JP3315535B2 - Cosmetic base material - Google Patents

Description

DETAILED DESCRIPTION OF THE INVENTION

[0001]

BACKGROUND OF THE INVENTION 1. Field of the Invention The present invention relates to a cosmetic base comprising a silylated peptide. For more information,
The present invention comprises a silylated peptide in which a functional group containing only one silicon atom in 50% or more and 75% or less of all amino groups of the peptide is covalently bonded, and is water-soluble and incorporated into hair cosmetics and skin cosmetics. , Imparts gloss and moisture to hair, improves combability of hair, and prevents branching of 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, a silicone oil (organic silicone compound) and a polypeptide have been blended into hair cosmetics to provide the excellent extensibility of silicone oil, the effect of imparting gloss and gloss to hair, and the water repellency to hair. Attempts have been made to exert a protective effect by the application, a sorbing effect of the polypeptide on hair, an alleviating effect on skin irritation, a protective effect by film formation, a moisturizing effect, and the like.

[0003] For example, Japanese Patent Publication No. Sho 63-5005 proposes a hair cosmetic containing a hydrophobic silicone oil and a mono-N-long chain acyl basic amino acid lower alkyl ester salt, and Japanese Patent Application Laid-Open No. Sho 63-310812. Has proposed a hair treatment in which methylpolysiloxane or methylphenylpolysiloxane is mixed with hydrolyzed collagen.

[0004] However, silicone oil is originally a hydrophobic (lipophilic) substance, and polypeptide is essentially a hydrophilic substance. Therefore, these are hardly compatible with each other. Lacks emulsion stability,
Because 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 portion that first came into contact with the silicone oil. There was a problem that the oil could not be adhered and the properties of both could not be fully exhibited.

[0005] In order to solve the above-mentioned problems, a compound which combines the characteristics of silicone oil and the polypeptide by reacting a hydrophobic silicone oil with a hydrophilic polypeptide is synthesized. Attempts have been made to eliminate the drawbacks of using silicone oil and polypeptide in combination by using it as a material and to exhibit the properties of silicone oil and the properties of polypeptide (Japanese Unexamined Patent Publication No. 3-223207). No.).

[0006]

However, the peptide-modified silicone derivative disclosed in the above-mentioned Japanese Patent Application Laid-Open No. 3-223207 has a problem in that it has a pH stability and a storage stability in water due to the effect of the silicone portion which is hardly soluble or insoluble in water. However, the hair cosmetics and skin cosmetics are mainly water-soluble, and there is a problem that they become cloudy or precipitate during storage.

In the production of the above-mentioned peptide-modified silicone derivative, a reaction between a water-soluble polypeptide and a water-soluble polypeptide which is hardly soluble or insoluble in water is carried out. Has a problem that a water-soluble organic solvent such as alcohol must be added.

Accordingly, the present invention has both the excellent properties of the silicone compound and the excellent properties of the 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 The inventors of the present invention have conducted intensive studies to achieve the above object, and as a result, have found that 50% or more of all amino groups including amino groups in the amino acid side chain of the peptide are 75% or more.
% Or less, the following general formula (I)

[0010]

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[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 covalently bonded with a functional group containing only one silicon atom represented by the formula is water-soluble, has excellent pH stability and storage stability in water, and has excellent properties of silicone compounds. And the excellent properties of polypeptides, when blending them into hair cosmetics and skin cosmetics,
Gives gloss and moisture to hair, improves combability of hair, and prevents branching of hair, gives gloss and moisture to skin,
In addition, it was found that when used in a cleaning agent such as shampoo, it softens the foam, smoothes hair and skin after use, and does not cause turbidity or sedimentation during storage. The invention has been completed.

The present invention will now be described with reference to the structures and properties of silylated peptides, the effects of silylated peptides on hair and skin, peptides and silyl compounds used in synthesizing silylated peptides, synthesis of silylated peptides, This will be described in detail from the viewpoint of the use of a cosmetic substrate comprising an oxidized peptide.

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

[0014]

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[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
Is a covalently bonded functional group containing only one silicon atom represented by
The following general formula (III)

[0016]

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[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 all of R ⁶ , R ⁷ and R ⁸ may be the same;
They may also be different. a is 1 or 3],
A typical example is the following general formula (II)

[0018]

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[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 a terminal amino group of a basic amino acid having an amino group at a terminal of a side chain; R ⁵ represents an amino group other than R ⁴ ;
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 the amino acid sequence)].

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

The silyl compound represented by the general formula (III) is
Since it contains only one silicon atom, it is generally used in cosmetics as a high-molecular silicone (degree of polymerization: 100 to 1000)
Although it is inferior in film forming properties to itself, it reacts with the terminal amino group of the peptide and the amino group of the amino acid side chain, so that several silyl groups are bonded to one peptide chain, and the silyl compound It can exhibit the same effects as high-molecular silicones, such as excellent extensibility, friction reduction, gloss and gloss imparting effects, and water repellency imparting effects possessed by. at the same time,
The sorbing action of the peptide on the hair, the accompanying increase in the volume of the hair, the addition of tension, the protective action by film formation, the moisturizing action, and the like can be exhibited.

