JP3407765B2 - Cosmetic base material - Google Patents

Description

Detailed Description of the Invention

[0001]

FIELD OF THE INVENTION The present invention relates to a cosmetic base material comprising a specific silylated peptide. More specifically, the present invention is composed of a specific silylated peptide in which a functional group containing only one silicon atom is covalently bonded to the amino group of the peptide, is water-soluble, and is incorporated into hair cosmetics and skin cosmetics. To improve the combability of hair, prevent hair branching, impart gloss and moisture to the skin, make the skin smooth, and have excellent pH stability and storage stability. The present invention relates to a cosmetic base material which 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, since the reaction between the water-insoluble polypeptide and the hardly soluble or insoluble silicone oil is carried out in water, the reactivity is poor and the yield is low. There is also a problem that a water-soluble organic solvent such as alcohol must be added. Therefore, the present invention provides a cosmetic base material having both the excellent properties of a silicone compound and the excellent properties of a polypeptide, excellent pH stability and storage stability in water, and does not cause turbidity or precipitation during storage. The purpose is to provide.

[0007]

Means for Solving the Problems As a result of intensive studies to achieve the above object, the present inventors have found that the following amino group of a peptide is covalently bonded with a functional group containing only one silicon atom. General formula (I)

[0008]

[Chemical 2]

[In the formula, at least two of R ¹ , R ² and R ³ represent a hydroxyl group, and the rest represent a methyl group. R ⁴ represents a residue excluding the terminal amino group of a basic amino acid having an amino group at the end of the side chain, R ⁵ represents a side chain of an amino acid other than R ⁴ , a is 1 or 3, and m is 0. ˜200, n is 1 to 200, and m + n is 2 to 200 (however, m and n only indicate the number of amino acids and do not indicate the order of amino acid sequences)]. , Is water-soluble, has excellent pH stability and storage stability in water, and also has the excellent properties of a silicone compound and the excellent properties of a polypeptide. When this is compounded in hair cosmetics or skin cosmetics, It imparts luster and moisture to the hair, improves combability of the hair, prevents branching of the hair, imparts luster and moisture to the skin, and smoothes the skin, especially as a detergent for shampoo and the like. When mixed, gives the foam a soft feel , To smooth the hair and skin after use, yet found that does not cause turbidity or precipitation during storage, have accomplished the present invention.

The structure and properties of the silylated peptide described above, the action of the silylated peptide on hair and skin, the peptides and silyl compounds used for synthesizing the silylated peptide, and the synthesis of the silylated peptide are described below. , Use of cosmetic base material consisting of silylated peptide,
It will be described in detail from the viewpoint such as.

[Structure and Properties of Silylated Peptide] The silylated peptide of the present invention is represented by the general formula (I) as described above, and the silylated peptide has an amino group of an amino acid side chain. A functional group containing only one silicon atom is covalently bonded to the amino group of the peptide containing (i.e., the terminal amino group of the peptide and the amino group of the side chain). The functional group containing only one silicon atom has the following general formula (II)

[0012]

[Chemical 3]

[In the formula, at least two of R ¹ , R ² and R ³ represent a hydroxyl group, and the rest represent a methyl group. a is 1
Or 3].

The silylated peptide represented by the above-mentioned general formula (I) includes peptides and, for example, the following general formula (III)

[0015]

[Chemical 4]

[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 be different, but the number of methyl groups does not exceed two. X is a halogen atom and a is 1 or 3] and is obtained by reacting with a silyl compound.

The silylated peptide represented by the general formula (I) of the present invention is obtained by reacting a hydrophilic peptide with a hydrophobic silyl compound. Since the reaction is carried out in water, a silicon atom is used. The alkoxy group, halogen atom, and the like bound to are substituted with water and all or part of them become hydroxyl groups, so that they become water-soluble after the reaction. Furthermore, since the molecular structure of the silyl compound 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 represented by the general formula (I) of the present invention, the introduction rate of a functional group containing only one silicon atom (for simplicity, referred to as a silyl functional group) to the amino group of the peptide is It is preferably 50% or more and 85% or less. That is, when the introduction rate of the silyl functional group is less than 50%, the properties based on the silyl compound are not sufficiently exhibited, and when it is more than 85%, the hydrophobicity increases and the hydrophilicity decreases,
This is because the storage stability becomes poor.

