TW201105355A - Hair treatment agent and starting material for hair treatment agent - Google Patents

Abstract

Disclosed is a hair treatment agent in which a peptide that comprises a group having a unit represented by the following formula (I) as a side chain group is blended. -S-S-(CH2)nCOO- (I) (In formula (I), n represents 1 or 2.) The side chain group in the peptide is preferably composed of one or more members selected from among carboxymethyl disulfide groups, salts of carboxymethyl disulfide groups, carboxyethyl disulfide groups and salts of carboxyethyl disulfide groups. The molecular weight of the peptide is preferably less than 40,000. The peptide preferably has hair permeability.

Description

[Technical Field] The present invention relates to a hair treatment agent used for hair care treatment, perm treatment, decolorization treatment, and the like, and a raw material for a hair treatment agent for use in a number of treatments. Seven-shot treatment agent [Prior Art] Physical treatment such as hair combing, hand-held hair dryer, electric rod f, etc. Chemical treatment such as perm treatment, #会 》 hair treatment, hair, compared with before the injury, the hair touch: become a wound. After the injury, the illusion, appearance (such as age, organization), strength (such as tensile strength of the elastic L will be softened. In order to enhance the hair hair specialization, it is known that the appropriate selection will be modified (import = A hair ester-based modified substance such as a hair ester is blended with a hair treatment agent. A peptide of a natural product and, as described above, 'is known to blend hair-selecting peptides with appropriate selection: a physical agent to enhance hair characteristics Or inhibiting the deterioration of hair characteristics, and the modified peptide suitable for δ-mite blending is continuing to be sought. In addition, in Japan, the special Kaiping 7__ 12 is modified, and the modified form is the protein of the second: report + reveal - a methyl disulfide group (-SS-CH2C; a base of ruthenium (u-) is converted into 竣.L and H) and is water-soluble. Also, as a specific use aspect of the modified peptide,铼八初士_邮本特开平7 ~ 126296 #"There is no intention to form this modified peptide into a film agent. -And'", about the hair department [invention content] In view of the above circumstances, this The object of the invention is to provide an initial elastic modulus or a hair suppression treatment for hair that is damaged by 201,105,355. In the present invention, the present inventors focused on the initial elastic modulus of the hair and repeated the results of the research on the hair treatment agent, and found that the peptide having the predetermined side chain group was used. The ruler is used to treat the hair, and the hairy insight can be improved, and the present invention is completed. The initial elastic modulus is based on the preparation of the hair treatment agent of the invention, characterized in that it is blended with a side chain group. The side chain group has a unit represented by the following formula (1), -SS-(CH2)nC〇〇-(1) (wherein 'η is 1 or 2 in the formula (1)), the "peptide, θ社1 7 peptide of the present invention" Key bond, keratin; or ::: more than one amino acid, such as a needle mf or a protein such as a protein, is also a peptide. The side chain of the peptide may be selected from the base of the methyl group One or more, carboxymethyl disulfide or more. One or two of the aforementioned peptides, the molecular weight of the above-mentioned peptides, is below. If the present invention is less than 40,000, more preferably 20,000, the present invention The initial phase of the peptide, its molecular weight, and the 1 W ϊ ·+ range is less than 40,000, not only for the elevated fracture Degree or inhibition of deterioration. In the case of h, the peptide is preferably a peptide having permeability of hair permeability, and for hair, the initial deterioration of the elastic modulus and the breaking strength of the hair will be deteriorated. More preferably. ^, liter or the aforementioned peptide, may also be _ 〇 above 6_ below, the molecular weight range of the ^ set is 'for example or more than 49000 and 64000. Even if push 4 201105355 with this molecular weight range of peptides, The hair elastic agent of the present invention can be effectively used as a hair conditioner, a scalding agent, a decolorizing agent or a styling agent.

The hair treatment agent of the present invention is produced, for example, by using a hair material which is a solvent for dissolving a peptide having a side chain group (having a unit represented by the formula (I)) in a solvent such as water. In the following, -s- s-(CH2)nCOO (where η is 1 or 2 in the formula (I)), when the hair treatment agent of the present invention having a predetermined peptide is used, the initial stage of hair can be achieved. The increase in the elastic modulus or the suppression of deterioration. [Embodiment] Hereinafter, the present invention will be described based on the embodiments. The hair treatment agent of the present embodiment is obtained by blending a peptide having a predetermined side chain group (hereinafter, "a peptide having a predetermined side chain group" is referred to as a "CAD peptide"). (CAD peptide) The CAD peptide has a main chain formed by a peptide bond of a plurality of amino acids and a main chain of a side chain-based CAD peptide bonded to the main chain, and is not particularly limited. Examples of the main chain include the same as the main chain of the peptide which is composed of cysteine as the amino acid. Further, examples of the peptide which comprises cysteine as one of the amino acids include keratin and casein. This keratin is known to have a high proportion of cysteine even among peptides derived from natural substances, and is a raw material for efficiently obtaining the CAD peptide. From this point of view, the main chain of the CAD peptide is preferably the same as the primary key of the horned egg 5 201105355. The side chain group of the CAD peptide has a unit represented by the following formula (I), and in this side group, the disulfide group is disposed on the main chain side of the CAD peptide. Preferably, the side chain group is present in a plurality of CAD peptides. Further, a group represented by the following formula (I) is referred to as a carboxy root thiodithio group when dissociated (ionized) to form a carboxy root anion. -S-S-(CH2)nC00- (I) (in the formula (I), η is 1 or 2) is preferably a chemical structural unit of the above-mentioned side chain group, and is selected from the following formula (ΙΑ) a carboxymethyldithio group, a salt of a carboxymethyldithio group represented by the following formula (ΙΒ) or (1C), a carboxyethyldithio group represented by the following formula (ΙΙΑ), and the following formula (ΙΙΒ) or One or two or more kinds of salts of carboxyethyldithio groups represented by (IIC). -SS-CH2COOH (ΙΑ) -S-S-CH2COOR' (IB) (R1 represents ammonium such as NH4) -S-S-CH2COOM1 (IC) (M1 represents a metal atom such as Na or K) -S-S- CH2CH2COOH (IIA) -S- s-CH2CH2COOR2 (IIB) (R2 represents ammonium such as NH4) -S-S-CH2CH2COOM2 (IIC) (M2 represents a metal atom such as Na, K, etc.) The preferred group of the above-mentioned side chain group is One or more selected from the following formulas (la), (lb), (Ic), 201105355 (Ila), (lib), and (lie) (Ri, Μ1, R2, Μ2 in the following formula are the same as above) ). -CH2- S- S- CH2COOH (la) -CH2- S- S- CH2COOR1 (lb) -CH2- s- S- CHjCOOM1 (Ic) —CH2- s- s- CH2CH2CO〇H (Ha) -CH2- s - s- CH2CH2COOR2 (lib) -CH2- s- s- ch2ch2coom2 (lie) It is considered that if a hair treatment agent incorporating a CAD peptide having two or more of the above-mentioned side chain groups is used to treat hair, the hair base is formed. It will crosslink through the CAD peptide. Further, it is also considered that in addition to the cross-linking, a CAD peptide in which only one side chain group of the CAD peptide reacts with the thiol group of the hair, and only one side chain group reacts with the thiol group of the hair occurs, and other cad peptides Polymerization or polymerization of CAD peptides in the hair with each other. These crosslinks and reactions are presumed to achieve the following two points (1) or (2). (1) Increase the initial elastic modulus of hair or suppress deterioration. (2) Increasing the initial elastic modulus of the hair or suppressing deterioration, and improving the breaking strength of the hair or suppressing deterioration. As described in the above (1) and (2), it is suitable to use a CA 〇 treatment agent for the hair which is increased in sputum due to damage. = A detailed description of the cross-linking mechanism of the (10) peptide between a pair of sparse bases. The expression of ~ch2-t==peptide is as follows. The CAD of the side chain base is taken as an example. 201105355 (I)

Ke-SH + HOOCCH2- S- S-CH2-Ra, - CH2- S-S-CH2COOH + HS-Ke — Ke - S - S - CH2 - Ral — CH2 - S -S- Ke + 2HSCH2COOH

Ke: Keratin residue of hair

Ral: CAD peptide residue, the cross-linking mechanism of one of the hairs to the ruthenium through the CAD peptide, if the C AD peptide with two CH2-S-S-CH2CH2COOH as the side chain group is taken as an example, it is like Shown below. (chemical 2)