In the silylated peptide of the present invention, the functional group containing only one silicon atom bonded to the amino group of the peptide (for the sake of simplicity, referred to as silyl functional group) should be 50% to 75% of the amino group. The reason is that if it is less than 50%, the properties based on the silyl compound are not sufficiently exhibited, and if it is more than 75%, the hydrophobicity increases, the hydrophilicity decreases, and the storage stability deteriorates. In addition, the chain length of the peptide moiety is also involved in exerting the properties 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 to be a methyl group or a hydroxyl group so that the silylated peptide can maintain water solubility. The reason why a is specified as 1 or 3 is 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 basic amino acids having an amino group at the terminal of lysine include lysine, arginine, histidine, and hydroxylysine. R ⁵ represents a side chain of an amino acid other than R ^4. Examples of such amino acids include glutamic acid, aspartic acid, alanine, serine, threonine, valine, methionine, leucine, isoleucine, tyrosine, and phenylalanine. No.

In the silylated peptide represented by the general formula (II), m is 0 to 50, preferably more than 0 and 1
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 in the side chain increases, and the sorption effect on the hair or skin inherent to the peptide decreases, and n is larger than the above range. Then, the ratio of the silyl compound portion to the peptide portion decreases, and the effect of the silyl compound cannot be sufficiently exhibited.
Is larger than the above range, the sorption property as a peptide is reduced as compared with a peptide having a low molecular weight, and the peptide is easily aggregated during storage, and the storage stability as cosmetics is reduced. The above m, n and m + n are theoretically integers. However, when the peptide portion is a hydrolyzed peptide as described later, the hydrolyzed peptide can be obtained as a mixture of those having different molecular weights. The value will be the average value. The peptide moiety in the silylated peptide represented by the general formula (II) is based on an amino acid, a peptide, or an ester of an amino acid or a peptide, as will be described later in detail with respect to peptides.

[Effect of Silylated Peptide on Hair and Skin] The silylated peptide represented by the general formula (II), when added to hair cosmetics, imparts luster and moisture to hair and smoothes hair. It also improves the combability of hair and prevents split ends and cuts. For example, in the case where hair is given firmness with silicone oil as in the past, a high molecular weight silicone is required, but once the high molecular weight silicone adheres, it is difficult to remove it, so that chemicals such as perm, bleach and hair dyeing are used. In addition to reducing the sorption effect of hair such as peptides and cationized polymers on the hair.

However, since the silylated peptide is a peptide in which a low molecular silyl group is bonded to the peptide portion and is absorbed onto the hair by a normal peptide sorption mechanism, it is washed with a peptide-free detergent. Thereby, the silylated peptide can be reversibly detached from the hair, and the above-mentioned adverse effects do not occur.

Further, since the high molecular silicone is hydrophobic, it sorbs to hair with little damage, that is, hair having a strong hydrophobic property. It is said that it is difficult to sorb to hair that has become stronger, but in that regard, peptides are easy to sorb to damaged hair, and silylated peptides are to sorb silyl groups to damaged hair via the peptide part. To restore the strength and feel of damaged hair.

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

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

[Peptides] The peptides constituting the peptide moiety in the silylated peptide represented by the general formula (II) include amino acids, peptides, and esters of amino acids or peptides.

Examples of the above amino acids include alanine, glycine, valine, leucine, isoleucine, proline, phenylalanine, tyrosine, serine, threonine, methionine, arginine, histidine, lysine, asparagine, aspartic acid, glutamine, glutamic acid, cystine, and 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 or enzymes.

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

As the protein source of the hydrolyzed peptide,
Collagen (including its denatured gelatin), keratin, silk fibroin, sericin, casein, conchiolin, elastin, egg yolk proteins of chickens, egg-derived proteins such as egg white proteins, soybeans, wheat, beer lees, Yeasts derived from plants such as corn, rice (rice bran), and potato proteins, and yeasts isolated from yeasts of the genus Saccharomyces, Candita, and Endomycopsis, and so-called beer yeasts and sake yeasts. Examples thereof include those derived from microorganisms such as proteins, mushrooms (basidiomycetes), and proteins isolated from Chlorella.

The hydrolyzed peptide used in the 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 used, the reaction temperature or the reaction time, the degree of amino acid polymerization of the obtained hydrolyzed protein can be made 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, for example, inorganic alkalis such as sodium hydroxide, potassium hydroxide, lithium hydroxide, barium hydroxide, sodium carbonate, potassium carbonate, and lithium carbonate are used.

For the enzymatic digestion of proteins, acidic or alkaline proteases such as pepsin, proctase A and proctase B, papain, bromelain, thermolysin, trypsin, pronase and chymotrypsin are used. . Bacterial neutral or alkaline proteases such as subtilisin and staphylococcal protease can also be used.

Examples of the ester of the above amino acid or peptide include esters with a hydrocarbon alcohol having 1 to 20 carbon atoms at the carboxyl group of the above amino acid or peptide, for example, methyl ester, ethyl ester, propyl ester, isopropyl ester, butyl ester Esters, lauryl esters, cetyl esters, 2-ethylhexyl esters, 2-hexyldecyl esters,
Stearyl esters and the like can be mentioned.

