JPH0867608A - Cosmetic base - Google Patents

Abstract

PURPOSE: To obtain a cosmetic base providing a hair cosmetic and a skin cosmetic, providing hair and skin and luster and moisture, improving combing properties, preventing split hair, smoothing skin, mot causing turbidity and precipitation during preservation. CONSTITUTION: This cosmetic base comprises a silylated peptide obtained by subjecting a functional group containing only one silicon atom of formula I (R<1> to R<3> are methyl or OH; (a) is 1-3) to covalent bonding to 50-70wt.% of the whole amino groups including amino groups at the side chain of amino acids of a peptide such as a silylated peptide of formula II (R<4> is the residue after removal of an end amino group of a basic amino acid containing an amino acid at the end of a side chain; R<5> is an amino group except R<4> ; (m) is 0-50; (n) is 0-50; m+n is 1-50). The silylated peptide is obtained by reacting a peptide with a silyl compound of formula III (R<6> to R<8> are each methyl, methoxy, ethoxy, OH or halogen). The cosmetic base has excellent characteristics of both silicone compound and polypeptide, excellent pH stability in water and storage stability.

Description

Detailed Description of the Invention

[0001]

FIELD OF THE INVENTION The present invention relates to a cosmetic base material comprising a silylated peptide. For more information,
The present invention comprises a silylated peptide in which 50% or more and 75% or less of all amino groups of the peptide have a covalently bonded functional group containing only one silicon atom, and is water-soluble, and when incorporated into hair cosmetics and skin cosmetics. , Imparts luster and moisture to the hair, improves combability of the hair, and prevents branching of the hair,
The present invention relates to a cosmetic base material that imparts luster and moisture to the skin, smoothes the skin, has excellent pH stability and storage stability, and does not cause turbidity or precipitation during storage.

[0002]

2. Description of the Related Art Conventionally, silicone oil (organosilicon compound) and polypeptide have been blended in hair cosmetics to give silicone oil excellent extensibility, action to impart gloss and luster to hair, and water repellency to hair. Attempts have been made to exert the protective effect by application, the sorption effect of polypeptide on hair, the effect of alleviating skin irritation, the effect of film formation and the effect of moisturizing.

For example, Japanese Patent Publication No. 63-5005 proposes a hair cosmetic composition containing a hydrophobic silicone oil and a mono-N-long-chain acyl basic amino acid lower alkyl ester salt, and is disclosed in Japanese Patent Laid-Open No. 63-310812. Proposes a hair treatment containing methyl polysiloxane or methylphenyl polysiloxane and hydrolyzed collagen.

However, since silicone oil is originally a hydrophobic (lipophilic) substance and polypeptide is originally a hydrophilic substance, it is difficult for them to be compatible with each other, and when they are used in combination. Lacks emulsion stability,
Since it is easy to separate, the commercial value of cosmetics is likely to be impaired, and it is difficult for the polypeptide to adhere to the part that has come into contact with the silicone oil first, and conversely, to the part that has come into contact with the polypeptide before the silicone. There was a problem that oil could not be attached and the properties of both could not be fully exhibited.

Therefore, in order to solve the above problem, a hydrophobic silicone oil and a hydrophilic polypeptide are reacted to synthesize a compound which combines the characteristics of the silicone oil and the characteristic of the polypeptide, and is used as a cosmetic base. It has been attempted to solve the drawbacks of the combined use of a silicone oil and a polypeptide and to exhibit the characteristics of the silicone oil and the characteristics of the polypeptide by using it as a material (JP-A-3-223207). Issue).

[0006]

However, the peptide-modified silicone derivative disclosed in Japanese Patent Application Laid-Open No. 3-223207 described above has pH stability and storage stability in water due to the influence of the hardly soluble or insoluble silicone moiety in water. Since the hair cosmetics and the skin cosmetics are mainly water-soluble, there is a problem that turbidity or precipitation occurs during storage.

Further, in the production of the above peptide-modified silicone derivative, the reaction between the poorly soluble or insoluble silicone oil and the water-soluble polypeptide is carried out in water, so that the reactivity is poor, the yield is low, and the yield is improved. However, there is a problem in that a water-soluble organic solvent such as alcohol must be added.

Therefore, the present invention has both the excellent properties of a silicone compound and the excellent properties of a polypeptide, and also has excellent pH stability and storage stability in water, and does not cause turbidity or precipitation during storage. It is intended to provide a cosmetic base material.

[0009]

Means for Solving the Problems As a result of intensive studies to achieve the above object, the present inventors have found that 50% or more of all amino groups including amino groups in the amino acid side chains of peptides are 75%.
The following general formula (I)

[0010]

[Chemical 3]

[In the formula, R ¹ , R ² and R ³ represent a methyl group or a hydroxyl group, and these R ¹ , R ² and R ³ may be the same or different. a is 1 or 3
The silylated peptide having a covalently bonded functional group containing only one silicon atom is water-soluble, has excellent pH stability and storage stability in water, and has excellent properties of a silicone compound. And has the excellent properties of a polypeptide, and when blending this into hair cosmetics and skin cosmetics,
It imparts luster and moisture to the hair, improves combability of the hair, prevents branching of the hair, and imparts luster and moisture to the skin.
Moreover, it was found that when it is blended into a detergent such as shampoo, it softens the foam, smoothes the hair and skin after use, and does not cause turbidity or precipitation during storage. It came to complete the invention.

In the following, the present invention is applied to the structure and properties of silylated peptides, the action of silylated peptides on hair and skin, peptides and silyl compounds used in the synthesis of silylated peptides, the synthesis of silylated peptides, and silyl compounds. It will be described in detail from the viewpoint of the application of the cosmetic base material comprising the modified peptide.

[Structure and Properties of Silylated Peptide] The silylated peptide of the present invention contains 50% or more and 75% or less of the total amino groups including the amino groups of the amino acid side chains of the peptide (ie, the terminal amino group and the side of the peptide). 50% or more and 75% or less of the amino group of the chain), the following general formula (I)

[0014]

[Chemical 4]

[In the formula, R ¹ , R ² and R ³ represent a methyl group or a hydroxyl group, and these R ¹ , R ² and R ³ may be the same or different. a is 1 or 3
Which is a covalently bonded functional group containing only one silicon atom represented by
The following general formula (III)

[0016]

[Chemical 5]

[Wherein R ⁶ , R ⁷ and R ⁸ represent a methyl group, a methoxy group, an ethoxy group, a hydroxyl group or a halogen atom, and these R ⁶ , R ⁷ and R ⁸ may be the same,
It may also be different. a is 1 or 3] and is obtained by reacting a silyl compound represented by
A typical example thereof is the following general formula (II)

[0018]

[Chemical 6]

[In the formula, R ¹ , R ² and R ³ represent a methyl group 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 group other than R ⁴ , and a
Is 1 or 3, m is 0 to 50, n is 0 to 50, m + n
Is 1 to 50 (however, m and n only indicate the number of amino acids and do not indicate the order of amino acid sequences)].

