JP5795485B2 - Hair treatment agent - Google Patents

Description

  The present invention relates to a hair treatment agent applied to hair before heating.

  The hair is damaged by physical or chemical treatments such as brushing on the hair, hand dryer, thermal iron, hair color, permanent wave, etc., resulting in deterioration of the feel of the hair, loss of gloss, reduction of elasticity. For the purpose of repairing such hair, it is known to incorporate modified peptides such as protein derivatives into various hair treatment agents.

  For example, Patent Document 1 discloses a hair treatment agent containing soluble keratin into which a carboxyl group has been introduced. Patent Document 2 discloses a hair treatment agent containing a modified peptide having a carboxymethyl disulfide group or the like, and immerses the hair in a hair care agent containing the modified peptide. The hair is washed with water and dried with warm air. It has been disclosed.

JP 2010-132595 A JP 2010-285401 A

  By the way, in order to repair hair, it is desired that the component for the repair is easy to adhere to hair. Therefore, it is desired to provide a hair treatment agent containing a modified peptide that functions as a component that easily adheres to hair.

  In view of the above circumstances, an object of the present invention is to provide a hair treatment agent in which a repair component easily adheres to hair.

  As a result of intensive studies on the modified peptide to be blended in the hair treatment agent applied before heating by the present inventors, if the prescribed modified peptide is blended in the hair treatment agent, the modified peptide adheres to the hair. It has been found that it exhibits a function as an easily repairable component, and the present invention has been completed.

That is, the present invention is a hair treatment agent applied to hair before heating, and has a unit selected from the structures represented by the following formulas (I) to (III) and salts of these structures: A modified peptide having one or more chain groups is blended.
_{-S-S- (CH 2) n} -COOH (I)
(In the formula (I), n is 1 or 2.)
_{-S-S-CH (CH 3} ) -COOH (II)
_{-S-S-CH (COOH)} -CH 2 -COOH (III)

  Here, “applied before heating” in the present invention means that the denatured peptide is not washed off from the hair by washing or the like before heating the hair coated with the hair treatment agent. The “modified peptide” in the present invention is a peptide having one or more side chain groups having units selected from the structures represented by the above formulas (I) to (III) and salts of these structures. “Peptide” is a peptide in which two or more amino acids are linked by a peptide bond, and proteins such as keratin also correspond to peptides.

  The heating temperature in the heating in the present invention is preferably 40 ° C. or higher, preferably 60 ° C. or higher, and more preferably 80 ° C. or higher. It is considered that the higher the heating temperature is, the more the modified peptide blended in the hair treatment agent according to the present invention becomes a film, so that the amount of repair components attached to the hair increases. “Heating temperature” means not the hair temperature but the temperature outside the hair that contacts the hair.

  The said heating in this invention is good to be performed with the pressurization to hair. It is considered that the pressure increases the adhesion of the repair component to the hair and also smoothes the surface of the repair component.

  As said modified | denatured peptide mix | blended with the hair treatment agent which concerns on this invention, it is good to use a thing with a molecular weight 2000 or more, and you may use a thing with a molecular weight 10,000 or more.

  According to the hair treatment agent of the present invention, the prescribed modified peptide blended is heated, so that the repair component easily adheres to the hair.

2 is a SEM observation photograph of hair after treatment according to Example 1. 3 is a SEM observation photograph of hair after treatment according to Comparative Example 1. 4 is a SEM observation photograph of hair after treatment according to Example 2. It is a SEM observation photograph of the hair after processing by comparative example 2a. It is a SEM observation photograph of the hair after processing by comparative example 2b. 4 is a SEM observation photograph of hair after treatment according to Example 3. 5 is a SEM observation photograph of hair after treatment according to Comparative Example 3. 4 is a SEM observation photograph of hair after treatment according to Example 4. It is a flowchart which shows the example of the manufacturing method of the modified | denatured peptide in this invention. It is an observation photograph after heating various peptide containing liquids. It is an observation photograph after heating various peptide containing liquids and immersing in water.

  Based on the hair treatment agent which concerns on this embodiment, this invention is demonstrated below.

  The hair treatment agent according to this embodiment is formulated with a predetermined modified peptide, and is typically formulated with water (the amount of water is, for example, 60% by mass or more). Moreover, you may mix | blend the raw material mix | blended with a well-known hair treatment agent with this hair treatment agent as an arbitrary raw material.

(Modified peptide)
The predetermined modified peptide blended in the hair treatment agent of the present embodiment includes a main chain formed by peptide bonds of a plurality of amino acids and a side chain group bonded to the main chain.

  The main chain of the modified peptide is not particularly limited. Examples of this main chain include the same main chain of peptides having cysteine as one of the constituent amino acids. Examples of peptides having cysteine as one of the constituent amino acids include keratin and casein. Keratin is known to have a high cysteine ratio among peptides derived from natural products, and is a raw material from which the modified peptide can be efficiently obtained. From this viewpoint, the main chain of the modified peptide is preferably the same as the main chain of keratin.

The modified peptide has one or more side chain groups having units selected from the structures represented by the following formulas (I) to (III) and salts of these structures.
_{-S-S- (CH 2) n} -COOH (I)
(In the formula (I), n is 1 or 2.)
_{-S-S-CH (CH 3} ) -COOH (II)
_{-S-S-CH (COOH)} -CH 2 -COOH (III)

The salt having the structure represented by the above (I) to (III) is an ionic conjugate of a carboxylate anion and a cation. Examples of the unit serving as the cation include ammonium such as NH ₄ and metal atoms such as Na and K.