In this silylated peptide, the content of the amino acid having an amino group in the side chain and the molecular weight of the peptide portion are important in order to exert the characteristics of the silyl compound.
In other words, in order to bring out the characteristics of the silyl compound strongly, a peptide having a small molecular weight and a large amount of amino acids having an amino group in the side chain may be used. When it is desired to add a peptide, a high molecular weight peptide having a small content of amino acids having an amino group in the side chain may be used.
However, in the case of low-molecular-weight peptides having a large amino acid content having an amino group in the side chain, if the number of silyl functional groups to be bound is extremely large, hydrophilicity is reduced, storage stability is deteriorated, and in addition to the peptide's original hair, Sorption effect is reduced. Conversely, if the introduction of the silyl functional group into the peptide moiety is too low, the properties of the silyl compound will not be fully exhibited.

In general, there is no natural protein having an amino group having an amino group at the terminal of a side chain, that is, the total content of lysine, arginine, hydroxylysine and the like exceeds 50 mol%. Does not cause the above-mentioned problem because the introduction ratio of the silyl functional group is too high. Conversely, when the introduction ratio of the silyl functional group is low, the characteristics of the silyl compound cannot be sufficiently exhibited,
Therefore, the introduction ratio of the silyl functional group into the amino group is 50%.
Although the above is necessary, the rate of introduction of the silyl functional group into the amino group of the peptide depends on the degree of amino acid polymerization of the peptide being 1 to 10
And the degree of amino acid polymerization of the peptide is 10 to 3%.
It is preferable that the introduction rate is 0 to 60 to 70%, the degree of amino acid polymerization of the peptide is 30 to 50 and the introduction rate is 65 to 75%.

That is, when the degree of amino acid polymerization of the peptide and the introduction ratio of the silyl functional group are within the above ranges, the characteristics of the silyl compound can be sufficiently exhibited without reducing the sorption effect of the peptide on hair and skin. In addition, since the hydrophilic properties of the silylated peptide are sufficiently maintained, no turbidity or precipitation due to aggregation of the silylated peptide occurs during storage even when blended in water-soluble cosmetics. . 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 incorporated into cosmetics, depending on the amount and other compounds, the silylated peptide may be added. May associate to form a layer separation or turbidity. If the introduction ratio of the silyl functional group is less than the above range, the properties possessed by the silyl functional group cannot be sufficiently exhibited.

When this silylated peptide is incorporated into hair cosmetics or skin cosmetics, the degree of amino acid polymerization of the peptide is 2 to 2 in consideration of the sorption properties of the peptide on hair and skin, film formation and permeability. Preferably it is 50,
Particularly, 3 to 30 is preferable.

[Silyl compound] As a 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 product called a silane coupling agent can be used. For example, TSL8355 and TSL8350 manufactured by Toshiba Silicone Co., Ltd.
(Trade name), SH6040 (trade name) manufactured by Dow Corning Silicone Toray Co., Ltd., KMB manufactured by Shin-Etsu Chemical Co., Ltd.
403, KMB402 (all trade names), A-187 (trade name) manufactured by Nippon Unicar Co., Ltd., etc. 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 because, in the reaction with peptides, when they become a methyl group or a hydroxyl group,
This is so that the silylated peptide can have water solubility.

[Synthesis of Silylated Peptide] The reaction of the peptide with the silyl compound represented by the general formula (III) is performed 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 onto peptides, and bringing them into contact with each other.

In the above reaction, 30 to 5 peptides are used.
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, the pH of the peptide solution must be adjusted to 8 to 11, particularly 9 to 10, by adding an alkaline solution such as sodium hydroxide or potassium hydroxide. The reaction proceeds 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 is increased in a state where the pH is high, the temperature is preferably set to 70 ° C. or less at most, particularly preferably at 40 to 60 ° C.

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

After completion of the reaction, the reaction solution is neutralized, concentrated as appropriate, purified by ion exchange resin, dialysis membrane, electrodialysis, gel filtration, ultrafiltration, etc., and used as a liquid or powdered hair cosmetics. And skin cosmetics.

[Use of Cosmetic Base Made of Silylated Peptide] Cosmetics to which a cosmetic base made of a silylated peptide is compounded include, for example, shampoo, hair rinse, split coat, first agent for permanent wave and second agent for permanent wave. Preparations, hair cream, hair conditioner, set lotion, hair color, hair treatment rinse,
Liquid cosmetics, hair packs, hair cosmetics such as hair tonics and hair restorers, lotions, aftershave lotions, shaving foams, various creams such as vanishing creams, cleansing creams, emollient creams, moisture creams, hand creams, facial cleansers, and depilatory agents It can be used for various cosmetics such as face packs, emulsions, facial cleansers, body shampoos, various soaps, makeup products, sunscreen products and the like.

The amount of the cosmetic base comprising the silylated peptide is preferably 0.1 to 30% by weight, more preferably about 1 to 20% by weight in the cosmetic. That is, when the amount of the silylated peptide in the cosmetic is less than the above range, the effect of imparting gloss and moisture to the hair, protecting the hair, and improving the combability is not sufficiently exhibited, In addition, even if the amount of the silylated peptide in the cosmetic is more than the above range, the effect is not increased, and the excess silylated peptide may sorb to the hair or skin and cause stickiness. There is.

