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WO2010143484A1 - Agent de traitement capillaire et matière première pour agent de traitement capillaire - Google Patents

Agent de traitement capillaire et matière première pour agent de traitement capillaire Download PDF

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Publication number
WO2010143484A1
WO2010143484A1 PCT/JP2010/057724 JP2010057724W WO2010143484A1 WO 2010143484 A1 WO2010143484 A1 WO 2010143484A1 JP 2010057724 W JP2010057724 W JP 2010057724W WO 2010143484 A1 WO2010143484 A1 WO 2010143484A1
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WIPO (PCT)
Prior art keywords
hair
hair treatment
treatment agent
mass
peptide
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PCT/JP2010/057724
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English (en)
Japanese (ja)
Inventor
正人 吉田
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Milbon Co Ltd
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Milbon Co Ltd
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Publication date
Priority claimed from JP2009141704A external-priority patent/JP5558034B2/ja
Priority claimed from JP2010005356A external-priority patent/JP5611603B2/ja
Priority claimed from JP2010005357A external-priority patent/JP2011144127A/ja
Application filed by Milbon Co Ltd filed Critical Milbon Co Ltd
Priority to CN201080024869XA priority Critical patent/CN102458352A/zh
Priority to KR1020117029136A priority patent/KR101951923B1/ko
Publication of WO2010143484A1 publication Critical patent/WO2010143484A1/fr
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

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    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
    • A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q5/00—Preparations for care of the hair

Definitions

  • the present invention relates to a hair treatment agent used in hair care treatment, perm treatment, coloring treatment, bleach treatment and the like of hair, and a raw material for hair treatment agent used in the production of this hair treatment agent.
  • ⁇ Physical treatments such as brushing, hand dryers, hot iron, etc., and chemical treatments such as coloring and permanent treatment damage hair. Damaged hair has worse hair properties, such as hair feel (for example, beam, strain, softness), appearance (for example, gloss, cohesion), strength (for example, tensile strength) compared to before being damaged. Will be.
  • hair feel for example, beam, strain, softness
  • appearance for example, gloss, cohesion
  • strength for example, tensile strength
  • JP-A-7-126296 discloses a kind of modified peptide, in which the modified peptide has a disulfide group (—S—S—) as a carboxymethyl disulfide group (—S—S—CH 2). Water-soluble one obtained by conversion to (COOH).
  • Japanese Patent Application Laid-Open No. 7-126296 discloses forming a film from the modified peptide as a specific embodiment of the modified peptide, but does not intend a hair treatment agent.
  • an object of the present invention is to provide a hair treatment agent and a raw material thereof that can improve the initial elastic modulus of damaged hair or suppress the deterioration of the initial elastic modulus of hair.
  • the present inventor improves the initial elastic modulus of the hair by treating the hair with water containing a peptide having a predetermined side chain group. Obtained knowledge. Based on this finding, the present invention has been completed.
  • the hair treatment agent according to the present invention is characterized by blending a peptide having a group having a unit represented by the following formula (I) as a side chain group.
  • —SS— (CH 2 ) n COO— (I) (In the formula (I), n is 1 or 2.)
  • the “peptide” in the present invention is a peptide in which two or more amino acids are bonded by peptide bonds, and proteins such as keratin protein and collagen protein also correspond to peptides.
  • the side chain group in the peptide may be one or more selected from carboxymethyl disulfide group, carboxymethyl disulfide group salt, carboxyethyl disulfide group and carboxyethyl disulfide group salt.
  • the molecular weight range of the peptide is preferably less than 40000, more preferably 20000 or less. If the peptide in the present invention has a molecular weight range of less than 40000, it is advantageous not only for improving or suppressing the initial elastic modulus of hair, but also for improving or suppressing the breaking strength of hair.
  • the peptide preferably has hair permeability. If it is a peptide which has this hair permeability, the improvement or the deterioration inhibitory effect of the initial elastic modulus and breaking strength of hair will become more favorable.
  • the molecular weight range of the high molecular weight is, for example, 40,000 to 67,000, and may be 49000 to 64,000. Even if a peptide having such a molecular weight range is blended, the above-described improvement in the initial elastic modulus of hair or suppression of deterioration can be effectively achieved.