This silylated peptide is obtained by reacting hydrophilic peptides with a hydrophobic silyl compound. Since the reaction is carried out in water, the alkoxy group or halogen atom bonded to the silicon atom is It is water-soluble after the reaction because it is replaced with water and all or part of it becomes hydroxyl groups. Furthermore, since the molecular structure of the silyl functional group portion is smaller than that of the hydrophilic polypeptide portion, the solubility of the reaction product in water is improved. As a result, storage stability in water is improved.

The silyl compound represented by the general formula (III) is
As it contains only one silicon atom, it is commonly used in cosmetics as a high molecular weight silicone (degree of polymerization 100-1000).
Although it is inferior in film-forming property to itself, it reacts with the terminal amino group of the peptide or the amino group of the amino acid side chain, so several silyl groups will be bonded to one peptide chain. It can exhibit the same effects as those of high molecular silicone such as excellent extensibility, friction reducing property, luster and gloss imparting action, and water repellency imparting action. at the same time,
It is possible to exert a sorption action of the peptide on the hair, a volume increase of the hair accompanied therewith, an application of elasticity (tension), a protective action by film formation, a moisturizing action and the like.

In the silylated peptide of the present invention, the functional group containing only one silicon atom bonded to the amino group of the peptide (referred to as a silyl functional group for simplification) is 50% or more and 75% or less of the above amino group. The reason is that when it is less than 50%, the properties based on the silyl compound are not sufficiently exhibited, and when it is more than 75%, the hydrophobicity increases and the hydrophilicity decreases, and the storage stability deteriorates. The chain length of the peptide portion also plays a role in exerting the characteristics of the silyl functional group and the silyl compound. This will be described in detail later.

In the silylated peptide represented by the general formula (II), R ¹ , R ² and R ³ are specified as a methyl group or a hydroxyl group so that the silylated peptide can maintain water solubility. This is because a is specified as 1 or 3 in order to ensure water solubility and stability.

In the silylated peptide represented by the general formula (II), R ⁴ is a 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 include lysine, arginine, histidine, hydroxylysine and the like. R ⁵ represents a side chain of an amino acid other than R ⁴ , and examples of such an amino acid include glutamic acid, aspartic acid, alanine, serine, threonine, valine, methionine, leucine, isoleucine, tyrosine, and phenylalanine. Can be mentioned.

In the silylated peptide represented by the general formula (II), m is 0 to 50, preferably greater than 0 and 1
It is 0 or less, n is 0 to 50, preferably 2 to 40, and m + n is 1 to 50, preferably 3 to 40, for the following reason.

That is, when m is larger than the above range, the number of silyl compounds bonded to the amino group of the side chain is increased, and the sorption action on the original hair or skin of the peptide is decreased, and n is larger than the above range. Then, the ratio of the silyl compound portion to the peptide portion becomes small, and the effect of the silyl compound cannot be sufficiently exerted, and m + n
When the value is larger than the above range, the sorption property as a peptide is reduced as compared with a low molecular weight peptide, and moreover, it easily aggregates during storage, and the storage stability as a cosmetic is reduced. The above m, n and m + n are theoretically integers, but 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 value is an average value. The peptide moiety in the silylated peptide represented by the general formula (II) is based on an amino acid, a peptide, an amino acid or an ester of a peptide, as will be described later in detail in the section of peptides.

[Action of Silylated Peptide on Hair and Skin] When the silylated peptide represented by the above general formula (II) is incorporated into a hair cosmetic product, it imparts luster and moisturization to the hair to make the hair smooth, It also improves combability of hair and prevents split ends and cut hair. For example, when conventional silicone oil is used to impart firmness to hair, a high molecular weight one is required, but once the high molecular weight silicone is attached, it is difficult to remove, and therefore chemicals such as perm, bleach, and hair dye are required. In addition to being difficult to carry out, it reduces the sorption of peptides and cationized polymers on the hair.

However, a silylated peptide is a peptide having a low-molecular-weight silyl group bonded to the peptide portion, and since it sorbs on hair by a normal peptide sorption mechanism, it is washed with a detergent containing no peptide. As a result, the silylated peptide can be reversibly desorbed from the hair, and the above-mentioned adverse effects do not occur.

Further, since the high molecular silicone is hydrophobic, it is sorbed on hair with little damage, that is, hair having a strong hydrophobic property, but the hydrophilic group is exposed on the surface due to the damage and the hydrophilic property is imparted. It is said that it is difficult to sorb to hair that has become stronger, but in that respect, peptides easily sorb to damaged hair, and silylated peptides sorb silyl groups to damaged hair via the peptide moiety. It is possible to restore the strength and feel of damaged hair.

When the silylated peptide represented by the above general formula (II) is incorporated into skin cosmetics, it sorbs to the skin, imparts luster and moisture to the skin, and makes the skin smooth.

Moreover, since this silylated peptide has a peptide portion and a silyl compound portion having a water-insoluble property in one substance, unlike the conventional mixture of silicone oil and polypeptide, the silyl compound portion is different. Has improved sorption on hair and skin, and has good emulsion stability,
It can also be used as an emulsifier for cosmetics, an emulsion stabilizer, and a penetrant.

[Peptides] The peptides serving as a group constituting the peptide portion in the silylated peptide represented by the general formula (II) include amino acids, peptides, amino acids or esters of 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-phosphoserine, citrulline and the like.

Examples of the peptides include natural peptides, synthetic peptides, hydrolyzed peptides obtained by partially hydrolyzing a protein (protein) with an acid, an alkali or an enzyme.

Examples of natural peptides include glutathione, bacitracin A, insulin, glucagon,
Oxytocin, vasopressin and the like, and synthetic peptides include, for example, polyglycine, polylysine,
Examples thereof include polyglutamic acid and polyserine.

As a protein source of hydrolyzed peptide,
Collagen (including its modified gelatin), keratin, silk fibroin, sericin, casein, conchiolin, elastin, egg yolk protein of eggs such as chicken, protein derived from animals such as egg white protein, soybean, wheat, beer meal, Plant-derived materials such as corn, rice (rice bran), and potato proteins, and yeasts isolated from Saccharomyces sp., Candita sp., Endomycopsis sp., And yeasts called so-called beer yeast and sake yeast. Examples include proteins, microbial origin such as mushrooms (basidiomycetes) and proteins separated from Chlorella.

The hydrolyzed peptide used for silylation can be obtained by hydrolyzing the above protein with an acid, an alkali or an enzyme.
By appropriately selecting the amount of acid, alkali or enzyme to be used, reaction temperature and reaction time, the degree of amino acid polymerization of the resulting hydrolyzed protein can be set to a preferable value of 1 to 50.

