzed to have the following general structural formula ( IV) R ¹⁰ pSi (OH) qY (4-q-p) (IV) wherein p is an integer of 0 to 2, q is an integer of 2 to 4,
When p + q ≦ 4, R ¹⁰ is an organic group or a hydrogen atom in which a carbon atom is directly bonded to a silicon atom, and p R ¹⁰ may be the same or different. (4-q-p) Ys are at least one group selected from the group consisting of an alkoxy group and a siloxy group]. Note that p, (4-p), q, and (4-q-p) in the general structural formulas (III) and (IV) are subscripts.

Specific examples of the silane compound represented by the general structural formula (III) include, for example, tetramethoxysilane, methyltrimethoxysilane, methyldimethoxysilane, dimethyldimethoxysilane, phenyltrimethoxysilane, diphenyldimethoxysilane Silane, hexyltrimethoxysilane, decyltrimethoxysilane, vinyltrimethoxysilane, 3-methacryloxypropyltrimethoxysilane, 3-methacryloxypropylmethyldimethoxysilane, N- (2-aminoethyl) -3-aminopropyltrimethoxy Silane, N- (2-aminoethyl)
-3-aminopropylmethyldimethoxysilane, 3-aminopropyltrimethoxysilane, N-phenyl-3-
Aminopropyltrimethoxysilane, 3-chloropropyltrimethoxysilane, 3-chloropropylmethyldimethoxysilane, 3-mercaptopropyltrimethoxysilane, 3-glycidoxypropyltrimethoxysilane,
3-glycidoxypropylmethyldimethoxysilane, dimethyloctadecyl [3- (trimethoxysilyl) propyl] ammonium chloride, 3- (trimethoxysilyl) propylpolyoxyethylene (10) ether,
Tetraethoxysilane, methyltriethoxysilane, methyldiethoxysilane, dimethyldiethoxysilane, phenyltriethoxysilane, diphenyldiethoxysilane, vinyltriethoxysilane, 3-methacryloxypropyltriethoxysilane, 3-methacryloxypropylmethyldi Ethoxysilane, N- (2-aminoethyl) -3
-Aminopropyltriethoxysilane, N- (2-aminoethyl) -3-aminopropylmethyldiethoxysilane, 3-aminopropyltriethoxysilane, 3-chloropropyltriethoxysilane, 3-chloropropylmethyldiethoxysilane, 3-glycidoxypropylmethyldiethoxysilane, 3-isocyanatopropyltriethoxysilane, methyldichlorosilane, methyltrichlorosilane, dimethyldichlorosilane, phenyltrichlorosilane, diphenyldichlorosilane, vinyltrichlorosilane, 3-chloropropylmethyldichlorosilane And N- (2-aminoethyl) -3-aminopropyltrimethoxysilane, N- (2-aminoethyl) -3-aminopropylmethyldimethoxysilane, 3
-Aminopropyltrimethoxysilane, 3-chloropropyltrimethoxysilane, 3-chloropropylmethyldimethoxysilane, 3-mercaptopropyltrimethoxysilane, 3-glycosidoxypropyltrimethoxysilane, 3-glycidoxypropylmethyldimethoxysilane, 3-methacryloxypropyltriethoxysilane, 3
-Methacryloxypropylmethyldiethoxysilane, N-
(2-aminoethyl) -3-aminopropyltriethoxysilane, N- (2-aminoethyl) -3-aminopropylmethyldiethoxysilane, 3-aminopropyltriethoxysilane, 3-chloropropyltriethoxysilane, 3 -Chloropropylmethyldiethoxysilane, 3-
Glycosidoxypropylmethyldiethoxysilane, 3-
Protein, alkyl group, polyoxyethylene ether, polyoxypropylene ether, acrylic polymer, polyester, resin acid, dye, ultraviolet absorber, preservative, antibacterial agent, alkyl, silane coupling agent such as isocyanate propyl triethoxy silane Examples thereof include those bonded with ammonium, an aromatic ring, and the like.

Next, a hydroxyl group directly bonded to a silicon atom is
The polycondensation reaction between a silylated peptide having at least two hydroxyl groups and a silane compound having two or more hydroxyl groups directly bonded to a silicon atom by hydrolysis will be described. In the description, it has two or more hydroxyl groups directly bonded to the silicon atom. As the silylated peptide, a silylated peptide represented by the general structural formula (I) or a silylated peptide represented by the general structural formula (II) will be described as a typical example. The silane compound generated more than once will be described with reference to a silane compound represented by the general structural formula (III).