The components which can be added to the above cosmetics in combination with a cosmetic base comprising a silylated peptide include:
For example, alkyl sulfates such as sodium lauryl sulfate and ethanolamine lauryl sulfate, polyoxyethylene (2EO) lauryl ether triethanolamine sulfate (EO is ethylene oxide, and the number before EO indicates the number of moles of ethylene oxide added. Polyoxyethylene (3EO) alkyl (any one or a mixture of two or more of carbon atoms), polyoxyethylene alkyl ether sulfates such as sodium ether sulfate, sodium laurylbenzenesulfonate, trilaurylbenzenesulfonate Alkylbenzene sulfonates such as ethanolamine, polyoxyethylene (3E
O) Polyoxyethylene alkyl ether acetates such as tridecyl ether acetic acid, N-acyl amino acid salts such as coconut oil fatty acid-sodium L-glutamate and sodium coconut oil sarcosine, collagen, keratin, fibroin, casein, soybean, wheat A protein hydrolyzate derived from animals and plants such as corn and yeast or a protein hydrolyzate derived from microorganisms such as mushrooms having 8 to 20 carbon atoms.
Acylated hydrolyzed protein or salt thereof acylated with a fatty acid, hydrogenated coconut oil fatty acid sodium glycerin sulfate, polyoxyethylene alkyl (C12 to C15)
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 Cationic surfactants such as ammonium, 2-
Alkyl (C12-15) -N-carboxymethyl-N-hydroxyethylimidazolinium betaine, undecyl hydroxyethylimidazolinium betaine sodium, N-coconut fatty acid acyl-L-arginineethyl-DL-pyrrolidonecarboxylic acid Salt, coconut oil fatty acid amidopropyl betaine, N-alkyl (C12 to C1)
8) Amphoteric surfactants such as betaine dimethylaminoacetate, polyoxyethylene alkyl (C12-14)
Nonionic surfactants such as ether (7EO), polyoxyethylene oleyl ether, polyoxyethylene nonyl phenyl ether, alkyl glucoside and alkyl polyglycoside; cationic polymers such as cationized cellulose and cationized hydroxyethyl cellulose; amphoteric polymers; anions Synthetic polymers such as hydrophilic polymers, thickeners such as diethanolamide isostearate, diethanolamide laurate, animal and plant extracts, polysaccharides or derivatives thereof, humectants such as propylene glycol, 1,3-butylene glycol, glycerin, ethanol, Lower alcohols such as methanol and propyl alcohol, sodium L-aspartate, DL-alanine, glycine, L-arginine, L-
Amino acids such as cysteine can be mentioned, and other components can be appropriately added in addition to these, as long as the effects of the present invention are not impaired.

The silylated peptide represented by the above general formula (II) can be used in combination with a chain or cyclic silicone oil such as methylpolysiloxane, methylphenylpolysiloxane, or amino-modified silicone oil.
The emulsification stability of the silicone oil can be improved and the action of the silicone oil can be increased.

[0056]

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

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

On the other hand, as a silylating agent, in the general formula (III), R ⁶ ＣＨCH ₃ , R ⁷ ＯOCH ₃ , R ⁸ ＯOCH
_{In step 3} , 2.3 g of a silyl compound having a = 3 (1.0 equivalent to the amount of amino nitrogen in hydrolyzed collagen) was added to 15% of water.
Dissolve so as 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 converted to hydroxyl groups by hydrolysis.

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

After the completion of the reaction, the introduction rate of the silyl functional group into the amino nitrogen was determined by measuring the amino nitrogen. The introduction rate of the silyl functional group was 67%.

After neutralizing the reaction solution with dilute hydrochloric acid, desalting it with an electrodialyzer, adjusting the pH to 6.5, concentrating and adjusting the concentration, the reaction product (silylated hydrolyzed collagen) was ) 63 g of an aqueous solution having a concentration of 20% were 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, and an average value of m + n = 10 (15 mmol as a stoichiometric mole obtained by measurement of amino nitrogen) To a 20% aqueous sodium hydroxide solution
9.5 and warmed to 55 ° C.

On the other hand, as a silylating agent, in the general formula (III), R ⁶ ＣｌCl, R ⁷ ＣＨCH ₃ , R ⁸ ＣｌCl and a
= 3 (3.1 equivalents to the amount of amino nitrogen in the hydrolyzed wheat peptide) was dissolved in water to form a 15% aqueous solution, and stirring was continued for 15 minutes to directly bond to silicon atoms. The existing Cl atom was converted to a hydroxyl group.

The above-mentioned aqueous solution of the hydrolyzed wheat protein was heated to 55 ° C.
While stirring with, an aqueous solution of a silyl compound converted to a hydroxyl group was added dropwise thereto over 1 hour. After dropping, 55 ° C
The stirring was continued for 5 hours to complete the reaction.