Ke-SH + HOOCCH2CH2- S- S- CH2-Ra2- CH2- S -S-CH2CH2COOH + HS-Ke ^ Ke- S- S- CH2- Ra2-CH2- S- S- Ke + 2HSCH2CH2COOH

Ke: Keratin residue of hair

Ra2 : CAD peptide residue The molecular weight of the CAD peptide of the present embodiment is not particularly limited. If the CAD peptides are roughly classified according to the molecular weight range, they can be classified into CAD peptides having a molecular weight range of less than 40,000 and CAD peptides having a molecular weight range of 40,000 or more and 67,000 or less. In the case of a hair treatment agent in which a CAD peptide having a molecular weight range of less than 40,000 is blended, the initial elastic modulus and the breaking strength of the damaged hair can be improved or the deterioration can be suppressed. The smaller the molecular weight of the CAD peptide, the more advantageous it is to improve the initial elastic modulus and the breaking strength of the hair, or to suppress the deterioration. Therefore, the molecular weight range of the CAD peptide of the present embodiment is preferably 20,000 or less, more preferably 10,000 or less, 201105355 Good for 5000 or less. The lower limit of the molecular weight range of the CAD peptide is not particularly limited and is, for example, 500. The molecular weight range of the CAD peptide is less than 40,000, and the m/z peak measured by time-of-flight mass spectrometry (TOFMS) (substrate-assisted laser desorption free method (MALDI method)) is taken as the molecular weight of the CAD peptide. This can be confirmed by the molecular weight range. In the result of the TOFMS, it is preferable that the peak of the highest intensity is m/Z 20000 or less, and it is more preferable to confirm that it is m/z 10000 or less, and it is preferable to confirm that it is m/z5000 or less. By. The lower limit of the peak of the highest intensity is not particularly limited. For example, if the m/z500 ° CAD peptide has hair permeability (permeability to the inside of the hair), the above-mentioned crosslinking and the like may occur inside the hair. Therefore, the CAD peptide of the present embodiment is preferably one having hair permeability. The CAD peptide has hair permeability and can be confirmed by the following steps (1) to (4). (1) Add FTSC-MES to the aqueous solution of CAD peptide. The FTSC - MES is modulated as follows. Into a solution obtained by dissolving 1.065 parts by mass of 2-(N-MORpholino)ethanesulfonic Acid (MES) in 40 parts by mass of water, an aqueous solution of 0.2 Μ-N a Ο 滴 was added thereto, thereby preparing ρΗ5.5. In the MES aqueous solution, 0.0004 parts by mass of the fluorescent pigment Fluorescein-5-thiosemicarbazide (FTSC) was dissolved in an aqueous MES solution, and then water was added to a total amount of about 50 parts by mass to prepare FTSC-MES. (2) The original hair was immersed in a CAD peptide aqueous solution after adding FTSC-MES for 10 minutes, and the hair was washed with water and dried at room temperature. (3) The dried hair was cut (❶) by a 201105355 microtome to observe the cut surface of the hair (excitation light wavelength: 340 nm) with a fluorescence microscope. In the fluoroscopy microscopic observation in the above step (4), if the fluorescence was confirmed on the inner side of the stratum corneum, the hair permeability of the CAD peptide was confirmed. Fig. 1 is a view showing the hair permeability of the CAD peptide by confirming the fluorescence of the inside of the hair by the observation of the fluorescence microscope obtained by the above steps (〇 to (4). On the other hand, Fig. 2 shows The fluorescence microscope observation photograph obtained by performing the above steps (1) to (4) without blending the CAD peptide can confirm that only the surface layer of the hair has the camping light, and it can be called because the CAD peptide is not blended, so It has hair permeability. The fluorescent microscope observation photograph of Fig. 2 cannot confirm the fluorescence inside the hair, because even if only the fluorescent substance penetrates into the inside of the original hair, the inside of the original hair is not chemically damaged, so the subsequent washing is performed. The fluorescent material also flows out to the outside of the hair.

When a hair treatment agent containing a CAD peptide having a molecular weight of 40,000 or more and 67,000 or less is blended, the initial elastic modulus of the damaged hair can be improved or the deterioration can be suppressed. The molecular weight of the CAD peptide can also range from 49〇〇〇 to 64〇〇〇. The molecular weight calculated by the relative distance between the band of the CAD peptide obtained by Sodium Dodecyl Sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and the molecular weight marker band is regarded as the molecular weight of the CAD peptide, and From this range, it was confirmed that the molecular weight of the CAD peptide was in the range of 4 (9) (9) or more and 67,000 or less. The lower limit of the amount of the CAD peptide blended in the hair treatment agent of the present embodiment is not particularly limited, and may be 〇〇1% by mass, preferably 〇〇5% by mass, more preferably 〇.1〇% by mass. . On the other hand, the upper limit of the amount of the CAD peptide blended is not particularly limited. The 201105355 is particularly limited, and may be 15% by mass, preferably 10% by mass, and more preferably 5, from the viewpoint of suppressing the increase in cost due to the large amount of use. The mass %, more preferably 3% by mass. Further, when the hair treatment agent blends a CAD peptide having a molecular weight range of less than 40,000, a CAD peptide other than the CAD peptide having a molecular weight range of less than 40,000, for example, a CAD peptide of 40,000 or more and 67,000 or less may be further blended. Further, when a CAD peptide having a molecular weight of 40,000 or more and 67,000 or less is blended, a CAD peptide having a molecular weight of not more than 40,000 to 67,000 or less, for example, a CAD peptide having a molecular weight range of less than 40,000 may be further blended. (Manufacturing method of CAD peptide having a molecular weight range of less than 40,000) The method for producing a CAD peptide having a molecular weight range of less than 40,000, for example, the production methods (A), (B) and (C) described below can be mentioned. [Production Method (A)] The production method (A) includes a reduction step of converting a disulfide group of a protein into a mercapto group, and a mercapto group formed in the protein molecule and a mercapto group of a mercaptoalkylcarboxylic acid in the reduction step, / or a mercapto group of a mercaptoalkyl carboxylate, forming a modification step of the unit represented by the above formula (I); hydrolyzing a protein (indicated by the above formula (I) obtained by the upgrading step) The hydrolysis step. In the reduction step, the disulfide group (_S_S-) contained in the protein is reduced to two sulfhydryl groups (-SH HS-) by mixing the raw material containing the protein, water and a reducing agent. Examples of the raw material to be produced include keratin as a constituent protein of wool (Melino wool, Lincoln wool, etc.), human hair, animal hair, feathers, nails, and the like. S- 11 201105355 ‘It is preferred to degrease, wash and cut the material from the wool. In this case, in order to obtain the raw material in a cheap and stable manner, it is possible to combine the sterilization, the crushing and the drying in a suitable combination, and to carry out the treatment in advance. The amount of κ is particularly limited, e.g., relative to the mass of the raw material to be produced, and the reduction reaction can be carried out smoothly in an amount of 20 parts by mass or more and 2 parts by mass of r.

The reduction of the protein in the reduction, in + tA ', in an alkaline liquid, by one or two or more reducing agents, the protein is temporarily reduced to a disulfide bond in the protein to form a Wei group 0 for The anti-reagent system for reducing such a disulfide bond is an inspective compound (aged compound) which is made alkaline by adding it to water. Examples of the basic compound include lithium hydroxide, hydrogen y L sodium hydride, mouse potassium oxide, and hydrogen hydroxide.