The reaction between the silylated peptide represented by the general structural formula (I) and the silane compound represented by the general structural formula (III) is, for example, first represented by the general structural formula (I) Adjust the aqueous solution of the silylated peptide to an acidic side with hydrochloric acid or sulfuric acid, or adjust it to a basic side with an aqueous sodium hydroxide solution or potassium hydroxide solution.
A silane compound represented by the general structural formula (IV) having two or more hydroxyl groups directly linked to a silicon atom by hydrolysis of an alkoxy group or a halogen group of the silane compound by dropping the silane compound represented by And then
By neutralization, the hydroxyl group of the silylated peptide represented by the general structural formula (I) and the hydroxyl group of the silane compound represented by the general structural formula (IV) are polycondensed to obtain a copolymer composition. As described above, the hydrolysis of the silane compound represented by the general structural formula (III) to the silane compound represented by the general structural formula (IV) is carried out with the silylated peptide represented by the general structural formula (I). It is not necessary to carry out hydrolysis of the silane compound represented by the general structural formula (III) in a system different from the above-mentioned polycondensation system.

Further, as described above, the silylated peptide represented by the general structural formula (II) is converted into the silylated peptide represented by the general structural formula (I) by hydrolysis. When the silylated peptide represented by the general structural formula (II) is used,
When the aqueous solution of the silylated peptide represented by is adjusted to an acidic side with hydrochloric acid or sulfuric acid, or adjusted to a basic side with an aqueous solution of sodium hydroxide or potassium hydroxide, an alkoxy group or a halogen group bonded to the silyl group is hydrolyzed. The compound is decomposed into a hydroxyl group to form a silylated peptide represented by the general structural formula (I). Thereafter, the silane compound represented by the general structural formula (III) is dropped therein similarly to the above. As a result, the alkoxy group or the halogen group of the silane compound represented by the general structural formula (III) is hydrolyzed into a silane compound represented by the general structural formula (IV), and then neutralized. Then, the hydroxyl group of the silylated peptide and the hydroxyl group of the silane compound represented by the general structural formula (IV) are polycondensed to obtain a copolymer composition. As described above, even when the silylated peptide represented by the general structural formula (II) is used, the hydrolysis can be performed by adjusting the acid side or the basic side. Hydrolysis of the silylated peptide represented by the structural formula (II) to the silylated peptide represented by the general structural formula (I) also includes
The reaction can be performed in the same system as the reaction system when the above-mentioned silylated peptide and the silane compound represented by the general structural formula (III) are polycondensed, and need not be performed in another system.

The hydrolysis reaction generally proceeds favorably at a pH of 2 to 3. However, some silylated peptides represented by the general structural formula (I) are apt to produce insolubles on the acidic side. It is preferably carried out at pH 10-11. When an alkoxysilane compound is used as the silane compound represented by the general structural formula (III), the pH may be adjusted only before the dropwise addition of the silane compound. When the reaction is carried out on the basic side using a compound, the pH drops during the reaction. Therefore, it is necessary to maintain the pH at 10 to 11 by adding an aqueous solution of sodium hydroxide or potassium hydroxide. When an aminosilane compound is used as the silane compound represented by the general structural formula (III) to react on the acidic side, pH during the reaction is
The pH rises to 2 by adding dilute hydrochloric acid or dilute sulfuric acid.
Need to keep ~ 3.

If the reaction temperature is too low, the reaction does not proceed easily. If the reaction temperature is too high, the alkoxy group and the halogen group of the silyl compound represented by the general structural formula (III) are rapidly hydrolyzed. preferable. The reaction time is
Although it depends on the reaction amount, it is preferable to drop the silane compound represented by the general structural formula (III) dropwise over 30 minutes to 2 hours, and then continue stirring for 1 to 6 hours.

At the end of the hydrolysis reaction, the silylated peptide represented by the general structural formula (I) and the silane compound represented by the general structural formula (III) are dissociated because the reaction solution is acidic or basic. If the reaction solution is acidic, add an alkaline aqueous solution such as aqueous sodium hydroxide or potassium hydroxide.If the reaction solution is basic, add an aqueous acid such as dilute hydrochloric acid or dilute sulfuric acid and stir. To neutralize the solution. By this neutralization, polycondensation proceeds to obtain a target silylated peptide-silane compound copolymer composition, but stirring after neutralization is preferably for about 2 to 20 hours.

The silylated peptide-silane compound copolymer composition, which is a cosmetic compound of the present invention, is produced as described above. The silylated peptide having two or more hydroxyl groups and the silane compound having two or more hydroxyl groups are prepared. In the reaction, the reaction ratio is represented by the composition ratio, and the silylated peptide: silane compound =
The reaction is carried out within the range of 5: 1 to 1: 1. This is because when the reaction ratio of the silane compound to the silylated peptide is 5: 1 or less in composition ratio, the polycondensation of the silylated peptide and the silane compound hardly proceeds, On the other hand, when the reaction ratio of the silane compound becomes 1: 1 or more in the composition ratio, the water-soluble transparency of the silylated peptide-silane compound copolymer composition becomes poor, and the water-soluble transparent cosmetic is produced. It is because it becomes difficult to mix in.