  The smaller the modified peptide molecule, the easier it is to dissolve in the hair treatment agent, and the smaller the effect on the solubility when the pH of the treatment agent is lowered. Therefore, the molecular weight of the modified peptide from the viewpoint of solubility of the modified peptide in water is preferably 70000 or less, preferably 60000 or less, and more preferably 50000 or less. Further, since the molecular weight of the modified peptide is more advantageous for adhesion of the repair component to the outer surface of the hair as the modified peptide molecule is larger, it is preferably 2000 or more, preferably 10,000 or more, more preferably 20000 or more, further preferably 30000 or more, 40000 The above is even more preferable. Here, regarding the molecular weight of the modified peptide, the molecular weight calculated from the relative distance between the band of the modified peptide and the band of the molecular weight marker by Sodium Dodecyl Sulfate-polyacrylamide gel electrophoresis (SDS-PAGE method) is the molecular weight of the modified peptide. Adopted by assuming that.

  The lower limit of the amount of the modified peptide in the hair treatment agent of this embodiment is, for example, 0.001% by mass or more, preferably 0.01% by mass or more, and more preferably 0.1% by mass or more. On the other hand, the upper limit of the modified peptide blending amount is preferably 5% by weight or less, preferably 3% by weight or less, more preferably 2% by weight or less, and even more preferably 1% by weight or less, from the viewpoint of suppressing an increase in cost due to blending in a large amount. . As described above, the smaller the molecular weight of the modified peptide, the easier it is to dissolve in the hair treatment agent. As described above, the blending amount of the modified peptide in the hair treatment agent may be appropriately set according to the molecular weight of the modified peptide.

  Next, as an example of a method for producing a modified peptide, a method for producing a modified peptide using keratin as a raw material will be described. As shown in FIG. 9, the modified peptide production method includes a reduction step (STP1), an oxidizing agent mixing step (STP2), a solid-liquid separation step (STP3), and a recovery step L (STP4). In the method including all the steps shown in FIG. 9, denatured peptides (denatured peptides dissolved in the liquid part L and denatured peptide contained in the solid part S shown in FIG. 9) are generated in the oxidizing agent mixing step (STP2). Therefore, the modified peptide can be produced without providing the solid-liquid separation step (STP3) and the recovery step L (STP4).

Reduction process (STP1)
The reduction step (STP1) is a step of mixing the reducing agent, keratin, and water. In this reduction step (STP1), the disulfide group (—S—S—) of keratin is reduced to a mercapto group (—SH HS—).

  Examples of keratin as a raw material include wool (merino wool, Lincoln wool, etc.), human hair, animal hair, feathers, nails and the like containing this as a constituent protein. Among them, it is preferable to use wool as a raw material in order to obtain a modified peptide inexpensively and stably. About raw materials, such as this wool, it is good to process beforehand, combining sterilization, degreasing, washing, cutting, crushing, and drying suitably.

  The reducing agent used in the reduction step (STP1) is one or two selected from thioglycolic acid, thioglycolate, mercaptopropionic acid, mercaptopropionic acid, thiolactic acid, thiolactate, thiomalic acid, and thiomalate. More than a seed. The combination of reducing agents when two or more reducing agents are used may be any combination, for example, a combination of thioglycolic acid and one thioglycolate, a combination of two thioglycolates, mercaptopropionic acid And a combination of one mercaptopropionate, a combination of two mercaptopropionates, a combination of thiolactic acid and one thiolactate, a combination of two thiolactates, a combination of thiomalic acid and one thiomalate, thioapple Combination of two acid salts, combination of one thioglycolate and one mercaptopropionate, combination of one thioglycolate and one thiolactate, combination of one thioglycolate and one thiomalate, mercaptopropion A combination of a single salt and a thiolactate, a single mercaptopropionate and a thiomalate Allowed, thiolactic acid salt type and thiomalate kind, and a combination of thioglycolate kind and thiosulfate lactate species as thiomalate kind.

  Examples of the thioglycolate include sodium thioglycolate, potassium thioglycolate, lithium thioglycolate, and ammonium thioglycolate. Examples of mercaptopropionate include sodium mercaptopropionate, potassium mercaptopropionate, lithium mercaptopropionate, and ammonium mercaptopropionate. Examples of the thiolactate include sodium thiolactate, potassium thiolactate, lithium thiolactate, and ammonium thiolactate. Examples of the thiomalate include sodium thiomalate, potassium thiomalate, lithium thiomalate, and ammonium thiomalate.

  The amount of the predetermined reducing agent used is preferably 0.005 mol or more and 0.02 mol or less based on 1 g of raw materials such as wool. In addition, the amount of the reducing agent used is 0.1 mol based on the volume of the liquid to be treated (including keratin or a keratin-derived treatment product and a reaction system in each step; the same shall apply hereinafter). / L or more and 0.4 mol / L or less.

  The amount of water in the reduction step (STP1) is not particularly limited, but may be, for example, 20 parts by volume or more and 200 parts by volume or less with respect to 1 part by mass of raw materials such as wool.