  • the hair treatment agent according to the present invention is used as a hair care agent, a permanent agent, a coloring agent, a bleaching agent or a styling agent.
  • the hair treatment agent according to the present invention is produced, for example, using a raw material for a hair treatment agent obtained by dissolving a peptide having a group having a unit represented by the following formula (I) as a side chain group in a solvent such as water.
  • a raw material for a hair treatment agent obtained by dissolving a peptide having a group having a unit represented by the following formula (I) as a side chain group in a solvent such as water.
  • the —SS— (CH 2 ) n COO— (I) In the formula (I), n is 1 or 2.
  • the initial elastic modulus of hair can be improved or the deterioration can be suppressed.
  • the hair treatment agent according to this embodiment is obtained by blending a peptide having a predetermined side chain group (hereinafter, “peptide having a predetermined side chain group” is referred to as “CAD peptide”).
  • the CAD peptide has 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 CAD 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. This keratin is known to have a high cysteine ratio among peptides derived from natural products, and is a raw material from which the CAD peptide can be obtained efficiently. From this point of view, the same main chain of CAD peptide as that of keratin is preferable.
  • the side chain group of the CAD peptide is a group having a unit represented by the following formula (I), and in this side chain group, the disulfide group is arranged on the main chain side of the CAD peptide. It is preferable that a plurality of side chain groups exist in the CAD peptide.
  • the group represented by the following formula (I) is dissociated (ionized) into a carboxylate anion, it is called a carboxylatoalkyl disulfide group.
  • —SS— (CH 2 ) n COO— (I) In the formula (I), n is 1 or 2.
  • Suitable as the chemical structural unit of the side chain group is a carboxymethyl disulfide group represented by the following formula (IA), a salt of a carboxymethyl disulfide group represented by the following formula (IB) or (IC), It is 1 type, or 2 or more types selected from the salt of the carboxyethyl disulfide group represented by Formula (IIA), and the carboxyethyl disulfide group represented by the following formula (IIB) or (IIC).
  • a preferable group as the side chain group is one or more selected from the following formulas (Ia), (Ib), (Ic), (IIa), (IIb), and (IIc) (in the following formula R 1 , M 1 , R 2 and M 2 are the same as above.)
  • a hair treatment agent containing a CAD peptide having two or more side chain groups it is considered that the mercapto groups constituting the hair are cross-linked via the CAD peptide.
  • the mercapto groups constituting the hair are cross-linked via the CAD peptide.
  • only one side chain group in the CAD peptide reacts with the mercapto group of the hair, or only one side chain group reacts with the mercapto group of the hair and another CAD peptide.
  • a polymerization reaction with a peptide or a polymerization reaction between CAD peptides in hair is also conceivable.
  • the cross-linking mechanism between mercapto groups in hair via CAD peptides is represented as follows by taking, as an example, a CAD peptide having two —CH 2 —SS—CH 2 COOH as side chain groups.
  • a cross-linking mechanism through a CAD peptide between a pair of mercapto groups in hair is represented by using a CAD peptide having two —CH 2 —SS—CH 2 CH 2 COOH as side chain groups as an example, It is as follows.
  • the molecular weight of the CAD peptide in this embodiment is not particularly limited. If the CAD peptide is roughly classified based on the molecular weight range, it can be divided into a CAD peptide having a molecular weight range of less than 40000 and a CAD peptide having a molecular weight range of 40,000 to 67,000.
  • the initial elastic modulus and breaking strength of damaged hair can be improved or suppressed. Since the smaller the molecular weight of the CAD peptide, the more advantageous is the improvement of the initial elastic modulus and breaking strength of the hair, or the suppression of deterioration. Therefore, the molecular weight range of the CAD peptide in this embodiment is preferably 20000 or less, more preferably 10,000 or less, and 5000 or less. Further preferred. Although the lower limit of the molecular weight range of CAD peptide is not specifically limited, For example, it is 500.
  • the molecular weight range of the CAD peptide is less than 40,000. This is because the m / z peak by time-of-flight mass spectrometry (TOFMS) employing matrix-assisted laser desorption / ionization (MALDI method) is regarded as the molecular weight of the CAD peptide. It can be confirmed from the range.