The silylated peptide-silane compound copolymer composition obtained as described above can be used as it is as a cosmetic compounding agent, but since a hydroxyl group remains in the terminal silyl group of the copolymer composition, Further, a silane compound in which one hydroxyl group is generated by hydrolysis may be added.

Examples of the silane compound having one hydroxyl group directly bonded to a silicon atom by such hydrolysis include the following general structural formula (V) R ¹¹ ₃ SiZ (V) [wherein three R ¹¹ Is an organic group in which a carbon atom is directly bonded to a silicon atom, and three R ^{11 s} may be the same or different. Z is at least one group selected from the group consisting of a hydroxyl group, an alkoxy group, a halogen group, a carboxyl group, and an amino group], and the silane compound has the following general structure by hydrolysis. Formula (VI) R ¹¹ ₃ Si (OH) (VI) [wherein three R ³ are organic groups having a carbon atom directly bonded to a silicon atom, and the three R ¹¹ may be the same or different. Silane compound represented by the formula:

Specific examples of the silane compound represented by the general structural formula (V) include, for example, dimethylvinylchlorosilane, n-butyldimethylchlorosilane, te
rt-butyldimethylchlorosilane, tert-butyldiphenylchlorosilane, octadecyldimethylchlorosilane, methyldiphenylchlorosilane, tri-n-butylchlorosilane, triethylchlorosilane, trimethylchlorosilane, tri-n-propylchlorosilane, triphenylchlorosilane, trimethylsilyl iodide, dimethylethoxy Examples include silane, dimethylvinylethoxysilane, dimethylvinylmethoxysilane, trimethylethoxysilane, trimethylmethoxysilane, and triphenylethoxysilane.

In addition, silyl compounds having two silicon atoms, such as hexamethyldisilazane and hexamethyldisiloxane, can also be used because one hydroxyl group directly connected to the silicon atom is generated by hydrolysis. it can.

As is apparent from the general structural formula (V), such a silane compound has only one reactive group directly bonded to a silicon atom, and thus has the general structural formula (VI) obtained by hydrolyzing it. The represented silane compound reacts with the hydroxyl group present in the silylated peptide-silane compound copolymer composition to reduce the hydroxyl group in the silylated peptide-silane compound copolymer composition, and the silylated peptide-silane compound Prevents the copolymer composition from undergoing polycondensation during storage.
That is, by reacting the silane compound represented by the general structural formula (VI) obtained by hydrolyzing the silane compound represented by the general structural formula (V), a silylated peptide-silane having good storage stability is obtained. It can be a compound copolymer composition. In the reaction between the silylated peptide represented by the general structural formula (I) and the silane compound represented by the general structural formula (III), during the step of neutralizing the solution and subjecting it to a polycondensation reaction, When the silane compound represented by the structural formula (VI) is reacted, the molecular weight of the silylated peptide-silane compound copolymer composition can be controlled.

The reaction between the silylated peptide-silane compound copolymer composition and the silane compound represented by the general structural formula (V) can be carried out, for example, by treating the silylated peptide-silane compound copolymer composition in an aqueous solution of the general structural formula By dropping the silane compound represented by (V), the hydroxyl group of the silyl compound represented by the general structural formula (VI) is bonded to the hydroxyl group of the silylated peptide-silane compound copolymer composition.

However, in the silane compound represented by the above general formula (V), the silane compound in which Z is a halogen group has good hydrolyzability, so that the above silane compound in an aqueous solution of a silylated peptide-silane compound copolymer composition is used. The above reaction proceeds by directly dropping the silane compound represented by the formula (V), but the silane compound represented by the general structural formula (V), wherein Z is an alkoxy group, hexamethyldisiloxane, etc. Since the reactivity of the silane compound having two silicon atoms is slightly lower, it is necessary to adjust the pH of the aqueous solution of the silylated peptide-silane compound copolymer composition to 2 to 3 and then drop those silane compounds. .

The reaction temperature between the silylated peptide-silane compound copolymer composition and the silane compound represented by the above general formula (V) is preferably 30 to 60 ° C. Although the reaction time varies depending on the reaction amount, it is preferable that the silane compound represented by the general structural formula (V) is dropped for 30 minutes to 2 hours and the subsequent stirring is about 1 to 6 hours.

After completion of the stirring, the reaction solution is neutralized with an aqueous alkali solution such as an aqueous sodium hydroxide solution or an aqueous potassium hydroxide solution, and further stirred for about 2 to 10 hours to complete the reaction. A compound copolymer composition is obtained.

After completion of the neutralization reaction, the reaction solution is adjusted to pH, and then used as a liquid or powdered as a compounding agent for cosmetics, fiber treatment agents, and the like. After purification by ion exchange resin, dialysis membrane, electrodialysis, gel filtration, ultrafiltration, etc., it is used as a liquid or powdered.