  In the reduction step (STP1), one or more alkaline compounds may be mixed with the liquid to be treated. An alkaline compound is a compound that can be made alkaline by adding it to water. Examples of the alkaline compound include lithium hydroxide, sodium hydroxide, potassium hydroxide, barium hydroxide, sodium carbonate, potassium carbonate, ammonia and the like.

  The mixing amount of the alkaline compound is not particularly limited, but is an amount for adjusting the pH of the liquid to be treated in the reduction step (STP1) to the following range. As a minimum of pH in a reduction process (STP1), 9 is preferred and 10 is more preferred. On the other hand, the upper limit of the pH in the reduction step (STP1) is preferably 13, and more preferably 12. By setting the pH in the reduction step (STP1) to the above lower limit or higher, keratin can be reduced efficiently. Further, by making the pH below the above upper limit, the cleavage of the keratin main chain can be suppressed (for the purpose of promoting the cleavage of the keratin main chain, the pH of the liquid to be treated should be adjusted to exceed 13. Just do it.)

  Although the temperature conditions of a reduction process (STP1) are not specifically limited, 35 degreeC or more and 60 degrees C or less are good, and 40 degreeC or more and 50 degrees C or less are preferable. When the temperature condition is less than 35 ° C., the reduction reaction rate for converting the disulfide group into a mercapto group is lowered, and keratin may not be sufficiently reduced. On the other hand, when it exceeds 60 ° C., the keratin main chain tends to be cleaved. Moreover, the time of the reduction process (STP1) becomes longer as the set temperature is lower, and becomes shorter as the set temperature is higher.

Oxidant mixing step (STP2)
The oxidizing agent mixing step (STP2) is a step of mixing the processed product (keratin-derived product) that has undergone the reducing step (STP1) and an oxidizing agent to generate a modified peptide. The mixing of the oxidizing agent is performed to promote an oxidation reaction that modifies the mercapto group of the processed product. Usually, an oxidizing agent is mixed with the liquid to be processed containing the processed product that has undergone the reduction step (STP1).

  Examples of the oxidizing agent include sodium bromate, potassium bromate, sodium perborate, potassium perborate, hydrogen peroxide, and the like. The oxidizing agent to be used is 1 type, or 2 or more types.

  The amount of the oxidizing agent used in the oxidizing agent mixing step (STP2) is not particularly limited, but may be 0.001 mol or more and 0.02 mol or less based on 1 g of raw materials such as wool, and the oxidizing agent mixing step ( STP2) is preferably 0.02 mol / L or more and 1 mol / L or less based on the volume of the liquid to be treated.

  When mixing the oxidant with the liquid to be treated, an oxidant solution of about 1 mol / L or more and 5 mol / L or less is used, for example, in order to avoid local concentration of the oxidant in the liquid to be treated. It is good to mix gradually regardless of continuous and intermittent over 6 minutes to 6 hours.

  It is preferable that the amount of oxidizing agent (A) mixed with the liquid to be treated having a pH of 9 or more is larger than the amount of oxidizing agent (B) mixed with the liquid to be treated having a pH of 7 or more and less than 9. This shortens the modified peptide production time. The ratio of the oxidizing agent amount (B) to the total of the oxidizing agent amounts (A) and (B) is preferably 20 mol% or less, more preferably 10 mol% or less, still more preferably 5 mol% or less, and particularly preferably 0 mol%.

  The pH of the liquid to be treated in the oxidizing agent mixing step (STP2) is adjusted according to the progress of this step. The pH at the start of mixing of the oxidizing agent is preferably 9 or more, and more preferably 10 or more. The pH is preferably 13 or less, preferably 12 or less, and more preferably 11 or less. When the pH is 9 or more, the generation efficiency of the modified peptide is good, and when the pH is 13 or less, the cleavage of the main chain of the keratin-derived processed product can be suppressed. The pH at the end of the oxidizing agent mixing step (STP2) is not particularly limited, but may be about 7.

  In the oxidant mixing step (STP2), the time of pH 9 or more is preferably longer than the time of pH 7 or more and less than 9, more preferably the time of pH 9 or more and 12 or less is longer than the time of pH 7 or more and less than 9, and pH 10 or more and 11 More preferably, the following time is longer than the time of pH 7 or more and less than 9. When such a procedure is adopted, the generation efficiency of the modified peptide is increased.

  As the acid for adjusting the pH of the liquid to be treated, one or more selected from organic acids and inorganic acids may be used. Examples of the organic acid include citric acid, lactic acid, succinic acid, and acetic acid, and examples of the inorganic acid include hydrochloric acid and phosphoric acid. The mixing amount of the acid may be appropriately set while monitoring the pH of the liquid to be treated. When mixing the acid with the liquid to be treated, if the pH is locally lowered in the liquid to be treated, the mercapto groups of the treated product may become disulfide groups, so the acid is gradually mixed with the liquid to be treated. It is preferable.

  The temperature condition in the oxidizing agent mixing step (STP2) is preferably 10 ° C. or more and 60 ° C. or less, and preferably 40 ° C. or less. By controlling the temperature within the above range, the production of by-products such as cystine monoxide can be suppressed.

The reaction formula in the oxidizing agent mixing step (STP2) is the thioglycolic acid or salt thereof, mercaptopropionic acid or salt thereof, thiolactic acid or salt thereof, or thiomalic acid or salt thereof as the reducing agent in the reduction step (STP1). When used, the reducing agents are listed in the order listed below.