For acid hydrolysis of proteins, for example, inorganic acids such as hydrochloric acid, sulfuric acid, phosphoric acid, nitric acid and hydrobromic acid, and organic acids such as acetic acid and formic acid are used. For alkaline hydrolysis of proteins, inorganic alkalis such as sodium hydroxide, potassium hydroxide, lithium hydroxide, barium hydroxide, sodium carbonate, potassium carbonate and lithium carbonate are used.

When the protein is enzymatically decomposed, acidic proteolytic enzymes such as pepsin, proctase A and proctase B, and neutral or alkaline proteolytic enzymes such as papain, bromelain, thermolysin, trypsin, pronase and chymotrypsin are used. . Further, a fungal neutral or alkaline proteolytic enzyme such as subtilisin and staphylococcus protease can also be used.

Examples of the amino acid or peptide ester include esters with a hydrocarbon alcohol having 1 to 20 carbon atoms in the carboxyl group of the above amino acid or peptide, such as methyl ester, ethyl ester, propyl ester, isopropyl ester and butyl. Ester, lauryl ester, cetyl ester, 2-ethylhexyl ester, 2-hexyldecyl ester,
Stearyl ester etc. are mentioned.

In this silylated peptide, the amino acid content having an amino group in the side chain and the molecular weight of the peptide portion are important points in order to exert the characteristics of the silyl compound.
That is, in order to bring out the characteristics of the silyl compound strongly, it is sufficient to use a peptide having a small molecular weight and a large amount of amino acids having an amino group in the side chain. Conversely, the characteristics of the peptide portion are emphasized and When it is desired to add, a peptide having a low amino acid content having an amino group in the side chain and having a high molecular weight may be used.
However, in the case of a low molecular weight peptide having a large number of amino acids having an amino group in the side chain, if the number of silyl functional groups attached is extremely large, the hydrophilicity decreases, the storage stability deteriorates, and the original hair of the peptide is lost. The sorption effect of is reduced. On the contrary, when the introduction of the silyl functional group into the peptide portion is too low, the characteristics of the silyl compound are not sufficiently exhibited.

In general, no natural protein has an amino group having an amino group at the end of its side chain, that is, a total content of lysine, arginine, hydroxylysine, etc., exceeding 50 mol%. Does not cause the above problems due to too high introduction rate of the silyl functional group. On the contrary, when the introduction rate of the silyl functional group is low, the characteristics of the silyl compound cannot be sufficiently exhibited,
Therefore, the introduction rate of silyl functional groups to amino groups is 50%.
The above is required, but the introduction rate of the silyl functional group into the amino group of the peptide is such that the degree of amino acid polymerization of the peptide is 1 to 10
50-65%, the degree of amino acid polymerization of peptide is 10-3
It is preferable that the introduction rate is 0 to 60 to 70%, the amino acid polymerization degree of the peptide is 30 to 50, and the introduction rate is 65 to 75%.

That is, when the amino acid polymerization degree of the peptide and the introduction rate of the silyl functional group are within the above ranges, the characteristics of the silyl compound can be sufficiently exhibited without reducing the sorption action of the peptide on hair or skin. In addition, since the hydrophilic property of the silylated peptide is sufficiently maintained, it does not cause turbidity or precipitation due to agglomeration of the silylated peptide during storage even when incorporated into a water-soluble cosmetic product. . However, when the introduction ratio of the silyl functional group exceeds the above range, the ratio of the silyl functional group in the molecule of the silylated peptide increases, and when the cosmetic is compounded, the silylated peptide may be added depending on the compounding amount and other compounds. May associate with each other to cause layer separation or turbidity. When the introduction rate of the silyl functional group is less than the above range, the characteristics of the silyl functional group cannot be sufficiently exhibited.

When the silylated peptide is blended in hair cosmetics or skin cosmetics, the degree of amino acid polymerization of the peptide should be 2 to 2, considering the sorption property of the peptide on hair and skin, the film-forming action and the permeability. 50 is preferable,
Particularly, 3 to 30 is preferable.

[Silyl Compound] As the silylating agent for silylating the above peptides, for example, a silyl compound represented by the above general formula (III) is preferably used. As the silyl compound represented by, a commercially available compound called a silane coupling agent can be used. For example, TSL8355 and TSL8350 manufactured by Toshiba Silicone Co., Ltd. (both are
Trade name), Toray Dow Corning Silicone SH6040 (trade name), Shin-Etsu Chemical Co., Ltd. KMB
403, KMB402 (all are trade names), A-187 (trade name) manufactured by Nippon Unicar Co., Ltd., and the like correspond to this.

In the above general formula (III), R ⁶ , R ⁷ ,
R ⁸ is specified as a methyl group, a methoxy group, an ethoxy group, a hydroxyl group or a halogen atom, in the reaction with peptides, they become a methyl group or a hydroxyl group,
This is to allow the silylated peptide to have water solubility.

[Synthesis of Silylated Peptide] The reaction between the peptides and the silyl compound represented by the general formula (III) is carried out by first stirring the silyl compound in water at 30 to 50 ° C. for 5 to 20 minutes. It is carried out by converting an alkoxy group or a halogen atom bonded to a silicon atom into a hydroxyl group, dropping the hydroxylated silyl compound into peptides, and bringing them into contact with each other.

In the above reaction, the peptides were 30 to 5
The aqueous solution is preferably about 0% by weight, and the dropping of the hydroxylated silyl compound is preferably completed in 30 minutes to 5 hours.

Since the reaction proceeds on the basic side, it is necessary to add an alkaline solution such as sodium hydroxide or potassium hydroxide to the peptide solution to adjust the pH to 8 to 11, particularly 9 to 10. The reaction proceeds even at room temperature, but the higher the temperature, the faster the reaction rate. However, since the hydrolysis of the silyl compound is promoted when the temperature rises in a high pH state, it is preferably at most 70 ° C. or lower, and particularly preferably 40 to 60 ° C.

The progress and completion of the reaction can be confirmed by measuring the amount of amino nitrogen of the peptides in the reaction by the Van Slyke method.

After the completion of the reaction, the reaction solution is neutralized and then appropriately concentrated, and purified by ion exchange resin, dialysis membrane, electrodialysis, gel filtration, ultrafiltration, etc., and is left as a liquid or powdered to prepare a hair cosmetic product. It is also used in skin cosmetics.

[Use of Cosmetic Base Material Consisting of Silylated Peptide] Examples of cosmetics in which the cosmetic base material comprising a silylated peptide is blended include shampoo, hair rinse, split ends coat, first and second permanent wave agents. Agent, hair cream, hair conditioner, set lotion, hair color, hair treatment rinse,
Liquid hair styling products, hair packs, hair cosmetics such as hair nourishing agents, hair lotions, after-shave lotions, shaving foams, burnishing creams, cleansing creams, emollient creams, moisturizing creams, hand creams, facial creams, and other creams, depilatories. It can be used for various cosmetics such as face packs, emulsions, face wash, body shampoo, various soaps, makeup products and sunscreen products.