钡, sodium carbonate 'potassium carbonate, ammonia guanidine, I ^ 虱 其他 other examples of monoethanolamine, diethanolamine, arginine, lysine and other alkaline guanamine amino acid or sodium hydrogencarbonate, ammonium hydrogencarbonate and the like. Here, from the viewpoint of performing protein reduction inexpensively and efficiently, it is preferable to use sodium hydroxide or oxymethanol emulsified potassium, and sodium arsenate is particularly preferable. The basic compound may be used in one type or in two or more types. The amount of the above-mentioned basic compound to be mixed is not limited, and it is only necessary to adjust the pH of the reduction reaction system to the following target. The lower limit of this pH is preferably 9, particularly preferably 10. On the other hand, the upper limit of PH can be 13, which is 12, and the best is 11. When the pH is adjusted to the above 4 r limit, the protein can be efficiently reduced. On the other hand, the pH is adjusted to be less than or equal to the above upper limit, and the cleavage of the main chain of the protein molecule can be suppressed. A mercaptoalkyl carboxylic acid and a potting can be used as a reducing agent. Further, in addition to the 12, 2011,053,55 2, a melityl acid and/or a salt thereof, any other sigma may be used as the reducing agent. Examples of such an optional reducing agent include thioprecipitate and/or a salt thereof, monothiothreitol, 2-thioethanol, glutamine sulfur, thiourea, and the like. Any one or two or more of these optional reducing agents may be used. The above-mentioned base acid and/or a salt thereof is also formed in the reforming step to form a unit represented by the above formula (I), and is selected from the group consisting of the acid and/or its salt. A type or a mixture of two or more of acetic acid, erythric acid salt, 3-propionic acid, and 3-propionate. The acetic acid salt is exemplified by sodium acetate, potassium cesium acetate, lithium ruthenium acetate, and ammonium phthalate acetate. Among them, from the viewpoint of being able to form a carboxymethyl group disulfide group with good efficiency, it is preferred that sodium phthalate and potassium acetate are more preferably sodium phthalate. Further, the 3-propionate salt may, for example, be sodium 3-propionate, potassium 3-propionate, lithium 3-propionate or ammonium 3-propionate. Among them, from the viewpoint of forming a carboxymethyl group disulfide group with good efficiency, sodium 3-propionate and potassium 3-propionate are preferred, and sodium 3-propionate is more preferred. The amount of the above-mentioned sulfhydryl-based acid and its salt is preferably based on the raw material of the raw material, preferably 0,0050 m or more, 〇2 mol or less, and particularly preferably 〇〇〇75 m or more and 0.01 mol. the following. Further, the amount of use is preferably 〇. l〇m〇i / l or more 〇.40 mol/L or less, based on the raw material, water and reducing agent, and g. Above 〇25m〇1/L or less. By using the amount of the mercaptoalkylcarboxylic acid and the salt thereof in the above range, the reduction reaction of the protein can be smoothly performed. The lower limit of the temperature of the reaction system in the reduction step is preferably 2 CTC, more preferably 30 ° C' and still more preferably 40 ° C. On the other hand, the above upper temperature limit is preferably 13 '5 201105355 60 C. When the right is lower than the lower limit of the above temperature, the reduction time for converting the disulfide group of the protein into a mercapto group is elongated, and there is a possibility that the reduction cannot be sufficiently carried out. On the other hand, if the temperature is exceeded, the main chain of the protein molecule is cleaved. The set time of the reduction reaction system is set to be longer as the temperature is lower. The higher the temperature, the shorter the setting. This setting time is, for example, 20 minutes or more and 12 minutes or less. In the modification step, the unit represented by the above formula (1) is introduced into the protein by mixing the acid and the oxidizing agent with the liquid obtained in the reduction step. Further, the mixing of the acid may be carried out before the oxidizing agent is mixed, after the oxidizing agent is mixed, and at the same time as the mixed oxidizing agent. The acid is used to lower the pH of the reaction system of the upgrading step, and the unit represented by the above formula (1) is sufficiently introduced to the protein. This acid may be used in one type or in two or more types. ~ State 岐, 醏殴 and other organic s hydrochloric acid and other inorganic acids. If acetic acid is used, the problem of the odor of the CAD peptide may be caused. If citric acid or the like is used, the mixing amount of the specific odor acid may be suppressed without any particular limitation, as long as the blending reaction will be a modification step. The pH of the system can be adjusted to the following range. Finally, it is preferable that the above 9 is T, and particularly preferably 6 or more and 8 or less. In this way, the final pH of the horn solution is adjusted to the above range, whereby the unit shown above can be promoted to the protein while suppressing the (di) disulfide group formed by the protein. Further, when the yang of the reaction system is locally lowered, the possibility that the sulfhydryl groups of the protein become disulfide groups becomes large, and it is preferred to slowly mix the acid in the reaction system. ^ 14 201105355 The temperature of the sigma-acid reaction system is preferably above and below 20 C and below 40 C. By controlling this temperature range, formation of oxidized cystine or the like, which is one of the by-products, can be suppressed. The standing time after completion of the acid mixing can be, for example, 1 hour or longer and 48 hours or less. If the time is set for this, the unit represented by the above formula (1) can be sufficiently guided. The above oxidizing agent is used to promote the introduction of the unit represented by the above formula (1) into the protein. One or two or more oxidizing agents may be used. The oxidizing agent' may, for example, be sodium sulphate, potassium oxychloride, sodium chlorate, hydrogen peroxide or the like. The amount of oxidant used is not particularly limited to 1 liter/man, and is based on the raw material lg: preferably, it is less than or equal to mAh, and is preferably based on the capacity of the liquid after mixing the oxidant. Dry and live horse 0.02m 〇 18 or more - ... 80% of the oxidant used in an amount greater than the above upper limit, there is the formation of by-products - money cysteic acid, dicysteine, and semi-tetracarboxylic acid. On the other hand, if the amount of the oxidizing agent used is less than the above lower limit value, the unit indicated by () will be insufficiently introduced. When the oxidizing agent is mixed, in order to avoid local concentration of the oxidizing agent in the liquid, the oxidizing agent aqueous solution of lm〇1 is slowly mixed in, for example, 30 minutes or less. The temperature at which the oxidizing agent is mixed is less than or equal to about 5 mol and less than or equal to the temperature of the reduction step. (7) Restriction ' For example, it can be set to express the above formula (1) to a protein by a modification step. For example, the use of a single 7, early introduction of the field using flat hair as a raw material, and Estonia as a reducing agent, is the carboxylic acid of the above formula (1) as a kind of carboxymethyl bis 15 S- 201105355 thio group The mechanism introduced into the protein molecule, as shown below β (chemical 3)

Pro-CH2-SH + HS~CH2COOH - Pr〇 - CH2 - S - S-ch2cooh

Pr. In the case of a protein molecular residue, when a wool is used as a raw material for production, and 3-propionic acid is used as a reducing agent, a mechanism in which a carboxyethyldisulfide group of one of the units represented by the above formula (1) is introduced into a protein molecule, such as Shown below. (4)

Pro — CH2 — S

CH2-SH + HS-CH2CH2COOH —S - CH2CH2C〇〇H

Pr. : The protein molecular residue is introduced into the protein of the above formula by the treatment of the virulence step & @ i 改 of the upgrading step, and contains a liquid which is soluble in the water and has such a protein in the early place, as needed: white Desalting of g S, etc.耷 仃 仃 父 换 换 ' 电 电 电 ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' ' (10) By the hydrolysis of hydrolyzed by the test, (10) by the hydrolysis method (a3), there is a "heart two I solution method. The above formula of the levy of the unit by the test of the 10,000 detachment reaction (υ The medium 'is preferably a method for hydrolyzing the enzyme or acid (4)) to (10) (al) by the hydrolysis of the enzyme to the method of the straw by the enzyme. 16 201105355 : prime, such as pepsin, protease A, protease b Such as acid white matter decomposition enzyme; papain, pineapple enzyme, thermolysin, bond white enzyme, chymotrypsin, chymotrypsin and other neutral protein decomposing enzymes /, commercially available protein decomposing enzymes, for example, Daiwa Chemical Industry Co., Ltd. "Pr〇telyzer A" manufactured by the system 1. The pH at the time of hydrolysis can be adjusted to 1 or more and 3 or less when the acidic protein is used. When the neutral proteolytic enzyme is used, it can be adjusted to 5 or more and 9 or less. The reaction temperature during hydrolysis can be 3 〇C above, below 60 °C, the reaction time can be more than 10 minutes, less than 24 hours (the longer the reaction between the two, the more the lower molecular CAD peptide can be produced to stop the hydrolysis - the temperature to 7 (rc above the enzyme) (a2) The acid-hydrolyzed acid may, for example, be an organic acid such as hydrochloric acid, sulfuric acid, phosphoric acid, nitric acid or hydrogen bromide, or an organic acid such as formic acid or oxalic acid. Below pH*, the reaction temperature is 40 ° C or more and l〇〇t or less, and the reaction time is 2 hours or less within 4 hours (the longer the reaction time, the lower the molecular weight of the ruthenium peptide can be produced). (a3) Hydrolysis of alkali by alkali Examples thereof include sodium hydroxide, potassium hydroxide, lithium hydroxide, sodium strontium carbonate carbonate, potassium carbonate, a carbonate chain, sodium bismuth, sodium sulphate, etc. The hydrolysis conditions are, for example, relative to the reaction system. The total mass is 1% by mass or more and 20% by mass or less, and the reaction temperature is 15. (: Above l〇 (TC below, reaction time is 30 minutes or more and 24 hours or less (the longer the reaction time, the lower the molecular weight of CAD can be manufactured) Peptide) can be dissolved by the hydrolysis step Molecular weight range of less than

S 17 201105355 40000 liquid of CAD peptide. When it is necessary to divide the solid component contained in the liquid, it can be separated by a known solid-liquid separation method such as filtration, centrifugation, press separation, sedimentation separation, or floatation separation. Moreover, when it is necessary to make the CAD peptide having a molecular weight range of less than 40,000 solid, it is possible to use: (1) CAD peptide solution (four) knot drying, (7) (d) spray drying of the peptide solution, and (3) addition of acid to make the pH of the CAD peptide solution from 25 becomes about 4〇, in order to generate a CAD peptide precipitate or the like (the smaller the molecular weight of the CAD peptide, the more difficult the method of the above (3) is to generate a CAD peptide and the solid CAD peptide for the recovered Washing and drying of water or acidic aqueous solution [manufacturing method (Β)] μ manufacturing method (Β) is purchased from water-insoluble egg yolks (in the same reduction and modification steps as in the manufacturing method (Α)) A method in which a Ding knife is separated and then subjected to a hydrolysis step. The water-insoluble protein is temporarily recovered by a known solid-liquid separation method. The hydrolysis step of the production method (Β), the hydrolysis of the disk (Α) The steps are the same. In addition, the method of obtaining the solid CAD ^ hurricane can be carried out by the method of the manufacturing method (A). In addition, the microfibril and the sulfur content are more than the formation angle of the matrix-shaped wool of the Rising fiber. Protein, in the manufacturing method m battle for In the hydrolysis step of B), the water-soluble protein derived from microfibrils is mainly hydrolyzed to be derived from the water-insoluble protein 基质 of the matrix, and the main hydrolysis object of 疋贝冯. β) is suitable for the production of cad with a large sulfur content [manufacturing method (C)] manufacturing method (C), which is soluble in water