Solid-liquid separation process (STP3)
The solid-liquid separation step (STP3) is a step of separating the liquid to be processed after the oxidizing agent mixing step (STP2) into the liquid part L and the solid part S. In the solid-liquid separation step (STP3), known solid-liquid separation means such as filtration, centrifugation, squeezing separation, sedimentation separation, and flotation separation can be employed, and desalting by ion exchange, electrodialysis, etc., if necessary. Etc.

Recovery process L (STP4)
The recovery step L (STP4) is a step of recovering the modified peptide L dissolved in the liquid part L obtained in the solid-liquid separation step (STP3) as a solid product. As a method for recovering the solid modified peptide L in the recovery step L (STP4), (1) recovery by freeze-drying the liquid part L, (2) recovery by spray-drying the liquid part L, (3) Examples thereof include recovery of a denatured peptide L precipitate generated by adding an acid such as hydrochloric acid to the liquid part L and lowering the pH of the liquid part L from about 2.5 to about 4.0. About the collect | recovered solid modified | denatured peptide L, washing | cleaning with water or acidic aqueous solution, drying, etc. are performed as needed.

  As described above, by finishing the treatment in the oxidizing agent mixing step (STP2), a denatured peptide dissolved in the solution to be treated and a denatured peptide not dissolved in the same solution are obtained. If these modified peptides are reduced in molecular weight, the solubility in water increases. As modes for reducing the molecular weight, (1) a mode in which the solid part S obtained in the solid-liquid separation step (STP3) is hydrolyzed, and (2) a solution in the liquid part L obtained in the solid-liquid separation step (STP3). The modified peptide L is hydrolyzed, (3) the modified peptide L recovered in the recovery step L is hydrolyzed, and (4) the modified peptide L and the solid part S are hydrolyzed together. Can be mentioned. In addition, as a method for reducing the molecular weight by hydrolysis, before the reduction step (STP1), simultaneously with the reduction step (STP1), between the reduction step (STP1) and the oxidizing agent mixing step (STP2), One example is hydrolysis for lowering the molecular weight.

  Examples of the method for hydrolyzing the modified peptide include (1) enzyme hydrolysis, (2) acid hydrolysis, and (3) alkali hydrolysis, which are known as peptide hydrolysis.

Hydrolysis by enzymes Examples of enzymes for hydrolysis include acidic proteolytic enzymes such as pepsin, protease A, and protease B; neutral to alkaline proteolytic enzymes such as papain, promelain, thermolysin, pronase, trypsin, and chymotrypsin Etc.

  The pH at the time of hydrolysis by the enzyme is preferably adjusted to 1 or more and 3 or less in the case of an acidic proteolytic enzyme, and is adjusted to 5 or more and 11 or less in the case of a neutral or alkaline proteolytic enzyme. Enzyme activity improves by making this pH into the said range.

  The reaction temperature at the time of hydrolysis with the enzyme is appropriately set within a range of 30 ° C. to 60 ° C. and the reaction time is 10 minutes to 24 hours. In order to stop the hydrolysis by the enzyme, it is preferable to deactivate the enzyme at a temperature of 70 ° C. or higher.

Hydrolysis with acid Examples of acids used for hydrolysis include inorganic acids such as hydrochloric acid, sulfuric acid, phosphoric acid, nitric acid, hydrobromic acid, and organic acids such as formic acid and oxalic acid. Is appropriately selected. The hydrolysis conditions are, for example, pH 4 or less, reaction temperature 40 ° C. or more and 100 ° C. or less, and reaction time 2 hours or more and 24 hours or less.

Hydrolysis with alkali Examples of the alkali used for hydrolysis include sodium hydroxide, potassium hydroxide, lithium hydroxide, barium hydroxide, sodium carbonate, potassium carbonate, lithium carbonate, sodium silicate, sodium borate and the like. Can be mentioned. The hydrolysis conditions are, for example, pH 8.0 or more, reaction temperature 50 ° C. or more and 100 ° C. or less, and reaction time 20 minutes or more and 24 hours or less.

  In order to recover the hydrolyzed modified peptide, the same method as in the recovery step L (STP4) can be employed. However, in the recovery method in which an acid is added so that the pH is about 2.5 to 4.0, the denatured peptide is reduced in molecular weight by hydrolysis, so that it may be difficult or impossible to recover.

(Optional raw material)
Raw materials other than the modified peptide optionally blended in the hair treatment agent of the present embodiment are appropriately selected from known hair treatment agent raw materials according to the purpose of use of the treatment agent. The known hair treatment materials include anionic surfactants, cationic surfactants, amphoteric surfactants, nonionic surfactants, higher alcohols, lower alcohols, polyhydric alcohols, sugars, fats and oils, ester oils, fatty acids, carbonized There are hydrogen, wax, synthetic polymer compounds, semi-synthetic polymer compounds, and natural polymer compounds. Other known hair treatment materials include silicone, protein, amino acid, animal and plant extracts, microorganism-derived materials, inorganic compounds, fragrances, preservatives, sequestering agents, and the like.