The silylated peptide-silane compound copolymer composition obtained by the above reaction has the following composition formula (R ¹¹ R ¹² R ¹³ SiO _1/2 ) a (R ¹⁴ R ¹⁵ SiO) b
(R ¹⁶ SiO _3/2 ) c (SiO ₂ ) d (R ¹⁷ O _1/2 ) e [wherein R ^{11 to} R ¹³ are organic groups in which a carbon atom is directly bonded to a silicon atom, and at least one of R ^{14 to} R ¹⁶ is a bond. A (bond A is _{-CH 2 -, - (CH 2} ) 3 -, -
_{(CH 2) 3 OCH 2 CH} (OH) CH 2 -, - (CH
_{2) 3 S -, - (} CH 2) 3 NH- or - (CH _2)
3 OCOCH ₂ CH ₂ — or the like)), the residue obtained by removing the silyl functional group portion from the silylated peptide to which the peptide is bonded, and the rest being a hydrogen atom, an alkyl group having 1 to 18 carbon atoms, or a phenyl group. Or a residue excluding the silyl functional group portion of a compound capable of bonding to the silyl functional group via a bond C (the bond C is the same as the bond A), and may be different from each other or may be the same. , R ¹⁷ represents a hydrogen atom or a lower alkyl group. a, b, c, d, and e are each an integer of 0 or more, and 2 ≦ b + c + d and a + e ≦ c
+ 2d + 2].

As cosmetics to which the cosmetic compounding agent comprising the silylated peptide-silane compound copolymer composition of the present invention is compounded, for example, shampoo, hair rinse, split coat, first agent for permanent web and second agent for permanent web Preparations, hair creams, hair conditioners, set lotions, hair colors, hair treatment rinses, liquid hair preparations, hair packs, hair cosmetics such as hair growth and hair growth agents, lotions, aftershave lotions, shaving foams, burnishing creams, cleansing creams, It can be used for various creams such as emollient cream, moisture cream, hand cream, facial cleansing foam, hair remover, face pack, milky lotion, face wash, body shampoo, various soaps, makeup products, sunscreen products, etc. Ah But since then polymerized to form a strong film by heating, hair rinses, split hair coat, hair cream, hair conditioner, set lotion, particularly preferably used for the hair cosmetics such as hair dressing.

The cosmetic compounding agent comprising the above-mentioned silylated peptide-silane compound copolymer composition is used in an amount of 0.1 to 30% by weight, especially 1 to 20% by weight in the cosmetic.
It is preferable to set the degree. That is, when the amount of the silylated peptide-silane compound copolymer composition in the cosmetic is less than the above range, a film is formed on the hair to impart gloss and moisture to the hair or to protect the hair. However, even if the effect of improving combability is not sufficiently exhibited, and the amount of the silylated peptide-silane compound copolymer composition in cosmetics is larger than the above range, the effect is increased accordingly. Rather, it can lead to sticky hair and skin.

In addition, the above cosmetics may contain a silylated peptide-
Examples of components that can be used in combination with a cosmetic compounding agent comprising a silane compound copolymer composition include sodium lauryl sulfate, ethanolamine lauryl sulfate, polyoxyethylene (2EO) lauryl ether triethanolamine sulfate (EO is ethylene). In oxides, the value before EO indicates the number of moles of ethylene oxide added),
Polyoxyethylene (3EO) alkyl (C11-C11)
15 or a mixture of two or more) sodium ether sulfate, sodium laurylbenzenesulfonate,
Laurylbenzenesulfonic acid triethanolamine, polyoxyethylene (3EO) tridecyl ether acetic acid,
Coconut oil fatty acid-sodium L-glutamate, coconut oil fatty acid sarcosine sodium, collagen, keratin, fibroin, casein, protein hydrolysates derived from animals and plants such as soybean, wheat, corn, and yeast, and protein water derived from microorganisms such as mushrooms An acylated hydrolyzed protein or a salt thereof obtained by acylating the decomposition with a fatty acid having 8 to 20 carbon atoms, hydrogenated coconut oil fatty acid sodium glycerin sulfate,
Anionic surfactants such as sodium polyoxyethylene alkyl (12 to 15 carbon atoms) ether phosphate (8 to 10 EO), sodium polyoxyethylene cetyl ether phosphate, sodium coconut fatty acid methyl taurate, and sodium coconut fatty acid isethionate Surfactants, cationic surfactants such as distearyldimethylammonium chloride and stearyltrimethylammonium chloride, 2-alkyl (C12-15) -N-carboxymethyl-N
-Hydroxyethyl imidazolinium betaine, undecyl hydroxyethyl imidazolinium betaine sodium, N-coconut fatty acid acyl-L-arginineethyl-DL-pyrrolidonecarboxylate, coconut fatty acid amidopropyl betaine, N-alkyl (carbon number 12-18)
Amphoteric surfactants such as betaine dimethylaminoacetate, polyoxyethylene alkyl (C12-14) ether (7EO), polyoxyethylene oleyl ether,
Nonionic surfactants such as polyoxyethylene nonyl phenyl ether, alkyl glucoside, alkyl polyglycoside, cationic polymers such as cationized cellulose and cationized hydroxyethyl cellulose, amphoteric polymers, synthetic polymers such as anionic polymers, animal and vegetable oils, carbonized Oils such as hydrogens, ester oils and higher alcohols, polysaccharides or derivatives thereof, humectants such as propylene glycol, 1,3-butylene glycol and glycerin, lower alcohols such as ethanol and propyl alcohol, sodium L-aspartate , DL-alanine, L-arginine, L-cysteine and other amino acids, collagen and keratin, fibroin, casein, soybean, wheat, corn and other animal and plant-derived proteins and yeasts Hydrolyzed peptides obtained by hydrolyzing proteins derived from microorganisms such as mushrooms and their quaternized derivatives, ester derivatives, animal and plant extracts, preservatives, fragrances and the like can be mentioned. Other components can be added as appropriate within a range that does not impair.