  • TOFMS time-of-flight mass spectrometry
  • MALDI method matrix-assisted laser desorption / ionization
  • the peak having the highest intensity in the TOFMS result is preferably confirmed at m / z 20000 or less, more preferably confirmed at m / z 10,000 or less, and m / z 5000 or less. What is confirmed is particularly preferred.
  • the lower limit value of the highest intensity peak is not particularly limited, but is, for example, m / z 500.
  • the CAD peptide in the present embodiment has the hair penetrability because the above-mentioned crosslinking and the like inside the hair are performed. Those are preferred.
  • the CAD peptide has hair permeability according to the following procedures (1) to (4).
  • the FTSC-MES is prepared as follows. A MES aqueous solution having a pH of 5.5 was added dropwise to a solution obtained by dissolving 1.065 parts by mass of 2- (N-Morpholino) ethanesulfide Acid (MES) in 40 parts by mass of water by adding 0.2 M NaOH aqueous solution dropwise.
  • MES 2- (N-Morpholino) ethanesulfide Acid
  • FTSC-MES Fluorescein-5-thiosemicabazide
  • FIG. 1 is a fluorescence microscopic observation photograph according to the procedures (1) to (4) above, and the fluorescence inside the hair, that is, the hair permeability of the CAD peptide can be confirmed.
  • FIG. 2 shows fluorescence microscopic photographs obtained by performing the above steps (1) to (4) without adding a CAD peptide. Since the fluorescence, that is, no CAD peptide is added to the hair surface layer, the hair penetrates. Can be confirmed. This is because the fluorescence inside the fluorescence micrograph shown in FIG. 2 could not confirm the fluorescence inside the hair because even if only the fluorescent substance penetrates the inside of the virgin hair, there is no chemical damage inside the virgin hair. In addition, the fluorescent substance flows out of the virgin hair in the subsequent water washing.
  • the initial elastic modulus of damaged hair can be improved or suppressed.
  • the molecular weight range of the CAD peptide may be 49000 or more and 64000 or less.
  • the molecular weight range of the CAD peptide is 40000 or more and 67,000 or less, which means that the molecular weight calculated from the relative distance between the band of the CAD peptide and the band of the molecular weight marker by Sodium Dodecyl Sulfate-polyacrylamide gel electrophoresis (SDS-PAGE method).
  • SDS-PAGE method Sodium Dodecyl Sulfate-polyacrylamide gel electrophoresis
  • the lower limit of the CAD peptide content in the hair treatment agent according to this embodiment is not particularly limited, but is preferably 0.01% by mass, preferably 0.05% by mass, and more preferably 0.10% by mass.
  • the upper limit of the blending amount of the CAD peptide is not particularly limited, but is preferably 15% by weight, preferably 10% by weight, more preferably 5% by weight, and further 3% by weight from the viewpoint of suppressing an increase in cost due to blending in a large amount. preferable.
  • a CAD peptide having a molecular weight range of less than 40000 is blended with the hair treatment agent, a CAD peptide other than a CAD peptide having a molecular weight range of less than 40000, for example, a CAD peptide having a molecular weight range of 40000 to 67000 may be further blended.
  • a CAD peptide having a molecular weight range of 40,000 or more and 67,000 or less is blended, a CAD peptide having a molecular weight range other than 40,000 or more and 67,000 or less, for example, a CAD peptide having a molecular weight range of less than 40,000 may be further blended.
  • Method for producing CAD peptide having a molecular weight range of less than 40000 examples include production methods (A), (B), and (C) described below.
  • the production method (A) includes a reduction step of converting a protein disulfide group into a mercapto group; a mercapto group generated in a protein molecule in the reduction step, a mercapto group of a mercaptoalkylcarboxylic acid, and / or a mercaptoalkylcarboxylate mercapto
  • the disulfide group (—S—S—) contained in the protein is reduced to two mercapto groups (—SH HS—) by mixing the production raw material containing the protein, water, and a reducing agent.
  • Production raw materials include wool (merino wool, lincoln wool, etc.), human hair, animal hair, feathers, nails and the like containing keratin as a constituent protein. Among them, it is preferable to use wool as a raw material in order to obtain it inexpensively and stably. About a manufacturing raw material, it is good to process beforehand combining sterilization, degreasing, washing
  • the amount of water is not particularly limited.