The reaction solution was neutralized with dilute hydrochloric acid, desalted by electrodialysis, and concentrated to adjust the concentration, thereby obtaining 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 In place of hydrolyzed collagen, hydrolyzed keratin (hydrolyzate of wool, average value of m = 0.6, average value of n = 4.
4, 50 g of a 30% aqueous solution (average value of m + n = 5) (42 mmol as a stoichiometric mole obtained by measurement of amino nitrogen) was used, and as a silylating agent, a compound 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 obtained in the same manner as in Example 1 except that 75 g (0.8 equivalents to the amount of amino nitrogen of hydrolyzed keratin) of the silyl compound of a = 3 was used in OC ₂ H _5. 58 g of an aqueous solution having a concentration of 20% (decomposed keratin) 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 to a hydroxyl group during the above reaction. It had been.

Example 4 Hydrolyzed soybean protein in place of hydrolyzed collagen (hydrolyzate of soybean protein, average value of m = 0.5, average value of n = 5.5, average value of m + n = 6) Of a 30% aqueous solution (18.4 mmol as a stoichiometric number of moles obtained by measurement of amino nitrogen) of a compound represented by the formula (III): R ⁶ ＣＨOCH ₃ , R ⁷
ＯOCH ₃ , R ⁸ ＯOCH ₃ , and 3.4 g of the silyl compound of a = 1 (0.9 equivalents to the amount of amino nitrogen of the hydrolyzed soybean protein) was used. Thus, 53 g of an aqueous solution having a reaction product (silylated hydrolyzed soybean protein) concentration of 20% was obtained. The introduction ratio 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 to a hydroxyl group during the above reaction.

Example 5 In place of hydrolyzed collagen, hydrolyzed yeast protein (hydrolyzate of yeast protein, average value of m = 1.2, average value of n = 6.8, average value of m + n = 8) Of a 30% aqueous solution (30 mmol as the stoichiometric number of moles obtained by measurement of amino nitrogen) of the following formula (III): R ⁶ ＣＨCH ₃ , R ⁷ ＯOC
Example 1 was the same as Example 1 except that 5.3 g (0.8 equivalents to the amount of amino nitrogen of the hydrolyzed yeast protein) of the silyl compound having ₂ H ₅ , R ⁸ = OC ₂ H ₅ and a = 3 were used. Similarly, 48 g of an aqueous solution having a concentration of a reaction product (silylated hydrolyzed yeast protein) of 20% was obtained. The introduction ratio 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 to a 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 a silylating agent, R ⁶ ＯOCH ₃ , R ⁷ ＯOCH ₃ , R ⁸ ＯOC in the general formula (III)
In H ₃ , 17.8 g (0.7 equivalents to the amount of amino nitrogen of L-lysine hydrochloride) of a silyl compound having a = 3 was added to 15 parts of water.
% Aqueous solution, adjusted to pH 3.5 with diluted hydrochloric acid, continued stirring at 50 ° C. for 15 minutes, and hydrolyzed the methoxy group to convert it to a hydroxyl group.

While stirring the aqueous solution of L-lysine hydrochloride, an aqueous solution of a silyl compound converted to a hydroxyl group was added dropwise thereto over 30 minutes. After completion of the dropwise addition, stirring was continued at 55 ° C. for further 5 hours to complete the reaction.

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

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

Comparative Example 1 The same 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 equivalent to the amount of amino nitrogen of the hydrolyzed collagen). By performing the same operation 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 The same hydrolyzed wheat protein and the same silyl compound as in Example 2 were used, and the amount of the silyl compound was changed to 4.5 g (1.3 equivalents to the amino nitrogen content of the hydrolyzed wheat protein). Except for 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 hydrolyzed keratin and the same silyl compound as in Example 3 were used, except that the amount of the silyl compound was changed to 11.3 g (1.2 equivalents to the amount of amino nitrogen of the 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 the silyl compound was changed to 2.3 g (0.6 equivalent to the amount of amino nitrogen of the hydrolyzed soybean protein). Except for the above, 43 g of a 20% aqueous solution of silylated hydrolyzed soybean protein was obtained in the same manner as in Example 4. The introduction ratio 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 amino nitrogen content of the hydrolyzed yeast protein). Except for the above, the same operation as in Example 5 was carried out to obtain 81 g of a 20% aqueous solution of a 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 increased to 80.5 g (1.2 equivalents to the amount of amino nitrogen in L-lysine hydrochloride). 173 g of a 15% aqueous solution of silylated L-lysine was obtained in the same manner as in Example 6, except for the change. 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 the 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 amount of amino nitrogen 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 solution of the silylated peptide obtained in each of Examples 1 to 7 and Comparative Examples 1 to 7 was kept at room temperature (for 10 to 25 ° C.) for 90 days.
Was visually inspected for the occurrence of a precipitate when stored under the conditions described above. The evaluation criteria are as follows.

Evaluation criteria +++: very large amount of precipitate ++: large amount of precipitate +: slight amount of precipitate or turbidity-: no significant amount of precipitate or turbidity

Tables 1 and 2 show the results. Table 1
In No. 2, the types of peptides used in synthesizing the silylated peptides of each Example and Comparative Example are also described.

[0084]

[Table 1]

[0085]

[Table 2]

As shown in Tables 1 and 2, none of the silylated peptides prepared in Examples 1 to 7 produced turbidity or precipitates 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 cause turbidity or precipitate, whereas Comparative Examples 2, 3, 5, and 7, in which the introduction rate of the silyl functional group was high. 6 causes turbidity,
In particular, Comparative Examples 3 and 6, in which a large amount of a silyl functional group was introduced into a peptide having a low degree of amino acid polymerization, were highly turbid.