The content of the cosmetic base material comprising the silylated peptide is 0.1 to 30% by weight, preferably 1 to 20% by weight in the cosmetic product. That is, when the amount of the silylated peptide compounded in the cosmetic is less than the above range, the effect of imparting luster and moisture to the hair, protecting the hair, improving combability is not sufficiently expressed, Further, even if the amount of the silylated peptide compounded in the cosmetic is more than the above range, the effect accompanying it is not observed, and rather excessive silylated peptide may be sorbed on the hair or skin to cause stickiness. There is.

The components which can be added to the above-mentioned cosmetics in combination with a cosmetic base material comprising a silylated peptide include
For example, sodium lauryl sulphate, alkyl sulphates such as ethanol lauryl sulphate, polyoxyethylene (2EO) lauryl ether sulphate triethanolamine (where EO is ethylene oxide and the value before EO is the number of moles of ethylene oxide added). ), Polyoxyethylene (3EO) alkyl (any of C11 to C15 or a mixture of two or more) polyoxyethylene alkyl ether sulfate such as sodium ether sulfate, sodium laurylbenzenesulfonate, trilaurylbenzenesulfonate. Alkylbenzene sulfonates such as ethanolamine, polyoxyethylene (3E
O) Polyoxyethylene alkyl ether acetate such as tridecyl ether acetic acid, sodium coconut oil fatty acid-L-glutamate, N-acyl amino acid salt such as coconut oil fatty acid sarcosin sodium, collagen, keratin, fibroin, casein, soybean, wheat , Protein hydrolyzate derived from plants and animals such as corn, or protein hydrolyzate derived from microorganisms such as yeast and mushrooms having 8 to 20 carbon atoms.
Hydrolyzed protein or its salt acylated with fatty acid of fatty acid, hydrogenated coconut oil fatty acid sodium glycerin sulfate, polyoxyethylene alkyl (C12-15)
Anionic surfactants such as sodium ether phosphate (8-10 EO), sodium polyoxyethylene cetyl ether phosphate, sodium coconut oil fatty acid methyl taurate, sodium coconut oil fatty acid isethionate, distearyl dimethyl ammonium chloride, stearyl trimethyl chloride A cationic surfactant such as ammonium, 2-
Alkyl (C12-C15) -N-carboxymethyl-N-hydroxyethyl imidazolinium betaine, undecyl hydroxyethyl imidazolinium betaine sodium, N-coconut oil fatty acid acyl-L-arginine ethyl-DL-pyrrolidone carboxylic acid Salt, coconut oil fatty acid amide propyl betaine, N-alkyl (C12 to C1
8) Amphoteric surfactants such as dimethylaminoacetic acid betaine, polyoxyethylene alkyl (C12-14)
Nonionic surfactants such as ether (7EO), polyoxyethylene oleyl ether, polyoxyethylene nonylphenyl ether, alkyl glucoside, alkyl polyglycoside, cationic polymer such as cationized cellulose, cationized hydroxyethyl cellulose, amphoteric polymer, anion Polymers such as organic polymers, isostearic acid diethanolamide, thickeners such as lauric acid diethanolamide, animal and plant extracts, polysaccharides or derivatives thereof, propylene glycol, 1,3-butylene glycol, wetting agents such as glycerin, ethanol, Lower alcohols such as methanol and propyl alcohol, sodium L-aspartate, DL-alanine, glycine, L-arginine, L-
Examples thereof include amino acids such as cysteine, and other components may be appropriately added within the range not impairing the effects of the present invention.

The silylated peptide represented by the above general formula (II) is used in combination with a chain or cyclic methylpolysiloxane, methylphenylpolysiloxane, or a silicone oil such as amino-modified silicone oil.
It is possible to improve the emulsion stability of the silicone oil and increase the action of the silicone oil.

[0056]

EXAMPLES Next, the present invention will be described more specifically with reference to examples. However, the present invention is not limited to only those illustrated in these examples. In the following examples and the like,% indicating the concentration of the solution is% by weight.

Example 1 Hydrolyzed collagen (a hydrolyzed product of collagen, the average value of m = 2, the average value of n = 18, the average value of m + n = 2
50 g of a 30% aqueous solution of 0) (10.6 mmol as the stoichiometric number of moles obtained by measurement of amino nitrogen)
A 20% aqueous sodium hydroxide solution was added dropwise to adjust the pH to 9.
5 and warmed to 55 ° C.

On the other hand, as the silylating agent, in the general formula (III), R ⁶ ═CH ₃ , R ⁷ ═OCH ₃ and R ⁸ ═OCH
_In 2.3, 15% of 2.3 g of a silyl compound with a = 3 (1.0 equivalent to the amount of amino nitrogen of hydrolyzed collagen) in water
Dissolve to form an aqueous solution, adjust the pH to 3.5 with dilute hydrochloric acid, continue stirring at 50 ° C for 15 minutes, and remove the methoxy group (-
OCH ₃ ) was hydrolyzed and converted to hydroxyl groups.

While stirring the above-mentioned hydrolyzed collagen solution at 55 ° C., an aqueous solution of a silyl compound converted into a hydroxyl group was added dropwise thereto over 30 minutes. 55 after the dropping
Stirring was continued for additional 5 hours at 0 ° C. to complete the reaction.

After completion of the reaction, the introduction ratio of the silyl functional group into the amino nitrogen of the hydrolyzed collagen of the silyl functional group was determined by measuring the amino nitrogen, and the introduction ratio of the silyl functional group was 67%.

After neutralizing the reaction solution with dilute hydrochloric acid, desalting with an electrodialyzer, adjusting the pH to 6.5, and then concentrating to adjust the concentration, the reaction product (silylated hydrolyzed collagen ) 63 g of a 20% strength aqueous solution was obtained.

Example 2 Hydrolyzed wheat protein (a hydrolyzate of wheat protein,
50 g of a 30% aqueous solution of an average value of m = 1.2, an average value of n = 8.8, an average value of m + n = 10 (15 mmol as a stoichiometric number of moles obtained by measurement of amino nitrogen) PH of 20% sodium hydroxide aqueous solution
It was brought to 9.5 and warmed to 55 ° C.

On the other hand, as the silylating agent, in the general formula (III), R ⁶ = Cl, R ⁷ = CH ₃ , R ⁸ = Cl, and a
= 3 g of silyl compound (0.9 equivalent to the amount of amino nitrogen of hydrolyzed wheat peptide) was dissolved in water to form a 15% aqueous solution, and stirring was continued for 15 minutes to directly bond to a silicon atom. The Cl atom present in the product was converted into a hydroxyl group.

The above hydrolyzed wheat protein aqueous solution is heated to 55 ° C.
With stirring, the aqueous solution of the silyl compound converted into the hydroxyl group was added dropwise thereto over 1 hour. After the dropping, 55 ℃
The reaction was completed by continuing stirring for 5 hours.