The silylated peptide-silane compound copolymer composition of the present invention, which is a cosmetic compound, contains a chain or cyclic silicone oil such as methylpolysiloxane, methylphenylpolysiloxane or amino-modified silicone oil. In this case, the action of the silicone oil can be increased while improving the emulsion stability of the silicone oil.

[0047]

Industrial Applicability The silylated peptide-silane compound copolymer composition of the present invention, which is a cosmetic compound, has excellent properties based on the silylated peptide represented by the general structural formula (I) and the general structural formula (III) Has excellent properties added based on the silane compound represented by, when adding it to hair cosmetics and skin cosmetics, impart gloss and moisture to the hair,
Improves combability of hair and prevents branching of hair, imparts luster and moisture to the skin, smoothes the skin, and, especially when blended with a cleaning agent such as shampoo, makes the foam a soft feel. It has properties such as smoothing hair and skin after use.

Further, the cosmetic compounding agent comprising the silylated peptide-silane compound copolymer composition undergoes polymerization by heating and forms a strong film. Therefore, when compounding in hair cosmetics, the hair has a setting property. Excellent in imparting and protecting effect.

[0049]

Next, the present invention will be described more specifically with reference to examples. However, the present invention is not limited to only these examples. Prior to the examples, conditions for gel filtration analysis and measurement conditions for infrared absorption spectrum analysis used in the examples will be described. In the following examples and the like,% indicating the concentration of the solution or dispersion is% by weight.

[Gel Filtration Analysis] Gel filtration analysis was performed under the following conditions. The results of the analysis are shown in the figure. The results of the obtained copolymer composition are indicated by solid lines, and the results of the silylated peptide as a raw material are indicated by broken lines.

Analytical column: TSKgel G3000PW (7.5 mm ID × 30 cm) manufactured by Tosoh Corporation Eluent: 0.1 M phosphate buffer (pH 6.8) +0.3 M NaCl aqueous solution Elution rate: 0.9 ml / min Detector : UV detector, 280 nm standard sample: γ-globulin (MW 155,000) Bovine serum albumin (MW 67,000) Ovalbumin (MW 45,000) β-lactoglobulin (MW 16,800) Cytochrome C (MW 12, MW) 000) Aprotinin (MW 6,500)

[Infrared absorption spectrum analysis] In the measurement of infrared absorption spectrum analysis, FT-M manufactured by Shimadzu Corporation was used.
Using IR8200PC (hereinafter referred to as FT-IR),
Samples were powdered by lyophilization and measured by the KBr tablet method.

Example 1 Silylated hydrolyzed collagen and methyltriethoxysila
Of ethylene and tetraethoxysilane with hydrolysates
Production of composition (equivalent ratio = 1: 0.7: 0.2 equivalent)

In a 300 ml beaker, silylated hydrolyzed collagen (N- [2-hydroxy-3-
(3′-methyldihydroxysilyl) propoxy] propyl hydrolyzed collagen) (number average molecular weight of hydrolyzed collagen is about 1500) 200.3 g and 18% hydrochloric acid 5.
0 g, and 0.78 equivalent of methyltriethoxysilane [KBE-13 (trade name) manufactured by Shin-Etsu Chemical Co., Ltd.] to silylated hydrolyzed collagen 1.38 g and 0.2 equivalent of tetraethoxysilane [Shin-Etsu Chemical Industry KBE-04
(Trade name)] After adding 0.46 g, the mixture was stirred with a magnetic stirrer at 55 ° C for 3 hours. Next, 4.8 g of a 20% aqueous sodium hydroxide solution was added dropwise while stirring, and p
H was adjusted to 6.5, and stirring was continued at 55 ° C. for 16 hours. After completion of the reaction, the reaction solution was filtered to remove insolubles, and water was added to adjust the solid content to 10%. Then, the solution was sterilized by heating at 80 ° C. for 1 hour, and then sterilized and filtered. The silylated peptide-silane compound copolymer composition
05.5 g were obtained.