  Examples of the anionic surfactant include N-acyl amino acid salts, alkyl ether carboxylates, fatty acid amide ether carboxylates, fatty acid amide ether carboxylic acids, acyl lactates, alkane sulfonates, α-olefin sulfonates, alkyls. Examples include sulfosuccinate, alkylsulfoacetate, alkylbenzenesulfonate, alkylnaphthalenesulfonate, alkyl sulfate, alkyl ether sulfate, fatty acid monoglyceride sulfate, alkyl phosphate, and polyoxyethylene alkyl ether phosphate. . One or two or more types of anionic surfactants may be added to the hair treatment agent, and the concentration of the anionic surfactant is, for example, from 0.1% by mass to 20% by mass.

  Examples of cationic surfactants include alkylamine salts, fatty acid amide amine salts, ester-containing tertiary amine salts, arkol-type tertiary amine salts, long-chain alkyltrimethylammonium salts, di-long-chain alkyldimethylammonium salts, and tri-long-chain alkylmonomethyls. Examples thereof include ammonium salts, benzalkonium-type quaternary ammonium salts, and monoalkyl ether-type quaternary ammonium salts. One or two or more cationic surfactants may be added to the hair treatment agent, and the concentration of the cationic surfactant is, for example, 0.1% by mass or more and 20% by mass or less.

  Examples of amphoteric surfactants include alkyl glycine salts, carboxymethyl glycine salts, N-acylaminoethyl-N-2-hydroxyethyl glycine salts, alkyl polyamino polycarboxy glycine salts, alkyl amino propionates, and alkyl imino dipropionic acids. Salt, N-acylaminoethyl-N-2-hydroxyethylpropionate, alkyldimethylaminoacetic acid betaine, fatty acid amidopropyldimethylaminoacetic acid betaine, alkyldihydroxyethylaminoacetic acid betaine, N-alkyl-N, N-dimethylammonium- N-propylsulfonate, N-alkyl-N, N-dimethylammonium-N- (2-hydroxypropyl) sulfonate, N-fatty acid amidopropyl-N, N-dimethylammonium-N- (2-hydride) Kishipuropiru) sulfonate. One or two or more amphoteric surfactants may be blended in the hair treatment agent, and the blending concentration of the amphoteric surfactant is, for example, 0.1% by mass or more and 10% by mass or less.

  Nonionic surfactants include, for example, polyoxyethylene alkyl ether, polyoxyethylene polyoxypropylene alkyl ether, polyoxyethylene fatty acid ester, polyoxyethylene sorbitan fatty acid ester, polyoxyethylene sorbitol tetra fatty acid ester, glycerin fatty acid ester, sorbitan Examples include fatty acid esters, polyglycerin fatty acid esters, and sucrose fatty acid esters. One or two or more kinds of nonionic surfactants may be blended in the hair treatment agent, and the blending concentration of the nonionic surfactant is, for example, 0.1% by mass or more and 20% by mass or less.

  Examples of the higher alcohol include cetanol, isocetyl alcohol, stearyl alcohol, isostearyl alcohol, behenyl alcohol, octyldodecanol, and myristyl alcohol. One or two or more higher alcohols may be blended in the hair treatment agent, and the blending concentration of the higher alcohol is, for example, 3% by mass or more and 15% by mass or less.

  Examples of the lower alcohol include ethanol and isopropyl alcohol. One or two or more lower alcohols may be blended in the hair treatment agent, and the blending concentration of the lower alcohol is, for example, 0.5% by mass or more and 3% by mass or less.

  Examples of the polyhydric alcohol include ethylene glycol, diethylene glycol, triethylene glycol, propylene glycol, dipropylene glycol, glycerin, diglycerin, and butylene glycol. One or more polyhydric alcohols may be blended in the hair treatment agent, and the blending concentration of the polyhydric alcohol is, for example, 1% by mass or more and 50% by mass or less.

  Examples of the saccharide include sorbitol, mannitol, glucose, fructose, xylitol, lactose, maltose, maltitol, and trehalose. One or two or more saccharides may be blended in the hair treatment agent, and the blending concentration of the saccharide is, for example, 0.1% by mass or more and 10% by mass or less.

  Examples of the fat include almond oil, avocado oil, olive oil, shea fat oil, evening primrose oil, camellia oil, peanut oil, and rosehip oil. One or two or more types of fats and oils may be blended in the hair treatment agent, and the blending concentration of the fats and oils is, for example, 0.1% by mass or more and 10% by mass or less.

  Examples of ester oils include ethyl oleate, isopropyl myristate, isopropyl palmitate, butyl stearate, cetyl palmitate, myristyl myristate, octyldodecyl myristate, isopropyl isostearate, ethyl isostearate, cetyl 2-ethylhexanoate Hexyl isostearate, ethylene glycol di-2-ethylhexanoate, ethylene glycol dioleate, di (capryl / capric acid) propylene glycol, propylene glycol dioleate, trimethylolpropane triisostearate, pentaerythritol tetra2-ethylhexanoate Isocetyl isostearate, 2-octyldodecyl dimethyloctanoate, myristyl lactate, trioctyldodecyl citrate, phosphorus Diisostearyl, succinate di-2-ethylhexyl, diisobutyl adipate, stearic acid cholesteryl. One or two or more ester oils may be blended in the hair treatment agent, and the blending concentration of the ester oil is, for example, 0.1% by mass or more and 10% by mass or less.