The reaction solution was neutralized with dilute hydrochloric acid, then desalted by electrodialysis, concentrated and adjusted in concentration to obtain 55 g of an aqueous solution having a reaction product (silylated hydrolyzed wheat protein) concentration of 20%. . The introduction rate of the silyl functional group was 62%.

Example 3 Instead of hydrolyzed collagen, hydrolyzed keratin (a hydrolyzed wool, mean value of m = 0.6, mean value of n = 4.
4, 50 g of 30% aqueous solution (average value of m + n = 5) (42 mmol as stoichiometric mole number obtained by measurement of amino nitrogen) was used as a silylating agent and represented by the general formula (II
In I), R ⁶ = CH ₃ , R ⁷ = OC ₂ H ₅ , R ⁸ =
The reaction product (silylated hydrolyzate) was used in the same manner as in Example 1 except that 75 g (0.8 equivalent to the amount of amino nitrogen of hydrolyzed keratin) of a silyl compound of a = 3 was used in OC ₂ H _5. 58 g of an aqueous solution having a decomposed keratin concentration of 20% was obtained. The introduction rate of the silyl functional group was 59%, and the ethoxy group (OC ₂ H ₅ ) directly bonded to the silicon atom in the silyl compound represented by the general formula (III) was converted into a hydroxyl group during the above reaction. It had been.

Example 4 Hydrolyzed soybean protein in place of hydrolyzed collagen (hydrolyzate of soybean protein, mean value of m = 0.5, mean value of n = 5.5, mean value of m + n = 6) Of 30% aqueous solution (18.4 mmol as the stoichiometric number of moles obtained by measurement of amino nitrogen) was used as a silylating agent in the general formula (III): R ⁶ ═OCH ₃ , R ⁷
= OCH ₃ , R ⁸ = OCH ₃ , and 3.4 g of the silyl compound of a = 1 (0.9 equivalents to the amount of amino nitrogen of hydrolyzed soybean protein) was used in the same manner as in Example 1. Thus, 53 g of an aqueous solution having a reaction product (silylated hydrolyzed soybean protein) concentration of 20% was obtained. The introduction rate of the silyl functional group was 60%, and the methoxy group directly bonded to the silicon atom in the silyl compound represented by the general formula (III) was converted into the hydroxyl group during the above reaction.

Example 5 Hydrolyzed yeast protein instead of hydrolyzed collagen (yeast protein hydrolyzate, mean value of m = 1.2, mean value of n = 6.8, mean value of m + n = 8) Of 30% aqueous solution (30 mmol as stoichiometric number of moles obtained by measurement of amino nitrogen) was used as a silylating agent in the general formula (III): R ⁶ ═CH ₃ , R ⁷ ═OC
₂ H ₅ , R ⁸ = OC ₂ H ₅ , and 5.3 g of the silyl compound of a = 3 (0.8 equivalents to the amount of amino nitrogen of hydrolyzed yeast protein) was used, and in the same manner as in Example 1. Similarly, 48 g of an aqueous solution having a reaction product (silylated hydrolyzed yeast protein) concentration of 20% was obtained. The introduction rate of the silyl functional group was 57%, and the ethoxy group directly bonded to the silicon atom in the silyl compound represented by the general formula (III) was converted into the hydroxyl group during the above reaction.

Example 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 the silylating agent, in the general formula (III), R ⁶ ═OCH ₃ , R ⁷ ═OCH ₃ and R ⁸ ═OC.
With H ₃ , 17.8 g of a silyl compound with a = 3 (0.7 equivalents relative to the amount of amino nitrogen of L-lysine hydrochloride) was added to 15 parts of water.
% Aqueous solution, the pH was adjusted to 3.5 with dilute hydrochloric acid, and stirring was continued at 50 ° C. for 15 minutes to hydrolyze the methoxy group to convert it into a hydroxyl group.

While the above L-lysine hydrochloride aqueous solution was stirred, the silyl compound aqueous solution converted into hydroxyl group was added dropwise thereto over 30 minutes. After completion of the dropping, stirring was continued at 55 ° C. for another 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%, indicating that not only the amino group at the terminal of the peptide but also the side chain. It was found that the amino group of was also reacted. After neutralizing the reaction solution with dilute hydrochloric acid, desalting and purifying with an electrodialyzer, adjusting the pH to 6.5, and then concentrating to adjust the concentration, the reaction product (silylated L-lysine) concentration 118 g of a 15% aqueous solution was obtained.

Example 7 Glycyl-L-alanine 10 instead of L-lysine hydrochloride
g (molecular weight 146.1, 68.4 mmol) is used as a silylating agent in the general formula (III), R ⁶ = C
In _{^{H 3, R 7 = OCH 3}} , R 8 = OCH 3, except using (0.9 equivalents relative to amino nitrogen of glycyl -L- alanine) a = 1 13.5g of the silyl compound, In the same manner as in Example 6, the reaction product (silylated glycyl-L
-Alanine) 104 g of an aqueous solution with a concentration of 15% was obtained. The introduction rate of the silyl functional group is 55%, and the introduction ratio of the general formula (III) is
In the silyl compound represented by, the methoxy group directly bonded to the silicon atom was converted into a hydroxyl group during the above reaction.

Comparative Example 1 The same silyl compound as hydrolyzed collagen and the same silyl compound as in Example 1 were used, except that the amount of the silyl compound was changed to 1.6 g (0.7 equivalents to the amount of amino nitrogen of hydrolyzed collagen). In the same manner as in Example 1, 45 g of a 20% aqueous solution of silylated hydrolyzed collagen was obtained. The introduction rate of the silyl functional group was 48%.

Comparative Example 2 Using the same hydrolyzed wheat protein and the same silyl compound as in Example 2, the amount of the silyl compound was changed to 4.5 g (1.3 equivalents to the amount of amino nitrogen in the hydrolyzed wheat protein). Other than the above, the same operation as in Example 2 was carried out to obtain 74 g of a 20% aqueous solution of silylated hydrolyzed wheat protein. The introduction rate of the silyl functional group was 77%.

Comparative Example 3 The same silyl compound as hydrolyzed keratin as in Example 3 was used, and the amount of the silyl compound was changed to 11.3 g (1.2 equivalents to the amount of amino nitrogen of hydrolyzed keratin). In the same manner as in Example 3, 80 g of a 20% aqueous solution of silylated hydrolyzed keratin was obtained. The introduction rate of the silyl functional group was 78%.

Comparative Example 4 Using the same hydrolyzed soybean protein and the same silyl compound as in Example 4, the amount of silyl compound was changed to 2.3 g (0.6 equivalent to the amount of amino nitrogen in hydrolyzed soybean protein). 43 g of a 20% aqueous solution of silylated hydrolyzed soybean protein obtained in the same manner as in Example 4 except for the above. The introduction rate of the silyl functional group was 47%.