In the silylated peptide represented by the general formula (I) of the present invention, at least two of R ¹ , R ² and R ³ are hydroxyl groups and the rest are methyl groups.
This is to allow the silylated peptide to maintain water solubility, and the reason a is specified as 1 or 3 is to ensure water solubility and stability.

In the silylated peptide represented by the general formula (I), 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, 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 (I), m is 0 to 200, preferably more than 0 and 50 or less, more preferably more than 0 and 10 or less, and n is 1 to 200, It is preferably 1 to 50, more preferably 2 to 40, and m + n is 2 to 200, preferably 2 to 100, more preferably 3 to 50, 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.

[Effect of Silylated Peptide on Hair and Skin] The silylated peptide represented by the above general formula (I), when incorporated into a hair cosmetic product, imparts luster and moisture to the hair to make the hair smoother, 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 a high molecular weight silicone is attached, it is difficult to remove, and therefore a perm, bleach,
In addition to making chemical treatment such as hair dyeing difficult, it also reduces the sorption of peptides and cationized polymers on hair.

However, the silylated peptide is a peptide having a low-molecular-weight silyl group bonded to the peptide portion, and is sorbed on the hair by a normal peptide sorption mechanism. Therefore, the peptide 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, the high molecular silicone 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 hair has a stronger hydrophilic property. Is said to be difficult to sorb,
In that respect, peptides are easily sorbed on damaged hair, and silylated peptides can sorb a silyl group on damaged hair via the peptide moiety, and can restore the strength and feel of damaged hair.

When the silylated peptide represented by the above general formula (I) 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] Peptides serving as a group constituting the peptide moiety in the silylated peptide represented by the general formula (I) include natural peptides, synthetic peptides, proteins (proteins) with acid, alkali or enzyme. Examples include hydrolyzed peptides obtained by partial hydrolysis.

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 2 to 200.

For acid hydrolysis of proteins, 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.

In this silylated peptide, in order to exert the characteristics of the silyl compound, the amino acid content having an amino group and the molecular weight of the peptide portion are important points. 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 low molecular weight peptides with amino acids in the side chains and high amino acid content, when the number of silyl functional groups attached is extremely high, the hydrophilicity decreases, the storage stability deteriorates, and the peptide's original hair retention Adhesion 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, the total content of lysine, arginine, hydroxylysine, etc., exceeds 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 necessary.

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. It is preferably 200, particularly preferably 3 to 50.

[Silyl Compound] As the silylating agent for silylating the above peptides, the silyl compound represented by the above general formula (III) is preferably used. As the silyl compound to be used, a commercially available silane coupling agent can be used. For example, Toshiba Silicone Co., Ltd. TSL8395, TSL8326, TSL
8325, TSL8320 (both are trade names), SH6076 manufactured by Toray Dow Corning Silicone Co., Ltd.
(Brand name), Shin-Etsu Chemical Co., Ltd. KMB703 (brand name), Nippon Unicar Co., Ltd. A-143 (brand name), 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, which means that after the reaction with peptides, they become methyl groups or hydroxyl groups and the silylated peptide has water solubility. This is to get it.

[Synthesis of Silylated Peptide] For the reaction between the peptides and the silyl compound represented by the general formula (III), first, the silyl compound is subjected to 5 times in water at 30 to 50 ° C.
It is carried out by stirring for 20 minutes to convert 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.

During the reaction, hydrogen halide is produced by the reaction to lower the pH of the reaction solution. Therefore, simultaneously with the reaction, an alkaline solution such as sodium hydroxide or potassium hydroxide is dropped to adjust the pH in the reaction system to 8 It is preferable to keep -11, especially 9-10. 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. It is used in cosmetics and skin cosmetics.

[Use of Cosmetic Base Material Consisting of Silylated Peptide] Examples of cosmetics in which the cosmetic base material comprising the silylated peptide represented by the general formula (I) of the present invention is blended include shampoo, hair rinse, and branch. Hair coat, first and second agents for permanent wave, hair cream, hair conditioner, set lotion, hair color, hair treatment rinse, liquid hair styling agent, hair pack, hair cosmetics such as hair nourishing agent, lotion, After shave lotion, shaving foam, vanishing cream, cleansing cream, emollient cream,
Various creams such as moisture cream, hand cream, face wash cream, depilatory, face pack, emulsion,
It can be used for various cosmetics such as face wash, body shampoo, various soaps, makeup products, sunscreen products.