[PH Stability of Silylated Peptide] 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 the silylated peptide is adjusted to pH 3, 4, 5, 7, 9, 10 with 6N hydrochloric acid or 20% sodium hydroxide, and the pH is adjusted to 24 at room temperature.
After standing for a time, the presence or absence of a precipitate or turbidity was visually confirmed. The results are shown in Tables 3 and 4. The evaluation criteria are the same as in the case of storage stability.

[0088]

[Table 3]

[0089]

[Table 4]

As shown in Tables 3 and 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 became cloudy at pH 3. As a result, the silylated L-lysine of Example 6 became turbid at pH 4 or lower, while the other silylated peptides showed no turbidity or precipitate within the tested pH range.

In addition, no turbidity or sediment was observed at pH 4 or higher for the silylated hydrolyzed keratin of Example 3, the silylated hydrolyzed yeast protein of Example 5, and the glycyl-L-alanine of Example 7. Hydrolyzed keratin and hydrolyzed yeast protein contain many amino acids having an amino group at the end of the side chain, so 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 occurred at a low pH, and in silylated glycyl-L-alanine, the molecular weight of the peptide was reduced. It is considered that the hydrophobicity of the silyl functional group was likely to appear due to the small size, and turbidity was generated.

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

[Test for Confirming Enhancement of Hair Tensile Strength by Silylated Peptide] The confirmation of the enhancement of hair tensile strength by silylated peptides was carried out according to the Journal of SCCJ,
vol. 21, No. The method was performed according to the method described in No. 2 “Evaluation Method of Hair Damage (I)”.

In the test, in order to suppress the variation in the strength of the hair used as a sample, hair which had been subjected to a decolorizing treatment once so that the strength of the hair was almost constant was used. That is, a hair bundle of 10 cm in length and 1 g in weight is immersed in 10 g of a 1: 1 mixed solution of 10% hydrogen peroxide and 10% ammonia water for 30 minutes to decolorize, rinsed with ion-exchanged water, and dried. For the test.

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

In the tensile strength test, the major and minor diameters of the central part (5 cm from the end) of each hair were measured with a micrometer to calculate the cross-sectional area, and the tensile strength of this part was measured with a tensile strength tester [Fudo Kogyo Co., Ltd. (Manufactured by Co., Ltd., rheometer), and the tensile strength per sectional area was calculated.

The comparison was made between untreated hair subjected to only the decolorization treatment and hydrolyzed collagen (average value of m + n = 2).
Tensile strength of hair treated in the same manner with a 5% aqueous solution of 0) and a 5% aqueous solution of hydrolyzed keratin (average value of m + n = 5) was measured. Table 5 shows the results.

[0098]

[Table 5]

As shown in Table 5, the hair treated with the silylated hydrolyzed collagen of Example 1 increased the tensile strength by about 9.5% with respect to the untreated hair, and the hair treated with the silylated hydrolyzed keratin of Example 3 Hair treated with about 16 to untreated hair
% Tensile strength increased. In addition, the hair treated with the silylated hydrolyzed collagen of Example 1 and the hair treated with the silylated hydrolyzed keratin of Example 3 are the same as the hair treated with the non-silylated hydrolyzed collagen of the same molecular weight or the hydrolyzed keratin. In comparison, an increase in strength was observed, and it was clear that the silylated peptide well sorbed the hair and contributed to the recovery of the strength of the damaged hair.

In contrast, the hair treated with the silylated hydrolyzed collagen of Comparative Example 1 had almost the same tensile strength as the hair treated with the non-silylated hydrolyzed collagen, and the hair of Comparative Example 3 had the same tensile strength. Hair treated with hydrolyzed keratin resulted in slightly lower strength than hair treated with unsilylated hydrolyzed keratin. This is presumably because the silylated hydrolyzed collagen of Comparative Example 1 had a low introduction rate of silyl functional groups and could not contribute to the recovery of hair strength as much as the silylated hydrolyzed collagen of Example 1. It is considered that the silylated hydrolyzed keratin of No. 3 is considered to be because the introduction rate of the silyl functional group was too high and the sorbing power of the peptide to the hair was reduced.

[Application Examples] Next, application examples in which the cosmetic base comprising the silylated peptide of the present invention is blended with various cosmetics will be described. In addition, in an application example, the silylated peptide represented by the general formula (II) is indicated by the example number, and the type of the silylated peptide is also described in parentheses after the number. Also, the amount is based on parts by weight,
In particular, except for the concentration indicated in parentheses, the compounding amount as a pure component is shown.

Application Example 1 Three kinds of treatment bases (Example 1 and Comparative examples 1 and 2) having the compositions shown in Table 6 were prepared, and the treatment base and LPG gas were pressurized at a weight ratio of 8: 2 in a pressurized container. And a treatment mousse was prepared.

[0103]

[Table 6]

Each of the treatment mousses of Example 1 and Comparative Examples 1-2 was used for a hair bundle of 10 cm in length and 1 g in weight, and the gloss and moisture of hair were given to five female panelists.
The combability was evaluated on a 5-point scale. The evaluation criteria are as follows, and the results are shown in Table 7 as average values.