Comparative Example 5 Using the same hydrolyzed yeast protein and the same silyl compound as in Example 5, the amount of the silyl compound was changed to 8.6 g (1.3 equivalents to the amount of amino nitrogen in the hydrolyzed yeast protein). Other than the above, the same operation as in Example 5 was carried out to obtain 81 g of a 20% aqueous solution of silylated hydrolyzed yeast protein. The introduction rate of the silyl functional group was 78%.

Comparative Example 6 Using the same L-lysine hydrochloride and the same silyl compound as in Example 6, the amount of the silyl compound was adjusted to 80.5 g (1.2 equivalents based on the amount of amino nitrogen in L-lysine hydrochloride). The same operation as in Example 6 was carried out except that it was changed to obtain 173 g of a 15% aqueous solution of silylated L-lysine. The introduction rate of the silyl functional group was 77%.

Comparative Example 7 Using the same glycyl-L-alanine and the same silyl compound as in Example 7, the amount of silyl compound was 15 g (glycyl-L).
The same operation as in Example 7 was carried out except that the amount was changed to 0.6 equivalent to the amino nitrogen amount of -alanine to obtain 105 g of a 15% aqueous solution of silylated glycyl-L-alanine. The introduction rate of the silyl functional group was 44%.

[Storage Stability of Silylated Peptide] The aqueous solutions of the silylated peptides obtained in Examples 1 to 7 and Comparative Examples 1 to 7 were kept at room temperature for 90 days (however, 10 to 25 ° C.).
The presence or absence of a precipitate generated when the sample was stored in was visually examined. The evaluation criteria are as follows.

Evaluation criteria ++: Very large amount of precipitate ++: Large amount of precipitate +: Slight precipitation or turbidity is observed −: No precipitate or turbidity is observed

The results are shown in Tables 1-2. In addition, Table 1
In Table 2, the types of peptides used in the synthesis of the silylated peptides of Examples and Comparative Examples are also shown.

[0084]

[Table 1]

[0085]

[Table 2]

As shown in Tables 1 and 2, the silylated peptides prepared in Examples 1 to 7 did not cause turbidity or precipitate when stored at room temperature. On the other hand, in Comparative Examples, Comparative Examples 1, 4 and 7 in which the introduction rate of the silyl functional group was low did not generate turbidity or precipitate, but Comparative Examples 2, 3, 5 and in which the introduction rate of the silyl functional group was high. 6 produced turbidity,
Particularly, the turbidity of Comparative Examples 3 and 6 in which a large amount of silyl functional group was introduced into a peptide having a low degree of amino acid polymerization was severe.

[PH Stability of Silylated Peptides] The pH stability of the silylated peptides prepared in Examples 1 to 7 and Comparative Examples 1 to 7 was examined. That is, a 10% aqueous solution of silylated peptide was adjusted to pH 3, 4, 5, 7, 9, 10 with 6N hydrochloric acid or 20% sodium hydroxide, and the pH was adjusted to 24 at room temperature.
The presence or absence of precipitates and turbidity after leaving for a while was visually confirmed. The results are shown in Tables 3-4. The evaluation criteria are the same as those for storage stability.

[0088]

[Table 3]

[0089]

[Table 4]

As shown in Tables 3 to 4, the silylated hydrolyzed keratin of Example 3, the silylated hydrolyzed yeast protein of Example 5 and the silylated glycyl-L-alanine of Example 7 were cloudy at pH 3. The silylated L-lysine of Example 6 produced turbidity at pH 4 or lower, while other silylated peptides showed no turbidity or precipitate within the tested pH range.

Also, with the silylated hydrolyzed keratin of Example 3, the silylated hydrolyzed yeast protein of Example 5 and the glycyl-L-alanine of Example 7, no turbidity or precipitate was observed at pH 4 or higher. Since hydrolyzed keratin and hydrolyzed yeast protein contain many amino acids having an amino group at the end of the side chain, there are many silyl functional groups bonded to the peptide part, and hydrophobic properties are likely to appear,
It is considered that turbidity occurred at low pH. In addition, since two silyl functional groups are bonded to one lysine in silylated L-lysine, it is considered that turbidity was caused at low pH, and that in silylated glycyl-L-alanine, the molecular weight of the peptide was It is considered that the silyl functional group was likely to show hydrophobicity due to its small size, resulting in turbidity.

On the other hand, in the comparative example, the silylated hydrolyzed collagen of Comparative Example 1, the silylated hydrolyzed soybean protein of Comparative Example 4, and the silylated hydrolyzed glycyl of Comparative Example 7 having a low introduction rate of silyl functional groups were used. -L-alanine is
No turbidity or precipitate was observed within the tested pH range, but the silylated hydrolyzed keratin of Comparative Example 3 and Comparative Example 6
The silylated and hydrolyzed L-lysine of (3) began to become turbid at around pH 5, and completely gelled at pH 3. In addition, even in the silylated hydrolyzed yeast protein of Comparative Example 5, turbidity occurs at a pH of 4 or less, and when the silyl functional group is introduced into a low-molecular weight peptide at a high introduction rate, it is clear that stability at low pH is poor. Met.

[Confirmation Test for Enhancement of Tensile Strength of Hair by Silylated Peptide] The confirmation of the enhancement of tensile strength of hair by the silylated peptide was performed in Journal of SCCJ,
vol. 21, No. The measurement was carried out according to the method described in "Hair damage evaluation method (I)" in 2.

In the test, in order to suppress variations in the strength of the hair used as a sample to a low level, hair that had been once decolorized so that the strength of the hair was almost constant was used. That is, a hair bundle having a length of 10 cm and a weight of 1 g is immersed in 10 g of a 1: 1 mixed solution of 10% hydrogen peroxide water and 10% ammonia water for 10 minutes for decolorization, rinsed with ion-exchanged water, and then dried. And used for the test.

As the test liquid, a 5% aqueous solution of silylated hydrolyzed collagen obtained in Example 1 and Comparative Example 1 and a 5% aqueous solution of silylated hydrolyzed keratin obtained in Example 3 and Comparative Example 3 were used. Using the above, the above-mentioned decolorized hair bundle was immersed at 40 ° C. for 5 minutes. After the immersion, it was thoroughly rinsed with ion-exchanged water and dried with a hair dryer. Do this operation 3
After repeating 30 times, 30 hairs were extracted from this hair bundle and subjected to a tensile strength test.

In the tensile strength test, the central area (5 cm from the end) of each hair is measured with a micrometer to measure its major axis and minor axis, and the cross-sectional area is calculated. Then, the tensile strength of this section is measured by a tensile strength tester [Fudo Kogyo] Rheometer manufactured by Co., Ltd.], and the tensile strength per cross-sectional area was calculated.