The amount of the cosmetic base material comprising the silylated peptide as described above is 0.05 to 50% by weight, particularly 0.1 to 30% by weight, and especially 0.5 to 20% by weight in the cosmetic product.
It is preferable to set the content to about wt%. 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 the combability of the hair is not sufficiently expressed, Further, even if the amount of the silylated peptide compounded in the cosmetic product exceeds the above range, the effect accompanying it is not observed, and rather, excessive silylated peptide may be sorbed on hair or skin to cause stickiness. is there.

Examples of components that can be added to the above-mentioned cosmetics in combination with the cosmetic base material comprising the above-mentioned silylated peptide include, for example, alkyl sulphates such as sodium lauryl sulphate and ethanolamine lauryl sulphate, polyoxyethylene (2EO). Lauryl ether triethanolamine sulfate (where EO is ethylene oxide, and the number before EO indicates the number of moles of ethylene oxide added), polyoxyethylene (3EO) alkyl (having 11 to 1 carbon atoms)
5 or a mixture of two or more thereof) Polyoxyethylene alkyl ether sulfate such as sodium ether sulfate, sodium laurylbenzenesulfonate, alkylbenzenesulfonate such as trilauramineamine laurylbenzenesulfonate, 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 (I) is used in combination with a chain or cyclic methyl polysiloxane, methylphenyl polysiloxane, amino-modified silicone oil, or other silicone oil.
It is possible to improve the emulsion stability of the silicone oil and increase the action of the silicone oil.

[0049]

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 [The number of polymerized amino acids in a collagen hydrolyzate is represented by m and n in the general formula (I). Mean value of m = 2, average of n] Value = 18,
The average value of m + n = 20] was added dropwise to 50 g of a 30% aqueous solution (10.6 mmol as the stoichiometric number of moles obtained by measurement of amino nitrogen), and a 20% aqueous sodium hydroxide solution was added dropwise to adjust the pH to 9.5. And heated to 55 ° C.

On the other hand, as the silylating agent, in the general formula (III), R ⁶ ═CH ₃ , R ⁷ ═OCH ₃ , R ⁸ ═OCH
₃ , with a = 3, 2.6 g of a silyl compound of X = Cl (1.0 equivalent to the amount of amino nitrogen of hydrolyzed collagen) was dissolved in water to form a 15% aqueous solution, and the pH was adjusted to 3 with dilute hydrochloric acid. After adjusting to 0.5, stirring was continued at 50 ° C. for 15 minutes to hydrolyze each of the two methoxy groups (—OCH ₃ ) to convert them into hydroxyl groups.

While the above hydrolyzed collagen solution was stirred at 55 ° C., a silyl compound aqueous solution 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 diluted 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 ) 75 g of a 20% strength aqueous solution was obtained.

Example 2 Hydrolyzed Wheat Protein [A hydrolyzate of wheat protein,
When the number of polymerized amino acids is represented by m and n in the general formula (I), the average value of m = 1.2 and the average value of n =
8.8, average value of m + n = 10] 50% 30% aqueous solution
(15 mmol as the stoichiometric mole number obtained by the measurement of amino nitrogen) was added dropwise to a 20% aqueous sodium hydroxide solution 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 = Cl, R ⁷ = CH ₃ , R ⁸ = Cl, a =
1, 1 g of silyl compound of X = Cl (1.0 equivalent to the amount of amino nitrogen of hydrolyzed wheat peptide) was added to 1 part of water.
It was dissolved so as to be a 5% aqueous solution, and stirring was continued for 15 minutes to convert two Cl atoms directly bonded to silicon atoms into hydroxyl groups.

The above-mentioned hydrolyzed wheat protein aqueous solution was added at 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, desalted by electrodialysis, concentrated, and the concentration was adjusted to obtain 45 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 65%.