  Examples of the fatty acid include isostearic acid, oleic acid, capric acid, stearic acid, palmitic acid, hydroxystearic acid, behenic acid, myristic acid, lauric acid, lanolin fatty acid, and linoleic acid. One or more fatty acids may be blended in the hair treatment agent, and the blending concentration of the fatty acid is, for example, 0.1% by mass or more and 10% by mass or less.

  Examples of the hydrocarbon include liquid paraffin, squalane, pristane, ozokerite, paraffin, ceresin, petrolatum, and microcrystalline wax. One or more hydrocarbons may be blended in the hair treatment agent, and the blending concentration of the hydrocarbon is, for example, 0.1% by mass or more and 20% by mass or less.

  Examples of the wax include beeswax, mole, candelilla wax, and carnauba wax. One or more waxes may be blended in the hair treatment agent, and the blending concentration of the wax is, for example, 0.1% by mass or more and 20% by mass or less.

  Examples of the synthetic polymer compound include carboxyvinyl polymer, polyvinyl alcohol, polyvinylpyrrolidone, polyacrylic acid, methacryloylethylbetaine / methacrylic acid ester copolymer. Examples of the semi-synthetic polymer compound include methyl cellulose, hydroxyethyl cellulose, hydroxypropyl cellulose, carboxymethyl cellulose, and soluble starch. Examples of natural polymers include sodium alginate, guar gum, glucan, cellulose, and sodium hyaluronate. One or two or more synthetic polymer compounds may be blended in the hair treatment agent, and the total blending concentration of the synthetic polymer compound, the semi-synthetic polymer compound and the natural polymer compound is, for example, 0.1 mass% or more and 15 mass % Or less.

(PH)
The pH of the hair treatment agent according to this embodiment is not particularly limited, but is preferably 5.0 or more and 11.0 or less, preferably 6.0 or more and 10.0 or less, and more preferably 6.5 or more and 9.0 or less. 6.5 to 8.0 is more preferable. If the pH is less than 5.0, the modified peptide tends to precipitate, and if the pH is 11.0 or more, hydrolysis of the modified peptide may progress. In order to adjust pH, an organic acid, an inorganic acid, an alkali metal hydroxide, or the like may be used.

(Form)
The dosage form at the time of use of the hair treatment agent according to this embodiment is not particularly limited, and for example, liquid, emulsion, lotion, cream, wax, gel, solid, foam (foam), fog Shape.

(how to use)
The method for using the hair treatment agent of this embodiment includes an application step and a heating step described below.

Application Step In the application step, the hair treatment agent of this embodiment is applied to the hair. The hair to be applied is a permanent treatment (a treatment that changes the hair shape into a wave shape, straight hair shape, etc. using a chemical reaction such as a reduction reaction or an oxidation reaction) or a coloring treatment (coloration of the hair with a dye, The hair may be any hair having a history of treatment that changes the hair color by decolorization of the hair pigment, or hair that has no history.

If the above-mentioned application is performed, it is considered that a reaction between the mercapto group of the hair and the modified peptide is accompanied. The mechanism of the reaction is as follows.
K _H -SH + K-S-S-R
→ K _H -S-S K + HS-R
[In the above reaction formula, K _H represents a keratin residue of hair, K—S—S—R represents a denatured peptide, R represents —CH ₂ —COOH, —CH ₂ —COOH salt, — (CH ₂ ) ₂ —COOH, — (CH ₂ ) ₂ —COOH salt, —CH (CH ₃ ) —COOH, —CH (CH ₃ ) —COOH salt, —CH (COOH) —CH ₂ —COOH, —CH ( COOH) —CH ₂ —COOH salt and any of these anions. ]

Heating Step In the heating step, the hair to which the hair treatment agent of this embodiment is applied is heated without performing an act of washing away modified peptides such as water washing. By not washing off the denatured peptide before heating, the amount of the repair component attached to the hair increases.

  By heating the hair, it is considered that the modified peptide blended in the hair treatment agent of the present embodiment becomes a poorly water-soluble component and adheres to the hair.

  FIG. 10 is an observation photograph after heating a glass plate on which various peptide-containing solutions have been dropped in a 105 ° C. atmosphere to dry the peptide-containing solution. FIG. 11 shows the glass plate after drying with water. It is an observation photograph after being immersed in for 30 minutes. Various peptide-containing liquids dropped on the glass plate were prepared in the same manner as the modified peptide used in the treatment of Example 1 described later, pH 7.5 solution containing 1% by mass of modified peptide in water, keratin-containing liquid (clauder) “Keratech IFP-HMW (containing 5% keratin)” and hydrolyzed keratin-containing liquid (“Promois KR-30” manufactured by Seiwa Kasei Co., Ltd.)

  In FIG. 10, the residue of any of the peptide-containing solutions dried can be confirmed, but in FIG. 11, it can be confirmed that only the modified peptide remained clearly. The denatured peptide shown in FIG. 11 remains as a film. From FIGS. 10 to 11, when the denatured peptide blended in the hair treatment agent of this embodiment is heated, it becomes a poorly water-soluble component. It is understood to head.

  The upper limit of the heating temperature when heating the hair is preferably 220 ° C., preferably 190 ° C., and more preferably 150 ° C. in order to suppress damage to the hair due to heat. 120 ° C. is more preferable. On the other hand, the lower limit of the heating temperature is preferably 40 ° C., preferably 60 ° C., more preferably 80 ° C., and still more preferably 100 ° C. so as to promote the poorly water-soluble componentization of the modified peptide.