Change the mussels (to the 匍 匍; i large, also γ A the same reduction step and the upgrading step obtained H ~, the table 10,000 to (A) into the 仃 separation, and then treated with hydrolysis step 18 201105355 Method: The protein dissolved in water can be recovered by a known solid-liquid separation method. The hydrolysis step of the production method (c) is the same as the hydrolysis step of the production method (A). Further, a method for obtaining a solid CAD peptide can be employed. The method of the production method (A) (method of producing a cad peptide having a molecular weight of 40000 or more and 67,000 or less), for example, a method of omitting the hydrolysis step of the above production method (c). (Hair treatment agent) The hair treatment agent is not particularly limited, and may be a hair conditioner, a perm agent, a coloring agent, a decolorizing agent, a styling agent, etc. "Hair-care agent" is a hair treatment used for hair repair, treatment, and the like. The hair conditioner may, for example, be a shampoo, a conditioner, a hair conditioner, a hair conditioner (for example, a non-rinsing conditioner, a rinse-off conditioner, a hair conditioner which can also be used as a hair conditioner, and more A kind of agent-type hair care Xin (4),. The constituents of the complex f, the hair conditioner before the perming, the conditioner for the treatment after perm, the conditioner for the dyeing treatment, the conditioner for the post-staining treatment, Hair conditioner before decolorization, hair conditioner for decolorization treatment.) "Perm agent" is used for the use of 屌 屌; 5 temple preparation + invitation r, € original reaction, oxidation reaction and other chemical reactions A hair treatment agent which changes the hair shape. For example, a hair curling agent such as a curling agent, a hair straightening agent for making a hair such as a roll, a one-side hair curling agent, and 2 The direct agent of the sword and the "i" 媒 才 1 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发 卷发"Whitening agent" is a hair treatment agent used for coloring hair 19 S-201105355. Direct dyes (4) ^ Listed if blended with ~" Hair dyeing requires the dyeing of the temple dye Agent's hair coloring material for temporarily coloring the hair ^Reaction type ^In order to remove the pigment from the hair The hair treatment agent used is the hair treatment agent used for temporarily maintaining the hair style. The type of the treatment agent (4) is not particularly limited to liquid, emulsion or lotion. Lotlon), frost: phantom solid shape, foamy shape (bubble), misty. Medical coagulation knee, for example: two: CAD peptide 'that is in accordance with the hair treatment agent of this embodiment. The leather (four) ^ (8) as It is known that the additional blending raw material of the hair treatment agent is J', and the hair treatment agent blended with the CAD peptide as a substitute raw material for the known hair treatment agent is in accordance with the actual treatment agent. ^~工> 犮Use of a hair treatment agent other than the above-mentioned hair treatment agent in the above-mentioned conditions (4) A well-known raw material appropriately selected. The known raw material for the treatment agent is an anionic surfactant, a cationic surfactant, a f-site surfactant, a nonionic surfactant, an alcohol, a polyol, a sugar, a fat, a vinegar oil, a fatty acid, a hydrocarbon, and a wax. , Ju Shi Xi oxygen, synthetic macromolecular. 'Semi-synthetic molecular compounds, natural polymer compounds. Other well-known hair treatment agent raw materials include protein, amino acid, animal and plant extract microorganisms, inorganic compounds, perfumes, preservatives, miscible spacers, ultraviolet absorbers, pigments, reducing agents, oxidizing agents, dyes, pigments. Etc. 'Anionic surfactants, such as fatty acid salts, alkyl ether carboxylic acid 20 201105355 salt, fatty acid guanamine ether carboxylate, fatty acid guanamine ether carboxylic acid, thiol lactic acid

Mercapto hydroxyethyl phthalate, alkoxy epoxide etherate, alkyl succinate, alkyl sulfoacetate, alkane sulfonate, alkylnaphthalene sulfonate, N-methyl sulfonate

Acid alkanolamine sulfate, fatty acid monoglyceride sulfate, alkane phosphate, polyethylene oxide ether phosphate, alkyl aromatic ether phosphate, fatty acid indoleamine phosphate. The blending concentration of the anionic surfactant can be appropriately set depending on the use of the hair treatment agent, for example, 〇·% by mass or more and 2% by mass or less. The cationic surfactant may, for example, be an alkylamine salt, a fatty acid guanamine amine salt, an ester-containing tertiary amine salt, a polyamidamine polyamine type 3 amine salt, a long-chain alkyltrimethylammonium salt, or a long-chain alkane. Dimercapto ammonium salt, tri-long alkyl alkanoyl ammonium salt, hydroxyaniline type 4-grade ammonium salt, monoalkyl ether type 4-grade ammonium salt. The blending concentration of the cationic surfactant can be appropriately set depending on the use of the hair treatment agent, and is, for example, 0.1% by mass or more and 20% by mass or less. The amphoteric surfactants may be exemplified by alkylglycinate, carboxymethylglycinate, N- ugly amine ethyl-2, ethylglycol oxime double salt, and 9 polyamine polyglycolate. , alkylamine propionate, alkylimidodipropionate, N_decylamine ethylhydroxyethylpropionate, alkyl dimethylamine acetate betaine, fatty amidoxime monodecylamine acetate beet Alkali, alkanedihydroxyethylamine acetate beet

Monomethylamino-N-propyl acid salt, N-alkyl N-(2-hydroxypropyl) sulfonate, N-fatty acid hydrazino 氦~N — (2-propyl) acid salt. The degree of amphotericity can be appropriately set according to the use of the hair treatment agent 21 201105355, for example, 0.1% by mass or more and 1% by mass or less. Nonionic surfactants, for example, polyethylene oxide (10), polyepoxyethyl propylene oxide ether, polyepoxyethyl fatty acid vinegar, polyepoxyethyl sorbitol needle fatty acid vinegar, polyethylene oxide A sorbitol four fatty acid vinegar, a glycerin fatty acid vinegar, a sorbitol liver fatty acid brewing, a polyglycerin fatty acid vinegar, an axe ^ fat. The blending concentration of the nonionic surfactant can be appropriately set according to the use of the hair: physic agent, for example, 〇.丨% by mass or more and 〇2% by mass or less. 0. Alcohols are listed as butanol 'lauryl alcohol, myristicol (4) alcohol, hard linoleyl alcohol, isopropanol, octadecanol, isostearyl alcohol, root benzyl alcohol, cholesterol, phytosterol. The blending concentration of the alcohol, the amount of the treatment agent can be appropriately set, for example, 1% by mass or more and 5 parts. The polyhydric alcohol may, for example, be ethylene glycol, diethylenedipropylene glycol, glycerin, glycerol, propylene glycol or propylene glycol, and may be used according to hair, and butyl alcohol. The blending concentration of the polyol and the mass % are appropriately set as, for example, 1% by mass or more and 5%. Examples of xylose include sorbitol, mannitol 'glucose, fructose, combined concentration, 矸4 maltose, hydrogenated maltose, and bacteriocin. The η of the saccharide is appropriately set depending on the use of the hair treatment agent, for example, 10% by mass. Oily moon, rushing, evening primrose can be enumerated as almond oil, luli oil, scented oil, shea butter, 粑 由, camellia oil, peanut oil, rosehip oil. The blending of fats and oils is appropriately set according to the use of the hair treatment agent, for example, 〇丨 mass% 22 201105355 or more and 1 〇 mass% or less. s oil, for example, ethyl oleate, meat beans recorded a isopropyl ester, palmitic acid isopropyl hydrazine, hard (four) Ding cool, brown yue _ purpose, meat beans M acid peas vinegar, meat ugly Sour acid sesame vinegar, iso-stearic acid isopropyl alcohol, isostearic acid ethyl 312-ethylhexanoic acid recorded «, isostearic acid hexane vinegar, diethylhexanoic acid B vinegar, oleic acid Vinegar, bis (xin. decanoic acid) propylene diacetate, propylene diacetate, diisostearic acid tripropyl propyl vinegar, tetra-2-ethylhexanoic acid neopentyl vinegar, isostearyl: known wax Stuffed, dimethyl octanoic acid 2-octyl vinegar, lactic acid nutmeg vinegar, citric acid-octadecane ester, diisostearyl malate, succinic acid di-2-ethyl, hydrazine, azelaic acid Butyl ester, cholesteryl stearate. The blending concentration of the ester oil can be appropriately set depending on the use of the hair treatment agent, for example, enamel & mass % or less. The upper 10 ^ fatty acid may, for example, be isostearic acid, oleic acid 'tannic acid, stearic acid' :=黾, hydroxystearic acid, behenic acid, myristic acid, lauric acid, aqueous sheep: known fatty acid, sub Sesame oil. The blending concentration of the fatty acid can be appropriately set according to the use of the hair or the rinsing agent, for example, 〇丨% by mass or more and 〇% by mass for woven, and examples thereof include liquid, thirty carbon burn, eighteen carbon burn, and ground stone. Bad, pure soil, petrolatum, microcrystalline. The concentration of the smoke is 20 艮, and the use of the treatment agent is appropriately set, for example, (M f %% or more of the purchase amount or less. Wax: Eight: two such as beeswax, wood wax, candelilla wax , Brazil brown wax. 〇丨 * σ / Chen can be appropriately set according to the use of the hair treatment agent, for example, 1% by mass or more and 20% by mass or less.