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 of Example 1 containing the silylated hydrolyzed collagen of Example 1 was silicone oil (dimethyl silicone).
Compared to the treatment mousse of Comparative product 1 and the treatment mousse of Comparative product 2 not containing silylated hydrolyzed collagen or silicone oil,
The evaluation value was high in both moisture and combability, and the effect of incorporating silylated hydrolyzed collagen was clear.

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

[0109]

[Table 8]

Using the shampoos of Example 2 and Comparative Examples 3 and 4, hair bundles each having a length of 10 cm and a weight of 1 g were washed. For washing, 0.5 g of each shampoo was used, washed with warm water, rinsed with warm water, and dried with a hair dryer. After repeating this operation five times, the five female panelists were asked to apply the applied example 1 on the gloss, moistness, smoothness, combability, and foam feel during washing (softness and smoothness) of the hair after washing. The evaluation was performed according to the same evaluation criteria. The results are shown in Table 9, where the evaluation values are average values.

[0111]

[Table 9]

As shown in Table 9, the shampoo of Example 2 containing the silylated hydrolyzed wheat protein of Example 2 was silicone oil (octamethyltrisiloxane).
In comparison with the shampoo of Comparative Product 3 containing no, the shampoo of the silylated hydrolyzed wheat protein and the shampoo of Comparative Product 4 not containing the silicone oil, the evaluation value was higher in any of the items, and the shamylated hydrolyzed wheat protein was compounded. The effect was clear.

Application Example 3 Three types of first agents for permanent wave (comparative 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,
A hair bundle having a weight of 1 g and a length of 15 cm was used as a test hair bundle, and a 6% aqueous sodium bromate solution was used as the second agent.
Permanent wave treatment was performed once, three times, and six times, respectively, with the first agent for permanent wave of Example product 3 and comparative products 5 to 6, and the appearance and tactile sensation of the treated hair were given to five female panelists. The evaluation was performed according to the same evaluation criteria as in Application Example 1. The results are shown in Table 11, where the evaluation values are average values.

[0116]

[Table 11]

As shown in Table 11, when the first product for permanent waving of Example 3 containing the silylated hydrolyzed soybean protein of Example 4 was used, the comparative product containing no silylated hydrolyzed soybean protein was used. In the case of the first agent for permanent wave of the comparative product 6 in which the silylated hydrolyzed soybean protein of Comparative Example 4 was used instead of the silylated hydrolyzed soybean protein of Example 4 in the case of the first agent for permanent wave of No. 5 In comparison, both the appearance and the feel of the treated hair were high in evaluation values, and the effect of incorporating the silylated hydrolyzed soybean protein of Example 4 was clear.

Application Example 4 A treatment rinse having the following composition (Example 4) was prepared by mixing the silylated hydrolyzed keratin obtained in Example 3.

Example 3 (silylated hydrolyzed keratin), (20%) 17.5 cetanol 4.0 stearyltrimethylammonium chloride (29%) 2.0 distearyldimethylammonium chloride (73%) 1.0 stearic acid Ethylene glycol (3.0 Ayacol EGS-D manufactured by Seiwa Kasei) Diethylaminoethylamide stearate (Ayacol Amineamide 50E manufactured by Seiwa 3.0 Kasei) Diglycerin isostearate (1.5 Ayachol DGMIS manufactured by Seiwa Chemical) Propylene glycol 3.0 Paraoxybenzoic acid ester / phenoxyethanol 0.5% mixture (Secept G, manufactured by Seiwa Kasei Co., Ltd.) Flavor Appropriate amount Sterile ion-exchanged water Total 100 Adjusted to malic acid pH 6.0

When the treatment rinse of Example 4 containing the silylated hydrolyzed keratin of Example 3 was used for hair, the treatment rinse not containing the silylated hydrolyzed keratin of Example 3 [that is, The treatment rinse, which does not contain the silylated hydrolyzed keratin of No. 3 and the amount of sterilized ion-exchanged water is the same as that of Example 4 except that the amount of sterilized ion-exchanged water is increased. Good, hair conditioning was easy.

Application Example 5 The face wash (Example 5) having the following composition was prepared by blending the silylated L-lysine obtained in Example 6.

Example 6 (Silylated L-lysine), (15%) 10.0 Coconut oil fatty acid hydrolyzed collagen potassium 40.0 (Promois ECP-C, 35%, manufactured by Seiwa Chemical Co., Ltd.) Coconut oil fatty acid methyltaurine Sodium (30%) 40.0 Diethanolamide laurate 3.0 Polyethylene glycol monostearate 4.5 Polyethylene glycol dioleate 4.0 Mixture of 0.5% paraoxybenzoate and phenoxyethanol (Secept, manufactured by Seiwa Chemical Co., Ltd.) G) Perfume Appropriate amount Sterile ion-exchanged water Total 100 Adjusted to malic acid pH 6.0

When the face was washed with the face wash of Example 5 in which the silylated L-lysine was blended in Example 6 above, the face wash in which the silylated L-lysine was not blended in Example 6 [that is, the face wash in Example 6 was used. Except for containing silylated L-lysine and increasing the amount of sterilized ion-exchanged water, the skin after use has luster and moisture compared to the case of using the same facial cleanser as Example Product 5, And the skin was smooth.