  The aspect of heating the hair is not particularly limited. Examples of the heating mode include a mode in which warm air from a dryer or the like is blown to the hair, and a mode in which a heating element such as an electric heater is brought into contact with the hair.

  When heating the hair, it is preferable that the hair is pressed together. This pressurization is considered to increase the adhesion of the repair component to the hair and smooth the surface of the component. Examples of the method for applying pressure to the hair include a method using a hair iron as disclosed in Japanese Patent Application Laid-Open Nos. 2000-232911 and 2002-356408.

  The time for heating the hair is not limited as long as the hair is heated, but is typically until the hair is dry. Further, heating may be continued after the hair is dried.

  The above is the method of using the hair treatment agent according to the present embodiment, and this method includes hair before shampooing, hair after shampooing, hair after washing treatment, and hair between shampooing and washing treatment. It is applied to hair before coloring treatment, hair after coloring treatment, hair before permanent treatment, hair after permanent treatment, hair between reduction treatment and oxidation treatment. Moreover, you may use the usage method of this embodiment as a treatment which does not wash away.

  Hereinafter, the present invention will be described more specifically with reference to examples. However, the present invention is not limited to the following examples unless departing from the gist of the present invention.

(Modified peptide)
The modified peptides used in Examples 1 to 3 and Comparative Examples 1 and 2 described below were produced as follows.

Reduction step Merino wool, washed with a neutral detergent and dried, was cut to about 5 mm. 5.0 parts by weight of this wool, 15.4 parts by weight of 30% by weight sodium thioglycolate aqueous solution and 8.5 parts by weight of 6 mol / L sodium hydroxide aqueous solution were mixed, and water was further mixed to give a total amount of 150 parts by weight, pH 11 A liquid to be treated was prepared. This liquid to be treated was stirred at 45 ° C. for 1 hour. Subsequently, water was further mixed to make the total amount 200 parts by mass, left under conditions of 45 ° C. for 2 hours, and then naturally cooled until the liquid temperature reached room temperature.

Oxidant mixing step While stirring the liquid to be treated after the reduction step, 178 parts by mass of an aqueous solution containing 15.26 parts by mass of 35% by mass hydrogen peroxide was mixed with the liquid while stirring over about 30 minutes. (The pH of the liquid to be treated increased with the mixing of the hydrogen peroxide solution, but the increase was adjusted to a range of pH 10 to 11 by mixing an aqueous solution of about 20% by mass acetic acid.) Then, about 20 mass% acetic acid aqueous solution was mixed gradually, and it adjusted so that the pH of a to-be-processed liquid might become 11-7 gradually. Thus, a denatured peptide solution was obtained.

Solid-liquid separation step and recovery step Insoluble matter in the solution was removed by filtering the denatured peptide solution. Thereafter, 160 parts by mass of an aqueous solution containing 97.2 parts by mass of a 36% by mass hydrochloric acid aqueous solution was added to the recovered liquid part (filtrate) to adjust the pH of the denatured peptide solution to 7 to 3.8, thereby denatured peptide. Precipitation occurred. This precipitate was recovered and washed with water to obtain a solid modified peptide.

  An aqueous solution in which the solid modified peptide obtained in the recovery step was 1% by mass and the pH was 8 with 2-amino-2-methyl-1-propanol was heated at 85 ° C. for 5 hours. The heated solution was filtered to obtain an aqueous solution of the modified peptide used in the examples.

  As a result of confirming the above-obtained modified peptide by a sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) method using “Protein Molecular Weight Marker (Low)” manufactured by Takara Bio Inc. as a molecular weight marker, 40000 to 50000 ( A molecular weight band was observed at 40 kDa to 50 kDa).

Details of the molecular weight band confirmation method by the SDS-PAGE method were as follows.
(1) Molecular weight marker “Protein Molecular Weight Marker (Low)” manufactured by Takara Bio Inc.
Details of the reference substances are Phosphorylase B (molecular weight 97200), Serum Albumin (molecular weight 66409), Ovalbumin (molecular weight 44287), Carbonic anhydrase (molecular weight 29000), Trypsin inhibitor (molecular weight 20100), Lysozyme molecular weight 20300 and above. 2) Polyacrylamide gel Concentrated gel concentration 4.5% by mass and separation gel concentration 10.0% by mass (3) Sample solution Modified peptide or reference material 1 part by mass Bromophenol blue Appropriate sample solvent 1 mass Parts (sample solvent: sodium dodecyl sulfate 1 mass%, 2-mercaptoethanol 1 mass%, tris hydrochloride (pH 6.8) 10 mM, glycerol 10 mass%)
(4) Electrophoretic conditions 40 mA, 30 minutes (5) Electrophoresis tank buffer BioRed's “10 × (Tris / Glycine / SDS) Buffer” 10-fold diluted aqueous solution (6) Staining conditions 1 hour with Coomassie brilliant blue solution After dyeing, decoloring with decoloring solution for about 6 hours

Example 1
The shampoo-treated black hair with no history of coloring and permanent treatment was immersed in a 1% by weight aqueous solution of denatured peptide having a pH of 7.4, dried with warm air using a dryer, and then passed through water for 5 seconds. It was made to dry with warm air later with the dryer. Thus, the hair treatment of Example 1 was obtained.