Example 3 Instead of hydrolyzed collagen, hydrolyzed keratin [a wool hydrolyzate, and the number of polymerized amino acids is represented by m and n in the general formula (I). = 0.
6, the average value of n = 4.4, the average value of m + n = 5] 30
% Aqueous solution (42 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 , a = 3, X = C
The reaction product (silylated hydrolyzed keratin) concentration was 20 in the same manner as in Example 1 except that 14.1 g of the silyl compound (1) was used (0.8 equivalent to the amount of amino nitrogen of hydrolyzed keratin). % Aqueous solution 68 g was obtained. The introduction rate of the silyl functional group was 61%, and the silyl compound represented by the general formula (III) was directly bonded to the silicon atom.
Each ethoxy group (OC ₂ H ₅ ) was converted into a hydroxyl group during the above reaction.

Example 4 Instead of hydrolyzed collagen, hydrolyzed soybean protein [a hydrolyzate of soybean protein, and the number of polymerized amino acids is represented by m and n in the general formula (I), Average value = 0.5, average value of n = 5.5, average value of m + n =
50 g of a 30% aqueous solution of 6] (18.4 mmol as the stoichiometric number of moles obtained by measurement of amino nitrogen)
R in the general formula (III) as a silylating agent
⁶ = OCH ₃ , R ⁷ = OCH ₃ , R ⁸ = OCH ₃ , a =
1, except that 3.1 g of a silyl compound of X = Cl (1.0 equivalent to the amount of amino nitrogen of hydrolyzed soybean protein) was used, the reaction product (silylation) was carried out in the same manner as in Example 1. 33g aqueous solution with 20% hydrolyzed soy protein concentration
Got The introduction rate of the silyl functional group was 59%, and the three methoxy groups directly bonded to the silicon atom in the silyl compound represented by the general formula (III) were each converted into a hydroxyl group during the above reaction. It was

Example 5 Hydrolyzed yeast protein in place of hydrolyzed collagen [a hydrolyzate of yeast protein, where the number of polymerized amino acids is represented by m and n in the general formula (I), Average value = 1.2, average value of n = 6.8, average value of m + n =
50 g of a 30% aqueous solution of 8] (30 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 =
CH ₃ , R ⁷ = OC ₂ H ₅ , R ⁸ = OC ₂ H ₅ , a = 3
In the same manner as in Example 1 except that 3.9 g of a silyl compound of X = Cl (1.0 equivalent to the amount of amino nitrogen of hydrolyzed yeast protein) was used, the reaction product (silylated hydrolyzed product) was used. 58 g of an aqueous solution containing 20% of decomposed yeast protein) was obtained. The introduction rate of the silyl functional group was 68%, and the two ethoxy groups directly bonded to the silicon atom in the silyl compound represented by the general formula (III) were each converted into a hydroxyl group during the above reaction. It was

[Storage stability of silylated peptide] Precipitation when the aqueous solution of the silylated peptide obtained in Examples 1 to 5 above was stored in a refrigerator at room temperature (however, 10 to 25 ° C) and 5 ° C for 90 days. The presence or absence of the generation of a product was visually inspected. The evaluation criteria are as follows.

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

The sample stored in the refrigerator was taken out from the refrigerator and then observed after the temperature of the sample reached room temperature. The results are shown in Table 1. In Table 1, the types of peptides used in the synthesis of the silylated peptide of each example are also shown below the example number.

[0065]

[Table 1]

As shown in Table 1, all of the silylated peptides prepared in Examples 1 to 5 were stored at room temperature and at 5 ° C.
No turbidity or precipitate was generated even when refrigerated.

[PH stability of silylated peptides] The pH stability of the silylated peptides prepared in Examples 1 to 5 was examined. That is, a 10% aqueous solution of the silylated peptide was adjusted to pH 3 with 6N hydrochloric acid or 20% sodium hydroxide,
It was adjusted to 4, 5, 7, 9, 10 and visually checked for the presence or absence of a precipitate or turbidity after standing at room temperature for 24 hours. The results are shown in Table 2. The evaluation criteria are the same as those for storage stability.

[0068]

[Table 2]

As shown in Table 2, the silylated hydrolyzed keratins of Example 3 and the silylated hydrolyzed yeast protein of Example 5 were slightly turbid at pH 3, but other silylated peptides were No turbidity or precipitate was observed within the tested pH range. Also, with the silylated hydrolyzed keratin of Example 3 and the silylated hydrolyzed yeast protein of Example 5, 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, so at low pH It is thought that turbidity occurred.

[Test for confirming enhancement of tensile strength of hair by silylated peptide] [0070] Confirmation of enhancement of tensile strength of hair by silylated peptide is described 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.