FIG. 1 shows the results of gel filtration analysis of the obtained copolymer composition and the silylated hydrolyzed collagen as a raw material. As is clear from FIG. The peak at a molecular weight of about 20,000 for gel filtration of the silylated hydrolyzed collagen decreased, and another peak was observed near the gel filtration molecular weight of about 85,000, confirming that the silylated hydrolyzed collagen and the silane compound were copolymerized. .

Further, the obtained copolymer composition and the raw material of the silylated hydrolyzed collagen were each subjected to FT-
Analysis by IR and comparison showed that the copolymer composition had 12
A peak near 50 cm ^-1 attributable to Si-CH ₃ is enhanced, and a peak near 1100 cm ^-1 attributable to Si-O is detected, indicating that the copolymer composition has an Si-O-Si bond. It was confirmed to have.

Example 2 Silylated hydrolyzed collagen and methyltriethoxysila
Copolymerization composition with a hydrolyzate of ethylene (equivalent ratio = 1: 0.
2) Manufacturing

In a 300 ml beaker, silylated hydrolyzed collagen (N- [2-hydroxy-3-
(3′-trihydroxysilyl) propoxy] propyl hydrolyzed collagen) (number average molecular weight of hydrolyzed collagen is about 1500) 204.0 g and 6.2 g of 18% hydrochloric acid
Is added, and 0.46 g of methyltriethoxysilane [KBE-13 (trade name) manufactured by Shin-Etsu Chemical Co., Ltd.] is added to the silylated hydrolyzed collagen in an amount of 0.2 equivalent. Stir for 2 hours. Next, while stirring, 5.5% of a 20% aqueous sodium hydroxide solution was used.
g was added dropwise to adjust the pH to 6.5, and stirring was continued at 55 ° C. for 16 hours. After completion of the reaction, the reaction solution was filtered to remove insolubles, and water was added to adjust the solid content to 10%. Then, the solution was sterilized by heating at 80 ° C. for 1 hour, and then sterilized and filtered. 234.2 g of a silylated peptide-silane compound copolymer composition was obtained.

FIG. 2 shows the results of gel filtration analysis of the obtained copolymer composition and the silylated hydrolyzed collagen as a raw material. As is clear from FIG. The peak of the gel filtration molecular weight of about 20,000 of the silylated hydrolyzed collagen decreased, and another peak was observed at about the gel filtration molecular weight of about 50,000, confirming that the silylated hydrolyzed collagen and the silane compound were copolymerized. .

The obtained copolymer composition and its raw material, silylated hydrolyzed collagen, were each converted to FT-
Analysis by IR and comparison showed that the copolymer composition had 12
A peak near 50 cm ^-1 attributable to Si-CH ₃ is enhanced, and a peak near 1100 cm ^-1 attributable to Si-O is detected, indicating that the copolymer composition has an Si-O-Si bond. It was confirmed to have.

Example 3 Silylated hydrolyzed silk and methyltriethoxysilane and
Composition of Poly (ethylene and tetraethoxysilane) with Hydrolyzate
Of a product (equivalent ratio = 1: 0.6: 0.2)

In a 300 ml beaker, silylated hydrolyzed silk (N- [2-hydroxy-3-
(3′-methyldihydroxysilyl) propoxy] propyl hydrolyzed silk) (200.0 g of hydrolyzed silk having a number average molecular weight of about 350) and 18.4 g of 18% hydrochloric acid were added to the silylated hydrolyzed silk. 0.6 equivalent of methyltriethoxysilane [KBE- manufactured by Shin-Etsu Chemical Co., Ltd.
13 (trade name)] 7.65 g and 0.2 equivalent of tetraethoxysilane [KBE-04 (trade name) manufactured by Shin-Etsu Chemical Co., Ltd.]
After adding 3.0 g, the mixture was stirred at 60 ° C. with a magnetic stirrer.
For 3 hours. Next, 18.0 g of a 20% aqueous sodium hydroxide solution was added dropwise with stirring to adjust the pH to 6.5, and stirring was further continued at 60 ° C. for 16 hours. After completion of the reaction, the reaction solution was placed in a cellophane tube for dialysis, dialyzed in running tap water for 12 hours, and desalted. The desalted solution was concentrated under reduced pressure, and after removing insoluble matters by filtration, water was added to adjust the solid content concentration to 20%.
After sterilization by heating at 80 ° C. for 1 hour, sterilization filtration was performed to obtain 114.8 g of a silylated peptide-silane compound copolymer composition.

The results of gel filtration analysis of the obtained copolymer composition and the silylated hydrolyzed collagen as a raw material are shown in FIG. 3. As is clear from FIG. 3, in the obtained copolymer composition, the raw material The peak of the gel filtration molecular weight of about 10,000 of the silylated hydrolyzed silk decreases, and the gel filtration molecular weight of about 48
Another peak was observed at around 000, confirming that the silylated hydrolyzed silk and the silane compound were copolymerized.