23 S 201105355 Polyoxyl oxide, for example, dimethyl polyfluorene oxide, tolyl polyoxymethylene, cyclic dimethyl polyoxo, alcohol modified polyoxane, calcined modified polyoxyl, amine modified Polyoxyl. The blending concentration of polyoxymethylene can be appropriately set depending on the use of the hair treatment agent, and is, for example, 0.1% by mass or more and 50% by mass or less. The synthetic polymer compound may, for example, be a carboxyvinyl polymer, a polyvinyl alcohol, a polyvinylpyrrolidone, a polyacrylic acid or a methacrylic acid ethyl betaine methacrylate copolymer. Examples of the semisynthetic polymer compound include mercaptocellulose, ethylcellulose, propylcellulose, and "methylcellulose" soluble starch. Further, examples of the natural polymer ' can be, for example, sodium alginate, guar gum, dextran, cellulose, or sodium hyaluronate. The blending concentration of the synthetic polymer compound and the semi-synthetic polymer compound 'the natural polymer compound can be appropriately set depending on the use of the hair treatment agent, for example, 〇1% by mass or more and 5% by mass or less. In the hair treatment agent of the present embodiment, it is possible to blend a CAD shape with a suitably selected hair treatment agent raw material. The combination ratio of the cad shape to the material to be pushed is as follows. Combination of raw materials for hair conditioner, ^Interfacial activity: agent, polyfluorene oxide, polymer compound (synthetic polymer compound half 〇 问 knife compound or natural polymer compound phenol, mis-separating agent and water. Soup #* The combination of the raw materials of the scald perm agent, for example, the first agent in the perm for the perm (hanny acetic acid, cysteine, acetyl cyanoic acid, cysteamine perm second: hydrogen bicarbonate, arginine, etc.) And water and as a combination of raw materials, such as dyes, alcohols, high: two::: W compound, semi-synthetic polymer compound or natural macromolecular:) 24 201105355 and water. A combination of the raw materials of the decolorizing agent, such as a permeating agent and water.造型 屌 虱 虱 虱 虱 虱 虱 虱 虱 虱 虱 虱 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型 造型) surfactant, alcohol. In the case of the raw material to be blended by the hair treatment agent, it is preferable to use a side chain group (having the following formula (1) - '8). The unit of the formula (1) The peptide is dissolved in the solvent (I) s-(CH2) nc (wherein η is 1 or 2 in the formula (I)) The solvent is not particularly limited, and for example, water, ethanol or the like can be used. In addition, the content of the peptide in the raw material for a hair treatment agent is not particularly limited, and is, for example, 0.1% by mass or more and 10% by mass or less. The peptide dissolved in the solvent is, for example, one having a molecular weight range of less than 0 and a molecular weight of from 40000 to 67,000. [Embodiment] Hereinafter, the present invention will be described in more detail with reference to the following embodiments. The present invention is not limited to the following embodiments as long as it does not deviate from the gist of the present invention. The CAD peptides (la), (lb), (2a), and (2b) having a molecular weight range of less than 4 (9) (9) and the CAD peptide (3) having a molecular weight range of 4 Å or more and 67,000 or less used in the hair treatment agent of the examples are as follows Said. In addition, the CAD peptides (1 hook, (ib), (2a), and (2b) have hair permeability, while the CAD peptide (3) has no hair permeability. (CAD peptide (la)) According to the reduction step shown below, The modification step and the hydrolysis step produce the peptide (la). 25 201105355 [Reduction step] The merino wool washed and dried with a neutral detergent is cut into about 5 mm. 5.0 parts by mass of this wool, 30% by mass 15 parts by mass of an aqueous solution of sodium hydrazineacetate and 8.5 parts by mass of a 6 mol/L aqueous sodium hydroxide solution were mixed, and further mixed with water to prepare a mixture of a total amount of 150 parts by mass and pH 1. The mixture was at 45 ° C. After stirring for 1 hour, the mixture was further mixed with water to make a total amount of 200 parts by mass, and was placed at 45° (:, 2 hours, and then naturally cooled until the liquid temperature became normal temperature. [Modification step] while stirring and reducing After the step, the mixture was mixed with 25 parts by mass of an aqueous solution containing 2.05 parts by mass of sodium bromate for about 60 minutes, and then the mixture was stirred from the beginning to the end, and the mixture was stirred for about 85 minutes. 7.80 parts by mass of citric acid in aqueous solution The mixture was mixed with the mixture, and the pH of the liquid after mixing the citric acid was 7. [Hydration step] 100 parts by mass of the solid portion and 3% by mass of the aqueous solution of the proteolytic enzyme were obtained by separating the mixture obtained by the modification step. ("Protelyzer A" manufactured by Daiwa Chemical Co., Ltd.) 1 part by mass of sodium hydrogencarbonate and water having a pH of 8 〇 to 8·5, and mixed, and hydrolyzed in 50: (: water for 20 minutes. Thereafter, at 80C, 5) The conditions of the minute deactivate the proteolytic enzyme. After deactivation, the aqueous solution of the CAD peptide (la) is obtained by filtration. The molecular weight analysis result of the CAD peptide (la) is roughly from ι to 3600 (lkDa to 3.6kDa). In addition, in the molecular weight analysis of the CAD peptide (u), "AXIMAPerformance" 26 201105355, manufactured by Shimadzu Corporation, was used as a laser free time-of-flight mass spectrometry device (MALDI - TOFMS), and the induced voltage of the analysis condition was 20 kV. The flight mode is Linear, and the detection ion is %. Further, the substrate is α-nitrile 4-hydroxy cassia in an aqueous solution of 0.1% by mass of tetragastoacetic acid and 5% by mass of B. (CHCA) 5mg persons. FIG. 3 is a CAD peptide (La) of FIG T〇FMS analysis' of the upper substrate just the graph, as the lower base

A chart containing the CAD peptide (la) in the plastid. The molecular weight of the CAD peptide (la) is as shown in Fig. 3, and it is confirmed to be in the range of approximately 1,000 to 3,600 (lkDa to 3.6 kDa). (CAD Peptide (lb)) A CAD peptide (ib) having a molecular weight smaller than that of the CAD peptide (la) was produced in the same manner as in the production of the CAD peptide 〇a) except for the step of changing the hydrolysis. The hydrolysis step for producing the CAD peptide (lb) is as follows. [Hydration step] A solid portion 100 stalk fraction and a 3% by mass of a proteolytic enzyme solution (a mass fraction of "pr〇telyzer A" manufactured by Daiwa Chemical Co., Ltd.) and a pH of 8 were obtained by filtration. 〇~8 5 of sodium hydrogencarbonate and water were mixed, and hydrolysis reaction was carried out for 5 minutes in 5 (TC water). Thereafter, the proteolytic enzyme was inactivated at 80 C for 5 minutes. Then, 3 mass% of protein was mixed. The decomposing enzyme aqueous solution ("Pr〇telyZerA" manufactured by Daiwa Chemical Co., Ltd.) was mass-produced, and the hydrolysis reaction was carried out under the conditions of 5 Torr and 2 Torr, and the proteolytic enzyme was inactivated at 8 Gt: for 5 minutes. An aqueous solution of the CAD peptide (lb) was obtained by filtration. (CAD peptide (2a)) In the same manner as the manufacture of the CAD-like 〇a), except for the change-modification step,

S 27 201105355 A CAD peptide (2a) having the same molecular weight as the CAD peptide (la) was produced. The upgrading step for producing the CAD peptide (2a) is as follows. [Modification step] While stirring the mixed solution after the reduction step, an aqueous acetic acid solution (165 parts by mass of an aqueous solution containing 7 parts by mass of acetic acid) was mixed, and the pH of the keratin mixture was gradually adjusted from 11 to 1 Torr. The mixing of hydrogen peroxide was carried out for about 30 minutes while stirring and stirring 36 parts by mass of 3 parts by mass of 35 mass% hydrogen peroxide water. After the start of the mixing of the hydrogen peroxide, the mixture was stirred at any time, and the aqueous acetic acid solution was mixed to maintain the pH at 1 Torr or more and 11 or less. Further, after the completion of the mixing of hydrogen peroxide, about 1 minute of the aqueous solution of acetic acid was slowly mixed for about 5 minutes, and the pH of the mixture was gradually adjusted from 1 to 7. (CAD Peptide (2b)) A CAD peptide aqueous solution was obtained in the same manner as the CAD peptide (lb) except that the upgrading step was carried out using the modification step in the production of the CAD peptide (2a). Then, this aqueous solution was used as a semipermeable membrane to obtain an aqueous solution of the cad peptide (2b) having a molecular weight range of 1 〇〇〇 or less. Further, the semipermeable membrane used for obtaining the cad peptide (2b) was cut into "spectra/p〇r" manufactured by Spectrum Corporation having a molecular weight of 1,000, a plane width of l〇mrn, and a diameter of 6.4 mm. (CAD Peptide (3)) The liquid portion obtained by filtering the mixture obtained by the modification step after the production of the CAD peptide (1 a) was obtained as an aqueous solution of the CA D peptide (3). The molecular weight of the CAD peptide (3) was determined by the "Protein Molecular Weight Marker (Low)" manufactured by TAKARABIO Co., Ltd. as a molecular weight, and confirmed by Sodium Dodecyl Sulfate-polyacrylamide gel electrophoresis (SDS-28201105355 PAGE). As a result of the tolerance, it was confirmed that the molecular weight of the CAD peptide (3) ranged from 40,000 to 67,000 (40 kDa to 67 kDa). The molecular weight of this CAD peptide (3) was confirmed by Sodium Dodecyl Sulfate - SDS-PAGE. The molecular weight band confirmation method by this Sodium Dodecyl Sulfate-polyacrylamide gel electrophoresis (Sds-PAGE method) is described in detail below. (1) Molecular weight marker "Protein Molecular Weight Marker (Low)" manufactured by TAKARABIO Co., Ltd. Detailed reference materials are Phosphorylase B (molecular weight 97200), Serum Albumin (molecular weight 66409), Ovalbumin (molecular weight 44287), Carbonic anhydrase (molecular weight 29000), Trypsin The above six substances of inhibitor (molecular weight: 20,100) and Lysozyme (molecular weight: 14,300). (2) Polyacrylamide gel was prepared to have a concentration of the concentrated gel of 4.5% by mass and a separation gel concentration of 1 〇·〇% by mass. (3) Sample solution CAD peptide or reference substance 1 part by mass of bromophenol blue appropriate amount of sample solvent 1 part by mass (sample solvent: sodium lauryl sulfate 丨 mass%, 2 - thioethanol 1 mass%, Tris hydrochloric acid (pH 6 .8) 10 mM, glycerol 10% by mass) (1) Electrophoresis conditions 40 mA, 30 minutes 29 201105355 (2) Electrophoresis tank buffer