The test solution was treated with the 5% aqueous solution of silylated hydrolyzed collagen obtained in Example 1 and the 5% aqueous solution of silylated hydrolyzed keratin obtained in Example 3 to carry out the above decolorization treatment. The applied 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. After repeating this operation three times, 30 hairs were extracted from this hair bundle and subjected to a tensile strength test.

In the tensile strength test, the central part (5 cm from the end) of each hair was measured with a micrometer for the major axis and the minor axis to calculate the cross-sectional area, and the tensile strength of this part was 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 3.

[0075]

[Table 3]

As shown in Table 3, the hair treated with the silylated hydrolyzed collagen of Example 1 had an increase of about 9.5% in tensile strength as compared with the untreated hair, and the silylated hydrolyzed keratin of Example 3 was used. 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.

[Application Example] Next, an application example in which the cosmetic base material comprising the silylated peptide of the present invention is incorporated into various cosmetic products will be described. In the application examples, silylated peptides represented by the general formula (I) are indicated by an example number, and the type of silylated peptide is also shown in parentheses after the number. Further, the blending amount is based on parts by weight, and except for the concentration shown in parentheses, the blending amount as a pure component is shown.

Application Example 1 Three types of treatment bases having the composition shown in Table 4 (implementation product 1 and comparative products 1 and 2) were prepared, and the treatment base and LPG gas were mixed in a weight ratio of 8: 2 to a pressurized container. It filled in and prepared the treatment mousse agent.

[0079]

[Table 4]

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 five 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 5 as an average value.

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

[0082]

[Table 5]

As shown in Table 5, the treatment mousse agent of Example 1 containing the silylated hydrolyzed collagen of Example 1 was silicone oil (dimethyl silicone).
Compared to the treatment mousse agent of Comparative Product 1 in which the mousse was blended and the treatment mousse agent of Comparative Product 2 in which the silylated hydrolyzed collagen was not blended, the evaluation values were higher in terms of luster, moisture and combability. The effect of incorporating the hydrolyzed collagen was clear.

Application Example 2 Three kinds of shampoos having the compositions shown in Table 6 (Example 2 and Comparative Items 3 to 4) were prepared.

[0085]

[Table 6]

Using the shampoos of Example 2 and Comparative Examples 3 to 4, the 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 same as in Application Example 1 was applied to 5 female panelists with regard to the gloss of the hair after washing, smoothness, combability and feel of foam during washing (softness and smoothness). The evaluation criteria were evaluated. The results are shown in Table 7, and the evaluation value is an average value.

[0087]

[Table 7]

As shown in Table 7, 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 same or the shampoo of Comparative Product 4 containing no silylated hydrolyzed wheat protein, the evaluation value was higher in all items, and the effect of adding the silylated hydrolyzed wheat protein was higher. It was clear.

Application Example 3 Two kinds of first permanent wave composition having the compositions shown in Table 8
Agents (working product 3 and comparative product 5) were prepared.

[0090]

[Table 8]

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,
First for permanent wave of product 3 and comparative product 5
The agents were subjected to permanent wave treatment once, three times, and six times, respectively, and five female panelists evaluated the appearance and feel of the hair after the treatment according to the same evaluation criteria as in Application Example 1. The results are shown in Table 9, and the evaluation value is an average value.

[0092]

[Table 9]

As shown in Table 9, in the case of the first agent for permanent wave of Example 3 containing the silylated hydrolyzed soybean protein of Example 4, the comparative product containing no silylated hydrolyzed soybean protein was used. Compared with the case of using No. 1 of the first agent for permanent wave, the appearance and feel of the treated hair were higher in evaluation value, and the effect of adding silylated hydrolyzed soybean protein was clear.

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

[0095]   Example 3 (silylated hydrolyzed keratin), (20%) 20.0   Cetanol 4.0   Stearyl trimethyl ammonium chloride (29%) 2.0   Distearyl dimethyl ammonium chloride (73%) 1.0   Ethylene glycol stearate (3.0, manufactured by Seiwa Kasei Co., Ltd.   Ayacol EGS-D)   Stearic acid diethylaminoethylamide (Satoru 3.0   Kasei Ayacol Aminamide 50E)   Diglycerin isostearate (manufactured by Seiwa Kasei Co. 1.5   Ayacol DGMIS)   Propylene glycol 3.0   Paraoxybenzoate / phenoxyethano 0.5   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, and the amount of sterilized ion-exchanged water was increased, and compared to the treatment rinse of the same composition as in Example 4, moisturized hair, combability and brushing properties were obtained. Good and easy hair conditioning.