The obtained copolymer composition and its raw material
And FT-IR
As a result, the copolymer composition was 1250.
cm ^-1Nearby Si-CH_ThreePeak likely to be due to
Is enhanced and is considered to be caused by Si—O.
100cm^-1A peak near the copolymer composition was detected.
It was confirmed that it had a Si-O-Si bond.

Example 4 Silylated hydrolyzed keratin and dimethyldiethoxysilane
Of copolymers of styrene and tetraethoxysilane with hydrolysates
Production of product (equivalent ratio = 1: 0.3: 0.2)

In a 300 ml beaker, silylated hydrolyzed keratin (N- [2-hydroxy-3-
(3′-Methyldihydroxysilyl) propoxy] propyl hydrolyzed keratin) (78.0 g of hydrolyzed keratin has a number average molecular weight of about 1000), 122.0 g of purified water and 10.3 g of 18% hydrochloric acid were put thereinto to silylate. 0.3 equivalent of dimethyldiethoxysilane based on hydrolyzed keratin [KBE-22 (trade name) manufactured by Shin-Etsu Chemical Co., Ltd.]
After adding 64 g and 1.5 equivalent of 0.2 equivalent of tetraethoxysilane [KBE-04 (trade name) manufactured by Shin-Etsu Chemical Co., Ltd.], the mixture was stirred at 60 ° C. for 2 hours with a magnetic stirrer. Next, 10.0 g of a 20% aqueous sodium hydroxide solution was added dropwise with stirring to adjust the pH to 6.5, and stirring was continued at 60 ° C. for 16 hours. After completion of the reaction, the reaction solution was placed in a cellophane tube for dialysis, dialyzed in running tap water for 12 hours, and desalted. The desalted solution was concentrated under reduced pressure, and after removing insoluble matter by filtration, water was added to adjust the solid content concentration to 20%, and then sterilization filtration was performed after heat sterilization at 80 ° C. for 1 hour. Thus, 61.5 g of a silylated peptide-silane compound copolymer composition was obtained.

FIG. 4 shows the results of gel filtration analysis of the obtained copolymer composition and the silylated hydrolyzed keratin of the starting material. As is clear from FIG. The peak of the gel filtration molecular weight of about 12,000 of the silylated hydrolyzed keratin decreases, and the gel filtration molecular weight of about 52
Another peak was observed at around 000, confirming that the silylated hydrolyzed keratin and the silane compound were copolymerized.

The obtained copolymer composition and its starting material, the silylated hydrolyzed keratin, were each converted to FT-I
When analyzed and compared by R, 125% was obtained in the copolymer composition.
A peak near 0 cm ⁻¹ attributable to Si—CH ₃ was enhanced, and a peak near 1100 cm ⁻¹ attributable to Si—O was detected, indicating that the copolymer composition had a Si—O—Si bond. It was confirmed to have.

[Coating Strength Test] The coating strengths of the silylated peptide-silane compound copolymers of Examples 1 to 4 and the silylated peptide as the raw materials were compared.

The test was carried out in accordance with the JIS paint general test and the pencil scratch test method (JIS K5400, 6.14). That is, 2 g of a sample adjusted to have an active ingredient concentration of 10% was uniformly applied to a stainless steel dish having a diameter of 9 cm, dried at 105 ° C for 1 hour, and then placed in a desiccator at 25 ° C and a relative humidity of 49%. After preservation for a time, it is used as a test membrane, using pencils having different hardness according to JIS 9H-9B,
The test membrane was scratched at a load of 30 g at a speed of 1 mm / sec, and the hardest pencil hardness that was not damaged was taken as the film strength of the membrane. The test was performed in an environment with a relative humidity of 58%. Table 1 shows the test results.

[0071]

[Table 1]

As shown in Table 1, any of the silylated peptide-silane compound copolymers of Examples 1 to 4 can form a film having a higher strength than the silylated peptide as each raw material. It was clear. In particular, the copolymer composition of Example 3 using silylated hydrolyzed silk as a raw material formed a very hard film.

[Test of Wave Effect on Hair]
The effect of setting the silylated peptide-silane compound copolymer composition prepared in 4 on the hair with the silylated peptide as a raw material was compared in terms of wave efficiency and wave retention.

The silylated peptide-silane compound copolymer compositions of Examples 1 to 4 and the silylated peptide of each raw material were used after adjusting the concentration of the active ingredient (solid content) to 5%. .