BioRed's 10-fold diluted aqueous solution of TriX/Glycine/SDS Bufferj (3) staining conditions were stained with Coomassie Brilliant Blue solution for 1 hour, and then decolorized with decolorizing solution for about 6 hours (4) The electrophoresis gel photograph of the CAD peptide (3) and the molecular weight marker which are treated under the conditions (1) to (6) above is shown in Fig. 4. According to this electrophoresis gel photograph, the distance X of the molecular weight marker based on the predetermined position is shown. The relationship between (cm) and the logarithm of the molecular weight (Y(ln[kDa]) is graphically shown in Fig. 5. If the calibration line shown in Fig. 5 is calculated from the molecular weight point of the graph, the correction line is calculated. The molecular weight of the CAD peptide (3) (based on the distance from the intended position of the belt) is 50000 (501 <:0&) and 63000 (63) <:0&), €8 peptide (3) The molecular weight is confirmed to be in the range of 40,000 to 67,000 (40 kDa to 67 kDa), more specifically 49000 (49 kDa) to 64,000 (64 kDa). As described below, using the hair treatment agent of Example la or the hair treatment agent of Example ,, Hair treatment 丨 treatment of hair. Also, for untreated hair and treated hair The initial modulus of elasticity and the breaking strength were measured. (Example la) A 3 mass% aqueous solution of the CAD peptide (la) was prepared as a hair treatment agent of Example ia. (Example lb) A 3 mass% aqueous solution of the CAD peptide (3) The hair treatment agent of Example 30 was prepared. (Hair treatment 1) The hair sample 1 was impregnated with hair which was severely damaged as described below, and the hair sample 1 was impregnated in Example la or Example (4) Hair treatment agent. After 1 minute, it was washed with water and dried with warm air. Hair sample 1 of the present treatment 1 was a straight hair black hair treated as shown below. Decolorization treatment, hair treatment, dye treatment, shampoo treatment, dyeing Processing, shampooing, perming, dyeing, shampooing, shampooing, and drying are performed in the order of straight hair black hair. The above-mentioned decoloring treatment is made by MILBON Corporation "PR〇Matiz FLAEVE-ADD |第1 | The first sodium of the "beat" and the second agent are mixed in a ratio of about i part by mass: 2 parts by mass, and are missing from JI 玄甘. Human 丄..., "applied to the hair. The amount of application is hair quality| 2 times. The coated hair is covered with a film, after 15 After a minute, wash the hair; wash it, then dry it with warm air. β Μ On the perm treatment, attach the roll to the perm rod with a diameter of 12 _ ^ 溃 贱 贱 贱 删 删 删 UM UM UM UM UM UM UM UM UM UM UM UM UM UM After washing with water, the second agent of the "REJUMEC/T" is used to dry the hair with warm air. The above dyeing treatment, M 1 ^ will be made by MILB0N "ORDEVE" The first dose and the second dose! Parts by mass: ” Apply to the hair afterwards. "Coating" - the ratio of the right and left is mixed, and then placed for a minute. The cloth is "10 times the hair quality. After the application, the above shampooing treatment is to use hair washing for 1 cycle, 6G t and dry ventilation. Hair shampoo, hair sample i