For comparison, untreated hair that had been only decolorized and hydrolyzed collagen (average value of m + n = 2)
The tensile strength of hair similarly treated with a 5% aqueous solution of 0) and a 5% aqueous solution of hydrolyzed keratin (average value of m + n = 5) was measured. The results are shown in Table 5.

[0098]

[Table 5]

As shown in Table 5, the hair treated with the silylated hydrolyzed collagen of Example 1 had a tensile strength increased by about 9.5% as compared with the untreated hair, and the silylated hydrolyzed keratin of Example 3 was added. About 16 times the hair treated with
% Tensile strength was increased. The hair treated with the silylated hydrolyzed collagen of Example 1 and the hair treated with the silylated hydrolyzed keratin of Example 3 were the same as the hairs not treated with silylated hydrolyzed collagen and hydrolyzed keratin. In comparison, the increase in strength was observed, and it was clear that the silylated peptide was well sorbed on the hair and contributed to the strength recovery of the damaged hair.

On the other hand, the hair treated with the silylated hydrolyzed collagen of Comparative Example 1 had about the same tensile strength as the hair treated with the unsilylated hydrolyzed collagen, and the silylated hydrolyzate of Comparative Example 3 was used. Hair treated with hydrolyzed keratin resulted in slightly lower strength than hair treated with unsilylated hydrolyzed keratin. This is considered to be because the introduction rate of the silyl functional group is low in the silylated hydrolyzed collagen of Comparative Example 1 and it cannot contribute to the strength recovery of hair as much as the silylated hydrolyzed collagen of Example 1. It is considered that in the silylated hydrolyzed keratin of No. 3, the introduction rate of the silyl functional group was too high, and the sorption power of the peptide to hair originally decreased.

[Application Example] Next, an application example in which the cosmetic base material comprising the silylated peptide of the present invention is blended with various cosmetic products will be described. In the application examples, the silylated peptide represented by the general formula (II) is shown by an example number, and the type of silylated peptide is also shown in parentheses after the number. Also, the blending amount is by weight,
Unless otherwise indicated in parentheses, the content is shown as pure content.

Application Example 1 Three types of treatment bases (implementation product 1 and comparative products 1 and 2) having the compositions shown in Table 6 were prepared, and the treatment base and LPG gas were mixed in a weight ratio of 8: 2 in a pressure vessel. It filled in and prepared the treatment mousse agent.

[0103]

[Table 6]

The treatment mousse agents of Example 1 and Comparative Examples 1 and 2 were used for a hair bundle having a length of 10 cm and a weight of 1 g, and were used by 5 female panelists to polish and moisturize their hair.
The combability was evaluated by 5 grades. The evaluation criteria are as follows, and the results are shown in Table 7 as an average value.

Evaluation Criteria 5: Very Good 4: Good 3: Normal 2: Bad 1: Very Bad

[0106]

[Table 7]

As shown in Table 7, the treatment mousse agent of Example 1 containing the silylated hydrolyzed collagen of Example 1 was a silicone oil (dimethyl silicone).
Compared to the treatment mousse agent of Comparative Product 1 containing the above and the treatment mousse agent of Comparative Product 2 containing no silylated hydrolyzed collagen or silicone oil,
The evaluation values were high in both moisturizing properties and combability, and the effect of adding silylated hydrolyzed collagen was clear.

Application Example 2 Three types of shampoos having the compositions shown in Table 8 (Example 2 and Comparative Items 3 to 4) were prepared.

[0109]

[Table 8]

Using the shampoos of Example 2 and Comparative Examples 3 to 4, hair bundles each having a length of 10 cm and a weight of 1 g were washed. 0.5 g of each shampoo was used for washing, and after washing with warm water, it was rinsed with warm water and dried with a hair dryer. After repeating this operation 5 times, the results were applied to 5 female panelists with regard to the gloss, moisturization, smoothness, combability, and feel of the foam (softness and smoothness) at the time of hair washing after application. It was evaluated by the same evaluation criteria. The results are shown in Table 9, and the evaluation value is an average value.

[0111]

[Table 9]

As shown in Table 9, the shampoo of Example 2 containing the silylated hydrolyzed wheat protein of Example 2 was a silicone oil (octamethyltrisiloxane).
Compared to the shampoo of Comparative Product 3 containing the above and the shampoo of Comparative Product 4 containing no silylated hydrolyzed wheat protein or silicone oil, the evaluation values were high in all items, and the silylated hydrolyzed wheat protein was added. The effect was clear.

Application Example 3 Three kinds of first agents for permanent wave (composition products 3 and comparative products 5 to 6) having the compositions shown in Table 10 were prepared.

[0114]

[Table 10]

In the permanent wave processing,
Using a hair bundle having a weight of 1 g and a length of 15 cm as a test hair bundle, and using a 6% sodium bromate aqueous solution as the second agent,
The first and second permanent wave agents of Example 3 and Comparative Examples 5 and 6 were applied to the permanent wave treatment once, three times, and six times, respectively, and the appearance and feel of the hair after treatment were given to five female panelists. Evaluation was made according to the same evaluation criteria as in Application Example 1. The results are shown in Table 11, and the evaluation value is an average value.

[0116]

[Table 11]

As shown in Table 11, in the case of using the first agent for permanent wave of Example 3 containing the silylated hydrolyzed soybean protein of Example 4, a comparative product containing no silylated hydrolyzed soybean protein was used. When using the first agent for permanent wave of No. 5 or when using the first agent for permanent wave of Comparative product 6 in which the silylated hydrolyzed soybean protein of Comparative Example 4 was blended in place of the silylated hydrolyzed soybean protein of Example 4. In comparison, the evaluated values of the appearance and feel of the hair after treatment were high, and the effect of adding the silylated hydrolyzed soybean protein of Example 4 was clear.

Application Example 4 The silylated hydrolyzed keratin obtained in Example 3 was blended to prepare a treatment rinse (Example 4) having the following composition.

Example 3 (silylated hydrolyzed keratin), (20%) 17.5 Cetanol 4.0 Stearyl trimethyl ammonium chloride (29%) 2.0 Distearyl dimethyl ammonium chloride (73%) 1.0 Stearic acid Ethylene glycol (3.0W Ayacol EGS-D manufactured by Seowa Kasei) Stearic acid diethylaminoethylamide (Ayacol amine amide 50E manufactured by Seowa 3.0 Kasei) Diglycerin isostearate (1.5 Ayacor DGMIS manufactured by Seowa Kasei) Propylene glycol 3.0 Paraoxybenzoate / phenoxyethano 0.5ol mixture (SEICEPT G manufactured by SEIWA KASEI CO., LTD.) Fragrance suitable amount Sterilized ion-exchanged water Total 100 Malic acid Adjusted to pH 6.0

When the treatment rinse of Example 4 containing the silylated hydrolyzed keratin of Example 3 above was used for hair, a treatment rinse containing no silylated hydrolyzed keratin of Example 3 [that is, Example No silylated hydrolyzed keratin of 3 was added, but the amount of sterilized ion-exchanged water was increased, and compared to the treatment rinse of the same composition as in Example 4, it moisturized the hair, and had combing and brushing properties. Good and easy hair conditioning.