Application Example 5 Three types of hair dyes having the compositions shown in Table 10 (Example 5 and Comparative Examples 6 to 7) were prepared.

[0098]

[Table 10]

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 water (35%) 15.5 parts   Sterilized ion-exchanged water 100 parts total

Hair bundles each weighing 1 g and having a length of 15 cm were dyed using the hair dye (first agent) of Example 5 and Comparative Examples 6 to 7 and the second agent. Hair dyeing is performed by mixing the first and second agents in equal amounts, and applying the mixture to the hair bundle,
Leave for 30 minutes, then rinse with warm water, then 2%
It was carried out by washing with an aqueous solution of polyoxyethylene nonylphenyl 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.

Further, 30 hairs each were extracted from the above-mentioned hair bundle after dyeing, and the central area (7.5 cm from the edge) of these hairs was measured with a micrometer to determine the cross-sectional area. 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 11.

[0102]

[Table 11]

As shown in Table 11, the hair dye of Example 5 containing the silylated hydrolyzed yeast protein of Example 5 was
Compared to the hair dye of Comparative Product 6 containing silicone oil (dimethylpolysiloxane) and the hair dye of Comparative Product 7 containing no silylated hydrolyzed yeast protein, the leveling of the hair after dyeing is uniform. The evaluation values were large in all of the following items: gloss, luster, moisture, and combability.

Regarding the tensile strength, when the hair dye of Example 5 containing the silylated hydrolyzed yeast protein of Example 5 was used, the hair dye of Comparative Example 7 [ie, silylated hydrolyzed yeast] was used. The strength is increased by about 5% compared to the hair dye containing neither protein nor silicone oil (dimethylpolysiloxane). Silylated hydrolyzed yeast protein is used for hair treatment by chemical treatment during hair dyeing. It was clear that it protected the hair from damage.

[0105]

As described above, the cosmetic base material comprising the silylated peptide represented by the general formula (I) of the present invention, when incorporated into a hair cosmetic product, imparts gloss and moisturizing to the hair, Improves combability, and when added to detergents such as shampoo, it makes the foam soft and smooth, improving the feel to the skin.When added to skin cosmetics, it imparts gloss and moisture to the skin, Smooth out.

Further, the cosmetic base material comprising the silylated peptide represented by the general formula (I) of the present invention is water-soluble, has excellent pH stability and storage stability in water, and is an aqueous solution type hair. When blended in cosmetics and skin cosmetics, it does not become cloudy or precipitate during storage.

─────────────────────────────────────────────────── ─── Continuation of the front page (51) Int.Cl. ⁷ Identification symbol FI A61K 7/13 A61K 7/13 7/50 7/50 (72) Inventor Segawa Emi 1-2-2 Nunoichi-cho, Higashiosaka-shi, Osaka Prefecture No. 14 Seiwa Kasei Co., Ltd. (56) Reference JP-A-7-223921 (JP, A) JP-A-7-228508 (JP, A) JP-A-63-277609 (JP, A) JP-A-3 -223207 (JP, A) (58) Fields investigated (Int.Cl. ⁷ , DB name) A61K ^7/ 00-7/50

Claims (2)

(57) [Claims] 1. A compound represented by the following general formula (I) in which a functional group containing only one silicon atom is covalently bonded to an amino group of a peptide containing an amino group on the side chain of an amino acid. Wherein at least two of R ^1, R ^2, R ³ represents a hydroxyl <br/> group, the remainder shows the methyl group. R ⁴ represents a residue excluding terminal amino group of a basic amino acid having an amino group at the end of the side chain, R ⁵ represents a side chain of amino acids other than R ^4,
a is 1 or 3, m is 0 to 200, n is 1 to 200,
m + n is 2 to 200 (however, m and n only indicate the number of amino acids, not the order of amino acid sequences)]. . 2. The cosmetic base material according to claim 1, wherein the amino acid polymerization degree of the peptide portion in the silylated peptide is 2 to 200.