31 S 201105355 The 5 times quality shampoo ("LUX · SUPERRICHSHINE" manufactured by UNILEVER) was applied to the hair, left for 3 minutes, and then washed with water. In the hair conditioner, hair conditioner ("LUX · SUPERRICHSHINE" manufactured by UNILEVER Co., Ltd.), which is 5 times the mass of the hair sample 1, was applied to the hair, and left for 3 minutes, and then washed with water. (Initial elastic modulus, breaking strength) The initial elastic modulus and breaking strength per unit cross-sectional area were measured using "TENSILON UTM-II-20" manufactured by ORIENTEC. The measurement conditions were that the hair sample 1 was immersed in water for 24 hours before the measurement, and the hair sample 1 was immersed in water at the time of measurement, the temperature was 25 ° C, the stretching speed was 2 mm/min, and the stretching distance of the hair sample 1 was 20mm. Table 1 below shows the results of initial elastic modulus and breaking strength of hair treated with hair treatment 1 and untreated hair. In Table 1, the "measured average value" is the average value of the number of times of measurement 5 times, and the "rate of change" is based on untreated hair. ----- Example la Example lb Molecular weight range of untreated CAD peptide - ________ 1000~3600 40000~67000 - Initial elastic modulus measurement average (GPa) 1.92 1.45 1.20 Rate of change (%) +59.6 +20.5 — breaking strength—measured average (MPa) 104.8 74.0 81.3 rate of change (%) +28.9 -9.0 - Example la, which incorporates the 201105355 peptide (la) having a molecular weight range of 1000 to 3600 as shown in Table 1 above, The initial elastic modulus and the breaking strength change 2 were not positive, and it was confirmed that the CAD peptide (la) can improve the initial elastic modulus and the breaking strength of the severely damaged hair. In the case of blending the molecular weight range side to the (10) peptide (3), the rate of change in the initial modulus of elasticity was confirmed to increase the initial modulus of elasticity of the CAD peptide (3). X, Example 1 a and the initial elasticity of the application of Example 1 b. The evaluation of the high-quality, 纟 果 fruit, the expression of the CAD peptide can improve the initial elastic modulus of the hair growth or inhibit the deterioration. $ (Example 2a) Hair solution = (10) Aqueous solution of (4) peptide (Example 2b) A 5 mass% aqueous solution of a CAD peptide (2b) was prepared as a hair treatment agent. i^ The hair of Example 2a was used. The treatment agent or the agent of the embodiment is treated according to the following hair (4) hair, and the hair and the treated hair, the day, the denier, the wolfberry treatment, the hair, the initial elastic modulus, The breaking strength and the degree of elongation were also calculated as the distance between the micro-original η ^ b 々 fiber·, 隹 (IF. lnte dlate filament). (Hair treatment 2a) After taking the aqueous solution of 20-year-old women for 3 minutes :,, '" Responsible for 3 mass% sulfuric acid laurel # Λ 4. # -V· Μ , 4, ordered to wash, then wipe off the water after drying, as the hair le § pattern 2. 1 part by mass of the hair #* θ hair 1 pattern 2 was subjected to the following reduction treatment, treatment of the % ion treatment agent, and oxidation treatment of the hair preparation sample 2 of the example 2b at 45 t and 1 〇8. In the reduction treatment, 1 part by mass of a condition of 0 is immersed in 30 parts by mass of 3 33 1 201105355 bar/6 巯 acetic acid aqueous solution (the pH is adjusted to 9 3 with monoethanolamine), and then washed with T warm water. Minutes, wipe off the water. The cation treatment was carried out by immersing the hair e-type 2 of the 丨 quality in 3 G parts by mass of vaporized dimethyl bis propylene ammonium • propane acid copolymer ("MERQuat 55 〇" manufactured by nALCOjAPAN Co., Ltd.) S 质 S % aqueous solution After 10 minutes, the surface moisture of the hair sample 2 was wiped off. By the treatment of the hair treatment agent of Example 2a or Example 2b, it is 胄! The hair sample 2 of the mass parts was impregnated into 3 parts by mass of the examples. Or, in the embodiment, the surface moisture of the hair sample 2 was wiped off after 1 minute of treatment. In addition, the oxidative treatment is a method of immersing the hair sample 2 of the 丨# parts in a detonated mass of a 7 mass% aqueous solution of sodium bromate (after a minute of the phosphate buffer solution, the hair (4) 2 is hydrated to make it moist. Dry ^1 () (initial modulus of elasticity, breaking strength 'stretching degree) " Measurement of initial modulus of elasticity and breaking strength, in the same manner as described above, and the degree of elongation was measured while measuring the breaking strength. (IF spacing), using the beam line SP of the SP-type radiant light device SPRING-8, and illuminating the calendering micro-rays with the axis of the 4-type 2, so that the calendering micro-rays are stepped from the outer circumference of the hair sample 2 In the radial direction, in the relative fishing degree of 60% of the ambient emulsion: measure the equatorial reflection intensity near the 9th, and directly determine the spacing of the tidal. The detailed measurement conditions are as follows. X-ray wavelength: 〇.〇83nm (E =15keV) Camera length: approx. 2〇〇〇mm = detector pixel size: 140.8 W pixels χ 14 () pixels ~ image size: 1 3 4 4 pixels X 1 〇 2 4 pixels, 34 201105355 Silver citrate cycle: 5.838nm (1 time) for correcting beam size: approx. 5 // m 1st pinhole: 5 # m 2nd pinhole: 20 0 # m Beam stop: </> 8 mm Detector: Image intensifier The initial elastic modulus of the hair after treatment 2a is shown in Table 2a. In Table 2a, the "measured average" is the number of measurements 10 times. The average value, "rate of change" is based on untreated hair. Further, "untreated" in Table 2a means that the treatment of the cation treatment and the treatment with the hair treatment agent of Example 2a or Example 2b is omitted. In addition, the "IF pitch" is the average value of 800 samples [Table 2a] Example 2a Example 2b Untreated hair sample 2 The molecular weight of the CAD peptide ranges from 1000 to 3600 1000 - an initial elastic modulus measurement average (GPa 0.77 1.00 0.67 1.55 Rate of change (%) +15 +49 ±0 - Average value of breaking strength measurement (MPa) 91.0 108.6 71.8 140.5 Rate of change (%) +26.7 +51.3 ±0 — Average value of tensile measurement (times) 1.70 1.71 1.67 1.59 Rate of change (%) +1.8 +2.4 ±0 - EF pitch (nm) 10.56 9.76 10.00 9.87 Indole acetic acid concentration in reduction treatment: 3 mass% In Table 2a, it can be confirmed that Example 2a and Example 2b Initial elastic modulus S- 35 201105355 and breaking strength Further, the IF pitch of Example 2a was longer than that of the untreated IF pitch, and it was judged that the CAD peptide (2a) was precipitated inside the hair after hair treatment 2a. Using the hair treatment agent of Example 2a or Example 2b, the hair was treated according to the following hair treatment 2b. Further, the initial elastic modulus, the breaking strength, and the elongation were measured for the untreated hair and the treated hair. (Hair Treatment 2b) The hair treatment 2b is the same as the hair treatment 2a except that the reduction treatment of only the hair treatment 2a is changed to the following. In the reduction treatment of the hair treatment 2b, a 3 mass% aqueous solution of indole acetic acid was changed to an aqueous solution containing 9 mass% of indoleacetic acid and 2 mass% of dimercaptoacetic acid (pH was adjusted to 9.3 with monoethanolamine). The initial elastic modulus of the hair after the treatment of the hair treatment 2b and the like are shown in Table 2b. The meanings of "measured average value", "change rate" and "unprocessed" in Table 2b are the same as those in Table 2a. [Table 2b] Example 2a Example 2b Untreated CAD peptide has a molecular weight range of 1000 to 3600 1000 or less - initial elastic modulus measurement average (GPa) 0.07 0.06 0.03 rate of change (%) +133 +100 - average value of breaking strength measurement (MPa) 14.4 10.6 6.6 Rate of change (%) +118.2 +60.6 — Average value of tensile measurement (times) 1.38 1.43 1.42 Rate of change (%) -2.8 +0.7 — Concentration of indole acetic acid in reduction treatment: 9 mass% 36 201105355 The shampoos of Example 3a, Example 3b, and Comparative Example 3 were prepared as described below, and the hair was treated according to the hair treatment 3. (Example 3a) A hair treatment agent of Example 3a was prepared by blending "DEESSE'S SHAMPOO S" manufactured by MILBON Co., Ltd. with a CAD peptide (la) of 2% by mass. (Example 3b) A hair treatment agent of Example 3b was blended in a "DEESSE'S SHAMPOO S" manufactured by MILBON Co., Ltd. with a CAD peptide (3) of 2% by mass. (Comparative Example 3) "DEESSE'S SHAMPOO S" manufactured by MILBON Co., Ltd. was used as the hair treatment agent of Comparative Example 3. (Hair Treatment 3) The hair bundle was subjected to a shampooing treatment by the hair treatment agent of Example 3a, Example 3b or Comparative Example 3. Next, the hair bundle was subjected to hair care treatment by "DEES SE'S TREATMENT SF" manufactured by MILBON Co., Ltd., and then the hair bundle was warmed and dried. The feel of the hair bundle after the hair treatment 3 treatment was evaluated by a special evaluator. As a result of the evaluation, the hair bundles treated with the hair treatment agents of Example 3a and Example 3b were smoother than those of the hair treatment agent treated with Comparative Example 3. Further, the hair bundle treated by the hair treatment agent of Example 3b was thicker than the hair bundle treated with the hair treatment agent of the comparative example. Here, "thickness" means that the surface of the hair is like a touch which is covered with any substance, and the meaning is the same in the following examples. 37 201105355 The hair treatment agents of Example 4a, Example 4b, Example 4c and Comparative Example 4 were prepared as described below, and the hair was treated according to the hair treatment 4. (Example 4 a) A 0.2% by mass aqueous solution of a CAD form (la) was prepared as a hair treatment agent of the example. (Example 4b) A 0.2% by mass aqueous solution of the CAD peptide (lb) was prepared as the hair treatment agent of Example 4b. (Example 4c) A 0.2% by mass aqueous solution of the CAD peptide (3) was prepared as the hair treatment agent of Example 4c. (Comparative Example 4) Water was used as the hair treatment agent of Comparative Example 4. (Hair Treatment 4) I Hair of Example 4c or Comparative Example 4 Example 4a 'Example treatment agent was sprayed onto the tufts'. The hair bundle was warmed and dried by a special evaluator. Hair treatment 4 treated hair was evaluated. The touch of the beam. The evaluation knot* was thicker than the hair bundle treated with the hair treatment agent of Example 4c, compared to the hair bundle treated with the hair treatment agent of (4) 4. Further, the hair bundles treated with the hair treatment agents of Examples 4a and 4b were smoother and softer than the main treatments treated with the hair treatment agent of Example 4c. (Example 5) The hair treatment agent of the following Comparative Example 5 was mixed with Cad peptide (3)" 38 201105355% by mass of shampoo, and the hair treatment agent of Example 5 (Comparative Example 5) was a polycyclic ring. 5% by mass of sodium oxyethyl lauryl ether sulfate, 4% by mass of triethanolamine dodecyl sulfate, 2% by mass of sodium polyoxyethylene ethyl ether, sodium acetate, sodium dimethoxide %, decyl propyl decyl bet = 4% by mass, coconut oil fatty acid diethanol decylamine 3% by mass, coconut oil fatty acid monoethanol decylamine (Μ% by mass, ls3_butylene glycol 〇 2% by mass: Barium chloride [2 search - 3 (trimethylammonium) propyl] hydroxyethyl cellulose 〇 4% by mass, wrong combination of 0.3% by mass, preservative 〇 3% by mass, antioxidant 〇 · 1% by mass And a shampoo prepared by blending 2% by mass of water as a hair treatment agent of Comparative Example 5. (Reference Example 5) The hair treatment agent of Comparative Example 5 was blended with a commercially available keratin 2% by mass of shampoo 'as a reference to the hair's hair treatment. Here, the commercially available keratin is made by using keratin containing 5 mass% of water. Liquid (4) (7)

JaPan^ hurts the company "KeratecIFP - HMW"). (Hair Treatment 5) β Prepare a plurality of hairs that have been entangled and decolorized into a hair bundle. The hair bundle was treated in the order of coating, water washing, hair care (hair treatment agent of Comparative Example 6 below), washing, and warm air drying of the hair treatment agent of Example 5, Comparative Example 5 or Reference Example 5. . The tactile sensation of the hair bundle treated by the special evaluator & hair treatment 5 was based on the use of the hair treatment agent of Comparative Example 5. The evaluation results are shown in Table 3 (the evaluation "one" in the table indicates that no evaluation was performed). 39 201105355 [Table 3] Hair treatment agent Example 5 Thickness and strongness Evaluation item Smoothness Strong ~ Softness Strong ~

(Example 6) The hair treatment agent of the following Comparative Example 6 was blended with a hair conditioner of CAD peptide (3) 〇 2% by mass as a hair treatment agent of Example 6. (Comparative Example 6) 2% by mass of desertified hexadecyltrimethyl I, 3 mass% of trimethylammonium gasification, 0_8 mass% of ethanol, 0.7 mass% of isopropanol, and 5 mass% of whale sterol 2% by mass of stearyl alcohol, % by weight of concentrated glycerin, 0.5% by mass of polyepoxy stearyl ether, and cetyl 2-ethylhexanoate! % by mass, 0.8% by mass of dipentaerythritol fatty acid ester, 3% by mass%, 3% by mass of high-polymerized fluorenyl polyoxyalkylene, dimethyl methoxy oxane, methyl stearyl oxime Oxygen: Polymer 〇 质量 2% by mass, preservative 0.2% by mass, and 〇 质量 3% by mass of the hair conditioner prepared by the use of water as the hair treatment of Comparative Example 6 (Reference Example 6) In the hair treatment agent of Comparative Example 6, a conditioner obtained by blending a commercially available keratin 2 and a % by weight was used as a hair treatment agent of Reference 6. Here, the commercially available keratin protein is an aqueous solution containing keratin 5 mass% (cr_

"Keratec IFP — HMW" made by Japan Stock Company. (Hair Treatment 6) 40 201105355 Preparation of a plurality of wound hairs of 3 g of decolorized hair. Seven targets of one hair bundle were used as evaluation hair bundles. Coating, washing with water, washing of Example 2, Comparative Example 6 or Reference Example 6 of shampoo (Comparative Example 5, Fengfeng® Laoqifa Treatment Agent), washing with water, warm air The order of drying is performed on the tufts. In the hair treatment table 4 (the evaluation of the hair treatment agent in the table, the tactile sensation of the hair bundle treated by the special evaluation 6 is evaluated by the comparison example). The evaluation result is shown in -" Not evaluated). [Table 4]