Application Example 5 The silylated L-lysine obtained in Example 6 was blended to prepare a face wash (Example 5) having the following composition.

Example 6 (silylated L-lysine), (15%) 10.0 Cocoa oil fatty acid hydrolyzed collagen potassium 40.0 (Promois ECP-C, 35% manufactured by Seo Kasei) Cocoa oil fatty acid methyl taurine Sodium (30%) 40.0 Lauric acid diethanolamide 3.0 Polyethylene glycol monostearate 4.5 Polyethylene glycol dioleate 4.0 Paraoxybenzoic acid ester / phenoxyethano 0.5ol Mixture (Seiwacept Co., Ltd.) G) Fragrance suitable amount Sterilized ion-exchanged water Total 100 Malic acid Adjusted to pH 6.0

When the face was washed with the face wash of Example 5 containing the silylated L-lysine of Example 6, the face wash without the silylated L-lysine of Example 6 [that is, that of Example 6] was used. It contains no silylated L-lysine, and the amount of sterilized ion-exchanged water is increased, and compared to the case of using the face wash having the same composition as in Example 5, the skin after use has gloss and moisture, And the skin was smooth.

Application Example 6 Three kinds of body shampoos having the compositions shown in Table 12 (Example 6 and Comparative Examples 7 to 8) were prepared.

[0125]

[Table 12]

The body shampoos of Example 6 and Comparative Examples 7 to 8 were used for 10 panelists (5 men and 5 women).
To use for 1 week (7 times for 7 people
The following criteria were used to evaluate the foam quality (softness and smoothness) during washing and the smoothness and moistness of the skin after washing. The results are shown in Table 13. The evaluation value in Table 13 is the average value of 10 persons.

Evaluation Criteria Best: 2 Next Best: 1 Inferior: 0

[0128]

[Table 13]

As shown in Table 13, when the body shampoo of Example 6 containing the silylated glycyl-L-alanine of Example 7 was used, the foam was soft and smooth on washing, and remained on the skin after use. Compared to the body shampoo of Comparative product 7 containing silicone oil [dimethyl siloxane / methyl (polyoxyethylene) siloxane copolymer], which gives a smoothness and moist feeling, and the body shampoo of Comparative product 8 containing neither of them. It was clear that it was excellent.

Application Example 7 Three types of hair dyes having the compositions shown in Table 14 (Example 8 and Comparative Products 10 to 11) were prepared.

[0131]

[Table 14]

As the second agent, a solution having the following composition was used. [Second agent composition] Stearic acid 1.0 part Glycerin monostearate 1.5 parts Polyoxyethylene oleyl ether (20EO) 1.0 part Hydrogen peroxide solution (35%) 15.5 parts Sterilized ion-exchanged water Total 100 Part

A hair bundle having a weight of 1 g and a length of 15 cm was dyed with each of the hair dyes (first agent) of Example 8 and Comparative Products 10 to 11 and the second agent. For hair dyeing, the first and second agents are mixed in equal amounts, the mixture is applied to the hair bundle, left for 30 minutes, then rinsed with warm water, and then,
It was carried out by washing with a 2% aqueous solution of polyoxyethylene noniphenyl ether. After the hair dyeing treatment, the hair bundle was dried with a hair drier, and the leveling, luster, moisturizing and combing properties of the hair were determined by 10 panelists (6 women, 4 men).
The evaluation criteria are the same as those in Application Example 1.

30 hairs were extracted from each of the hair bundles after dyeing, and the cross-sectional area was measured by measuring the major and minor diameters of the central part (7.5 cm from the end) of these hairs with a micrometer. After the calculation, the tensile strength of that portion was measured by a tensile tester [Rheometer, manufactured by Fudo Kogyo Co., Ltd.] to calculate the tensile strength per cross-sectional area. The results are shown in Table 15.

[0135]

[Table 15]

As shown in Table 15, the hair dye of Example 8 containing the silylated hydrolyzed yeast protein of Example 5 was
Compared to the hair dye of Comparative Product 10 containing silicone oil (dimethylpolysiloxane) and the hair dye of Comparative Product 11 containing no silylated hydrolyzed yeast protein or silicone oil, the hair after dyeing was smoothed. The evaluation values were large in terms of dyeability, luster, moisture and combability.

Regarding the tensile strength, when the hair dye of Example 8 containing the silylated hydrolyzed yeast protein of Example 5 was used, the hair dye of Comparative Example 11 [that is,
Hair dye containing neither silylated hydrolyzed yeast protein nor silicone oil (dimethylpolysiloxane)]
The strength was increased by about 4% as compared with the above, and it was clear that the silylated hydrolyzed yeast protein of Example 5 protected the hair from being damaged by the chemical treatment at the time of dyeing.

[0138]

As described above, the cosmetic base material comprising the silylated peptide of the present invention, when incorporated into a hair cosmetic product, imparts luster and moisture to the hair, improves combability of the hair, shampoo, etc. When added to the cleansing agent, it makes the foam soft and smooth to improve the feel to the skin, and when added to the skin cosmetics, it imparts luster and moisture to the skin and makes the skin smooth.

Further, the cosmetic base material comprising the silylated peptide of the present invention is water-soluble, has excellent pH stability and storage stability in water, and when formulated into an aqueous hair cosmetic product or skin cosmetic product. , No turbidity or precipitation during storage.

─────────────────────────────────────────────────── ─── Continuation of the front page (51) Int.Cl. ⁶ Identification number Reference number within the agency FI Technical indication location A61K 7/09 7/13 (72) Inventor Takashi Adachi 1-2-2 Nunoichi-cho, Higashiosaka-shi, Osaka No. 14 stock company Seiwa Kasei

Claims (3)

[Claims] 1. A peptide having the following general formula (I): [In the formula, R ¹ , R ² and R ³ represent a methyl group or a hydroxyl group, and R ¹ , R ² and R ³ may be the same,
It may also be different. a is 1 or 3], which comprises a silylated peptide covalently bonded with a functional group containing only one silicon atom. 2. The cosmetic base material according to claim 1, wherein the peptide portion of the silylated peptide has a degree of amino acid polymerization of 1 to 50. 3. The silylated peptide has the following general formula (I
I) [Chemical 2] [In the formula, R ¹ , R ² and R ³ represent a methyl group or a hydroxyl group, and R ¹ , R ² and R ³ may be the same,
It may also be 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 group other than R ⁴ , and a represents 1 or 3
, M is 0 to 50, n is 0 to 50, and m + n is 1 to 50 (however, m and n only indicate the number of amino acids, and do not indicate the order of amino acid sequences)]. The cosmetic base material according to claim 1, which is a silylated peptide.