(Comparative Example 1)
The hair treatment in the same manner as in Example 1 was omitted except that “warm air drying” before “passing in water for 5 seconds” in Example 1 was omitted.

  The hair surface after the treatment according to Example 1 and Comparative Example 1 was performed was observed at a magnification of 2000 using a scanning electron microscope (SEM). FIG. 1 is a SEM observation photograph of hair after treatment according to Example 1, and FIG. 2 is a SEM observation photograph of hair after treatment according to Comparative Example 1. Since the end-end cuticle is generally more unclear in the hair of FIG. 1 than the hair of FIG. 2, if there is warm air drying treatment (heating) before passing for 5 seconds in water, It can be confirmed that it is advantageous for adhesion of repair components.

(Example 2)
The treatment for repeating the hair treatment after “immersion in a 1% by weight aqueous solution of the modified peptide” in Example 1 30 times was defined as the hair treatment in Example 2.

(Comparative Example 2a)
A hair treatment that was carried out in the same manner as in Example 2 except that the “modified peptide 1% by mass aqueous solution” in Example 2 was replaced with “Promoice KR-30 (hydrolyzed keratin-containing solution) manufactured by Seiwa Kasei Co., Ltd.” was performed in Comparative Example 2a. Hair treatment.

(Comparative Example 2b)
The hair treatment was performed in the same manner as in Example 2 except that “1% by weight aqueous solution of the modified peptide” in Example 2 was replaced with “Keratech IFP-HMW (liquid containing 5% keratin) sold by Croda”. Hair treatment.

  FIG. 3 is a SEM observation photograph (2000 magnification) of the hair after treatment according to Example 2, FIG. 4 is a SEM observation photograph (2000 magnification) of the hair after treatment according to Comparative Example 2a, and FIG. It is a SEM observation photograph (2000 magnification) of the hair after the process by the comparative example 2b. The hair of FIG. 3 using a modified peptide has an obscure end-end cuticle, but the hair of FIGS. 4 and 5 using other peptides (hydrolyzed keratin and keratin) has an end-cuticle position. It can be confirmed clearly. That is, it can be confirmed that the use of the modified peptide is advantageous for the attachment of the repair component to the hair.

(Example 3)
2 g of the black hair bundle after the shampoo treatment and treatment treatment in which no history of coloring treatment and perm treatment was observed was immersed in an aqueous NaOH solution adjusted to pH 10.5 for 10 minutes and then washed with water. Next, 1 g of a 2% by weight aqueous solution of denatured peptide having a pH of 7.2 was applied to the black hair bundle and allowed to stand for 5 minutes, and then the black hair bundle that had been dried with warm air using a dryer was heated with a hair iron. The black hair bundle was immersed in water for 3 hours, and then dried with warm air using a dryer. Thus, the hair treatment of Example 3 was obtained.

  In the heating with the above-described hair iron, a pair of heating elements (a “thermal effect iron G regular” sold by Milbon Co., Ltd.) having a pair of plate-like heating elements (set temperature 120 ° C.) is used. The black hair bundle was passed three times between the heating elements while lightly pinching (pressurizing) the black hair bundle.

(Comparative Example 3)
Hair obtained in the same manner as in Example 3 except that the step of “applying 1 g of a 2% by weight aqueous solution of denatured peptide of pH 7.2 to a black hair bundle and leaving it for 5 minutes” in Example 3 was performed after “heating with a hair iron”. The treatment was the hair treatment of Comparative Example 3.

  FIG. 6 is a SEM observation photograph (2000 magnification) of the hair after the treatment according to Example 3, and FIG. 7 is a SEM observation photograph (2000 magnification) of the hair after the treatment according to Comparative Example 3. FIG. 6 in which a modified peptide aqueous solution is applied between “washing with NaOH aqueous solution for 10 minutes and then washing with hot air” and “drying with warm air with a dryer” is a residue on the hair surface (hair repair component) than FIG. 7. It can be confirmed that there are many.

Example 4
The hair treatment of Example 4 was carried out in the same manner as in Example 3 except that the treatment after “immersion in NaOH aqueous solution for 10 minutes” and the treatment after “immersion in water for 3 hours” in Example 3 was omitted.

FIG. 8 is an SEM observation photograph (2000 magnification) of the hair after treatment according to Example 4. It can be confirmed in FIG. 8 that a large amount of the repair component has adhered to the hair surface.

Claims (5)

A hair treatment agent applied to the hair before heating,
A modified peptide comprising one or more side chain groups having units selected from the structures represented by the following formulas (I) to (III) and salts of these structures is blended :
A hair treatment agent characterized by being heated to 60 ° C. or higher without being washed away .
_{-S-S- (CH 2) n} -COOH (I)
(In the formula (I), n is 1 or 2.)
—S—S—CH (CH ₃ ) —COOH (II)
-S-S-CH (COOH) -CH 2 -COOH (III) The hair treatment agent according to claim 1 , wherein a heating temperature in the heating is 80 ° C or higher. The hair treatment agent according to claim 1 or 2 , wherein the heating is performed together with pressurization of the hair. The hair treatment agent according to any one of claims 1 to 3 , wherein the modified peptide is formulated with a molecular weight of 2000 or more. The hair treatment agent according to any one of claims 1 to 4 , wherein the modified peptide has a molecular weight of 10,000 or more.