(Example 7) A non-rinsing cream conditioner containing CAD peptide (3) 〇 2% by mass was added to the hair treatment agent of Comparative Example 7 below, as the hair treatment agent of Example 7. Here, the CAD peptide (3) was blended using a 4% by mass aqueous solution of CAD peptide (3) adjusted to pH 8.72 with arginine. (Comparative Example 7) chlorinated stearyl trimethylammonium 〇·8 mass%, isopropyl alcohol oxime 2% by mass, cetyl alcohol 3% by mass, behenyl alcohol 〇8 mass%, and propylene glycol oxime 2 mass %, dipropylene glycol 2% by mass, soft lanolin fatty acid cholesterol $%, tallow resin 2% by mass, hydroxyethyl cellulose 〇〇 6% by mass, tamarind capsule 〇. 2% by mass, polydimethyl 1% by mass of a methoxyalkanol, 16% by mass of a cyclopentasiloxane, a cyclopentasiloxane of 16% by mass, a ruthenium-based polyoxylate of 2% by mass, and a crosslinked methylpolyoxane of 0.2% by mass. Amine modified polychlorinated oxygen 2% by mass 'highly polymerized dimercapto polyoxyalkylene. methyl (aminopropyl) decane copolymer 0.1% by mass, cocoamidopropyl dimethyl ammonium hydroxypropyl Acetyl oxy-oxo-methyl polyoxane copolymer acetate 0.5% by mass, acrylamide. 2~ (acrylic-hydroxy) ethyl chloromethyl ammonium copolymer 〇〇 3% by mass, anti- Non-rinsing creamy conditioner prepared by blending oxidizing agent 0.05% by mass, preservative 〇.2% by mass, and 〇2% by mass in water, as a hair treatment of Comparative Example 7. Agent. (Reference Example 7) The hair treatment agent of Comparative Example 7 was blended with a commercially available keratin 〇 2% by mass of a non-rinsing cream conditioner as a reference hair treatment agent. The keratin is applied to a hair containing a horned egg from a 5 mass solution (KemeciFp-〇7 (hair treatment 7) manufactured by Croda Japan Co., Ltd.). The sense of being = is the first... the worst is the third place). In addition, it is applied to the same evaluation as the real bamboo. Send it to '5'. From the results of Table 5, the frost of Comparative Example 7 of keratin was large in thickness. It can be seen that compared with the cream, the evaluation results of the thick feeling are shown in the table with the blended CAD peptide (3) and the blended CAD peptide (3). Example 7 42 201105355 [Table 5] Hair treatment agent Thickness Example 7 Comparative Example 7 Reference Example 7 1 3 ----- 2 (Example 8) CAD peptide (3) 2% by mass, hexadecyltrimethylammonium bromide 2% by mass, ethanol 1 mass %, cetyl alcohol 3% by mass, and stearyl alcohol 2% by mass were blended with water cream conditioner, and used as the hair treatment agent of Example 8. (Reference Example 8) 2% by mass of hexadecyltrimethylammonium bromide, 0.05% by mass of vaporized octadecyltrimethylammonium, 8 parts by mass of vaporized dicocoyldidecylammonium hydride, polyoxyethylene B Rarely recorded (2〇E.〇.)〇·01胄%, ethanol 1% by mass, recorded hexanol 6 mass%, high polymerized dimethyloxane 2% by mass, amine ethylamine propyl oxime Dimercaptomethoxypropane copolymer i% by mass, ethyl sulphate fatty acid amine propyl ethyl dimethyl group (7)!% by mass, amino acid G 2% by mass, preservative 0.3% by weight, and fragrant _ 〇 3% of the amount is changed to the creamy conditioner of water' as the hair treatment agent of Reference Example 8. (Hair treatment 8a) The hair treatment agent of Example 8 or Reference Example 8 was applied to a hair bundle, and then washed with water to dry with warm air. (Hair Treatment 8b) The hair treatment agent of Example 8 was applied to a tuft which was further coated with the hair treatment agent of Reference Example 8. After that, the tufts are washed with water and dried with warm air. The tactile sensation of the hair bundle treated by the hair treatment 8a and the hair treatment 8b treated 43 201105355 was evaluated by a dedicated evaluator. The results of this evaluation are shown in Table 6. [Table 6] Hair Treatment Method Hair Treatment 8a Hair Treatment 8a Hair Treatment 8b Hair Treatment Agent Example 8 Reference Example 8 Example 8 and Reference Example 8 A strong feeling of strength is hardly strong (Example 9) "LISEINTER made by MILBON" A hair dye containing 10 parts by mass of a CAD peptide (3) and a mass fraction of 10 parts by mass of "LISEINTER second agent (OXIDAN 3.0)" manufactured by MILBON Co., Ltd. is added to the first agent. As the hair treatment agent of Example 9. (Hair Treatment 9) The hair bundle was treated with the hair treatment agent of Example 9. The feel of the hair bundle treated hair treatment 9 was evaluated by a special evaluator. As a result of the evaluation, the hair bundle treated with the hair treatment agent of Example 9 was used, and the feeling of the fingers was good at the time of shampooing. (Example 10) The hair treatment agent of Example 10 was added to the "PREJUME C/T first agent" manufactured by MILBON Co., Ltd., in which 0.5% by mass of the CAD peptide (3) (the first agent of the two-part type perm agent) was added. (Comparative Example 10) A monomer having no CAD peptide (3) added in Example 10, that is, a "PREJUME C/T first agent" manufactured by MILBON Co., Ltd. was used as a hair treatment agent of a comparative example. 44 201105355 (Hair treatment ίο) The hair treatment agent of Example 10 or Comparative Example 1 was applied to a hair bundle, and after standing for 15 minutes, it was washed with water and wiped off with a towel. Then, "PREJUME C/T second agent" manufactured by MILBON Co., Ltd. was applied, and after standing for 5 minutes, it was washed with water, and further coated with rDEESSE manufactured by MILB0N, SNElJ Willows TREATMENT", and after washing with water, the bundle was dried by warm air. The feel of the hair bundle treated by the hair treatment was evaluated by a special evaluator. As a result of the evaluation, the hair bundle treated with the hair treatment agent of Example 10 was thicker than the hair bundle treated with the hair treatment agent of Comparative Example 1 . Industrial Applicability As described above, the hair treatment agent of the present invention is suitable for hair treatment for business use or household use because it can effectively improve the initial elastic modulus and breaking strength of the damaged hair or suppress the evil. BRIEF DESCRIPTION OF THE DRAWINGS Fig. 1 is a fluorescent microscope observation photograph of hair having a peptide permeated inside. Figure 2 is within the system. Fluorescence Microscopy Observation of Hair Without Penetrating Peptide Figure 3 is a MAL peptide blended with the hair treatment agent of the Example (a MALDI-TOFMS analysis chart of 1昀. Fig. 4 is a hair treatment agent of the embodiment) The electrophoresis photograph of the (10) peptide (7) by Sodium Dodecyl Sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Figure 5 shows the blending of the t CAD peptide of the hair treatment agent of the example (3) Sodium Dodecyl Sulfate - A diagram of the calibration curve for molecular weight markers in polyacrylamide gel electrophoresis (SDS — 45 201105355 PAGE) [Key component symbol description]

Claims (2)

201105355 VII. Patent application scope: A hair treatment agent characterized in that: (I) is blended with a peptide having a side chain group, and the side chain group has a unit represented by the formula, S-S-(CH2) nCO〇- (I) (in the formula (1), η is 1 or 2) 2_ The hair treatment agent base according to the scope of the patent application is selected from the group consisting of a slow methyl disulfide group and a slow methyl disulfide salt: : one or more of the side bond group and the salt of a carboxyethyl disulfide group. Ethyl disulfide, wherein the peptide, wherein the peptide has a molecular treatment stem having a molecular stem range of less than 40,000. 2. For example, the hair treatment agent in the second paragraph of the patent application scope has a molecular range of 20,000 or less. 5. If the scope of patent application is item 2 ^ ^ < Hair treatment agent has hair permeability. 6. If the scope of the patent application is 2, and the treatment is carried out by seven treatments, the amount of kansui is 4 〇〇〇〇 or more and 67 〇, and the V of the peptide is from the bottom. 7. For the scope of patent application, item VIII VIII θ # hair treatment agent, the range of the knives is 49000 and 64 〇〇〇, of which the peptide is from the bottom. 8. In the scope of patent application No. 1 to 7, it is a hair treatment agent for hair conditioners, perm agents, and dyes. 9 -Ms ^ ^ Decolorizer or styling agent. A raw material for a hair treatment agent, ^ g , characterized by: a peptide 201105355 -S-S- (CH2 having a side chain group (having a unit represented by the following formula (1) dissolved in a solvent) nC00- (I) (in the formula (I), n is 1 or 2). 10. The raw material for a hair treatment agent according to claim 9, wherein the peptide has a molecular weight range of less than 40,000. 1 L is a raw material for a hair treatment agent according to claim 9 in which the molecular weight of the peptide is in the range of 20,000 or less. 12. The raw material for a hair treatment agent according to claim 9, wherein the peptide has hair permeability. The raw material for a hair treatment agent according to claim 9, wherein the peptide has a molecular weight in the range of 40,000 or more and 67,000 or less. Eight, the pattern: (such as the next page) 48