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

[0125]

[Table 12]

The body shampoos of the above-mentioned product 6 and comparative products 7 to 8 were treated with 10 panelists (5 men, 5 women)
To use for one week (the number of uses is 7
(Four people three times), the foam quality (softness and smoothness) at the time of washing, and the smoothness and moist feeling of the skin after washing were evaluated according to the following criteria. Table 13 shows the results. The evaluation values in Table 13 are the average values of 10 persons.

Evaluation criteria : Best: 2 Next best: 1 Poor: 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 at the time of washing was soft and smooth, and after use, it was applied to the skin. It gives smoothness and moist feeling and is better than the body shampoo of comparative product 7 containing silicone oil [dimethylsiloxane / methyl (polyoxyethylene) siloxane copolymer] and the comparative shampoo containing neither of them. It was clear that it was excellent.

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

[0131]

[Table 14]

A solution having the following composition was used as the second agent. [Second agent composition] Stearic acid 1.0 part Glycerin monostearate 1.5 parts Polyoxyethylene oleyl ether (20EO) 1.0 part Hydrogen peroxide (35%) 15.5 parts Sterilized ion-exchanged water 100 in total Department

A hair bundle of 1 g in weight and 15 cm in length was dyed with each of the hair dye (first agent) of Example 8 and Comparative Products 10 to 11 and the second agent. In the hair dyeing process, the first agent and the second agent are mixed in equal amounts, and the mixture is applied to a hair bundle, left to stand for 30 minutes, and then rinsed with warm water.
This was performed by washing with a 2% aqueous solution of polyoxyethylene noniphenyl ether. After the hair dyeing treatment, the hair bundle is dried with a hair dryer, and the hair is leveled, glossed, moisturized and combed by 10 panelists (6 females, 4 males)
Then, the same evaluation criteria as in Application Example 1 were used.

Also, 30 hairs were respectively extracted from the hair bundle after the hair dyeing, and the major and minor diameters of the central part (7.5 cm from the end) of the hairs were measured with a micrometer to determine the cross-sectional area. After the calculation, the tensile strength of the portion was measured with a tensile tester (Rheometer, manufactured by Fudo Kogyo Co., Ltd.), and the tensile strength per sectional area was calculated. Table 15 shows the results.

[0135]

[Table 15]

As shown in Table 15, the hair dye of Example 8 containing the silylated hydrolyzed yeast protein of Example 5 was as follows:
Compared with the hair dye of Comparative Product 10 containing silicone oil (dimethylpolysiloxane) and the hair dye of Comparative Product 11 containing no silylated hydrolysed yeast protein or silicone oil, the hair after dyeing was evenly smoothed. The evaluation value was large for all of the dyeability, gloss, moisture, and combability.

As for 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 product 11 [ie,
Hair dye containing neither silylated hydrolyzed yeast protein nor silicone oil (dimethylpolysiloxane)]
The strength was increased by about 4% as compared with that of Example 5, and it was clear that the silylated hydrolyzed yeast protein of Example 5 protected the hair from damage to the hair due to the chemical treatment during hair dyeing.

[0138]

As described above, the cosmetic base comprising the silylated peptide of the present invention, when incorporated into hair cosmetics, imparts luster and moisture to hair, improves combability of hair, and improves shampoo and the like. When formulated into a detergent, it makes the foam soft and smooth, improving the feel to the skin, and when formulated into skin cosmetics, imparts luster and moisture to the skin and smoothes the skin.

The cosmetic base comprising the silylated peptide of the present invention is water-soluble, has excellent pH stability and storage stability in water, and is suitable for use in aqueous hair cosmetics and skin cosmetics. No turbidity or precipitation occurs during storage.

────────────────────────────────────────────────── ─── Continued on the front page (51) Int.Cl. ⁷ Identification code FI A61K 7/09 A61K 7/09 7/13 7/13 7/50 7/50 (72) Inventor Takashi Adachi Higashiosaka City, Osaka Prefecture 1-214 Fukuichicho Seiwa Kaseinai Co., Ltd. (56) References JP-A-3-223207 (JP, A) (58) Fields investigated (Int. Cl. ⁷ , DB name) A61K 7/00 -7/50 CA (STN)

Claims (3)

(57) [Claims] The present invention relates to the following general formula (I): 50% or more and 75% or less of all amino groups including amino groups in amino acid side chains of a peptide. [Wherein, R ¹ , R ² , and R ³ represent a methyl group or a hydroxyl group, and all of R ¹ , R ² , and R ³ may be the same;
They may also be different. a is 1 or 3], which comprises a silylated peptide having a functional group containing only one silicon atom covalently bonded thereto. 2. The cosmetic base according to claim 1, wherein the amino acid polymerization degree of the peptide moiety in the silylated peptide is 1 to 50. 3. A silylated peptide represented by the following general formula (I)
I) [Wherein, R ¹ , R ² , and R ³ represent a methyl group or a hydroxyl group, and all of R ¹ , R ² , and R ³ may be the same;
They 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 ; 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)]. 2. The cosmetic substrate according to claim 1, which is a silylated peptide.