The test method is as follows. First, ten hairs are bundled, the hair roots are aligned and fixed with tape, and the length is adjusted to 250 mm. The hair bundle is washed by immersing it in a 2% aqueous solution of 20% 2% polyoxyethylene (3) lauryl ether sulfate at 40 ° C. for 15 minutes, rinsing it in running tap water for 5 minutes, and further adding 10 times the amount of ion-exchanged water. After rinsing twice for 5 minutes, air-dry. The rod for curling has a diameter of 10 mm and a length of 150
Use a 10 mm glass tube and mark in advance every 10 mm (mark the other side by shifting 5 mm). Then, as shown in FIG. 5, a clip-type weight of 31.5 g is attached to the tip of the hair bundle so that the hair bundle can be curled with a constant tension, and the hair bundle is passed over the mark on the rod. And fix both ends with rubber bands.

Each of the above-mentioned samples having an active ingredient concentration of 5% was separately applied to the hair bundle wound around the rod as described above.
After applying 2 g each, the hair was well blended and dried in a thermostat at 80 ° C. for 15 minutes to form wavy hair. Then, the wave hair was removed from the rod, the wavelength of the formed curl was measured, and the wave efficiency immediately after the treatment was calculated. Then, the hair bundle was suspended and stored in a humidity chamber at a relative humidity of 70% so that the hair tip was turned down, and the wavelength of the web was measured after 1, 2, 4, and 20 hours. , Wave efficiency and wave retention were calculated.

In the measurement of the wavelength and the wave number, as shown in FIG. 6, except for the waves at both ends, the distance between the vertex of the second wave and the second vertex from the end is measured on both the left and right sides. . The distance from the end from the second wave apex of the left and right until the second vertex and L _1, L _2, L ₁ and L
The number of waves between ₂ is n ₁ and n ₂ , respectively, and the average wavelength (L) is obtained by the following equation.

[0078]

The wavelength (diameter) of the rod itself is 10 mm
Therefore, the wave efficiency can be obtained by the following equation.

[0080]

From the ratio between the wave efficiency after the setting process and the obtained wave efficiency after being stored in the constant humidity bath for a certain period of time, the wave holding ratio is obtained as shown by the following equation.

[0082]

Tables 2 and 3 show the wave efficiencies and wave holding ratios obtained as described above. In the tables, the silylated peptides as the raw materials of Examples 1 to 4 are described only as the raw materials of Examples 1 to 4 in terms of space, but the silylated peptides of the raw materials of each Example are as follows. Raw material of Example 1; Silylated hydrolyzed collagen; Raw material of Example 2; Silylated peptide; Raw material of Example 3; Raw material of Example 3; Raw material of Example 4 -Silylated peptide; silylated hydrolyzed keratin

[0084]

[Table 2]

[0085]

[Table 3]

As shown in Tables 2 and 3, the copolymer compositions of Examples 1 to 4 exhibited higher wave efficiencies than the starting silylated peptides of the respective Examples, Has a high wave retention even after being stored for 20 hours under the condition of a high humidity of 70% relative humidity, and is obtained by applying the copolymer compositions of Examples 1 to 4 to hair and subjecting the hair to heat treatment. Example 1 shows the setting force for the hair to be
It was clear that the silylated peptide, which is a raw material of the copolymer compositions of Nos. 1 to 4, was superior to the setting power for hair.

[0087]

[Brief description of the drawings]

FIG. 1 is a diagram showing the results of gel filtration analysis of a silylated hydrolyzed collagen-silane compound copolymer composition of Example 1 and a silylated hydrolyzed collagen as a raw material thereof.

FIG. 2 is a graph showing the results of gel filtration analysis of a silylated hydrolyzed collagen-silane compound copolymer composition of Example 2 and a raw material of the silylated hydrolyzed collagen.

FIG. 3 shows the results of gel filtration analysis of the silylated hydrolyzed silk-silane compound copolymer composition of Example 3 and the raw material of the silylated hydrolyzed silk.

FIG. 4 is a graph showing the results of gel filtration analysis of the silylated hydrolyzed keratin-silane compound copolymer composition of Example 4 and the raw material of the silylated hydrolyzed keratin.

FIG. 5 is a diagram schematically illustrating a method of preparing a hair bundle for measuring a wave efficiency and a wave retention.

FIG. 6 is a diagram schematically showing a state of a hair bundle after wave processing.

 ────────────────────────────────────────────────── ─── Continuing on the front page (72) Inventor Takashi Adachi 1-2-14 Fukuichicho, Higashiosaka-shi, Osaka F-term (reference) 4C083 AD161 AD162 AD411 AD432 AD442 AD452 CC32 CC34 DD23 DD27 EE25 EE28 EE29 FF01

Claims (1)

[Claims] 1. A composition comprising at least one silylated peptide having two or more hydroxyl groups directly bonded to a silicon atom and at least one silane compound having two or more hydroxyl groups directly bonded to a silicon atom by hydrolysis. : A cosmetic compounding agent comprising a silylated peptide-silane compound copolymer composition obtained by condensation polymerization in an aqueous solution in the range of 1 to 1: 1.