  • the amount of water is preferably 20 parts by mass or more and 200 parts by mass or less with respect to 1 part by mass of the production raw material. By setting the amount of water in the above range, the reduction reaction is favorably performed.
  • a mercapto group is generated by reducing a disulfide bond in the protein with one or more reducing agents in an alkaline solution.
  • Such a compound (alkaline compound) for making the reaction system in the reduction of the disulfide bond alkaline is made alkaline by adding it to water.
  • the alkaline compound include lithium hydroxide, sodium hydroxide, potassium hydroxide, barium hydroxide, sodium carbonate, potassium carbonate, ammonia and the like, and other basic compounds such as monoethanolamine, diethanolamine, arginine, and lysine. Amino acids, sodium bicarbonate, ammonium bicarbonate and the like are also included. Of these, sodium hydroxide and potassium hydroxide are preferred, and sodium hydroxide is particularly preferred from the viewpoint of reducing protein efficiently at low cost.
  • One or two or more alkaline compounds are used.
  • the mixing amount of the alkaline compound is not particularly limited, but it may be blended so that the pH of the reduction reaction system is adjusted to the following range.
  • As the lower limit of the pH 9 is preferable and 10 is particularly preferable.
  • As an upper limit of pH 13 is good, 12 is preferable, and 11 is particularly preferable.
  • Protein can be reduced efficiently by adjusting the pH to be equal to or higher than the above lower limit.
  • the main chain cleavage of the protein molecule can be suppressed by adjusting the pH to be not more than the above upper limit.
  • mercaptoalkylcarboxylic acid and / or a salt thereof is used as the reducing agent.
  • any other compound may be used as the reducing agent.
  • examples of such an optional reducing agent include thiolactic acid and / or a salt thereof, dithiothreitol, 2-mercaptoethanol, glutathione, thiourea and the like. These optional reducing agents can be used alone or in combination of two or more.
  • the mercaptoalkylcarboxylic acid and / or salt thereof also serves as a modifying agent that forms the unit represented by the above formula (I) in the modification step.
  • a modifying agent that forms the unit represented by the above formula (I) in the modification step.
  • the mercaptoalkylcarboxylic acid and / or salt thereof one or more selected from thioglycolic acid, thioglycolate, 3-mercaptopropionic acid, and 3-mercaptopropionic acid are used.
  • the thioglycolate include sodium thioglycolate, potassium thioglycolate, lithium thioglycolate, and ammonium thioglycolate.
  • sodium thioglycolate and potassium thioglycolate are preferable, and sodium thioglycolate is more preferable from the viewpoint that the carboxylatomethyl disulfide group can be efficiently formed.
  • 3-mercaptopropionate include sodium 3-mercaptopropionate, potassium 3-mercaptopropionate, lithium 3-mercaptopropionate, and ammonium 3-mercaptopropionate. Of these, sodium 3-mercaptopropionate and potassium 3-mercaptopropionate are preferred, and sodium 3-mercaptopropionate is more preferred from the viewpoint of efficiently forming a carboxylatoethyl disulfide group.
  • the amount of the mercaptoalkylcarboxylic acid and its salt used is preferably 0.0050 mol or more and 0.02 mol or less, particularly preferably 0.0075 mol or more and 0.01 mol or less, based on 1 g of the production raw material. Further, the amount used is preferably 0.10 mol / L or more and 0.40 mol / L or less, particularly 0.15 mol / L or more and 0.25 mol / L or less, based on the total capacity of the production raw material, water and the reducing agent. preferable. By making the usage-amount of this mercaptoalkylcarboxylic acid and its salt into the said range, progress of a protein reduction reaction will become favorable.
  • the upper temperature limit is preferably 60 ° C.
  • the reduction time for converting the disulfide group of the protein into a mercapto group becomes long, and there is a possibility that sufficient reduction cannot be performed.
  • the temperature upper limit is exceeded, the main chain of the protein molecule may be cleaved.
  • the set time of the reduction reaction system is set longer as the temperature is lower, and is set shorter as the temperature is higher. The set time is, for example, 20 minutes to 120 minutes.
  • the unit represented by the above formula (I) is introduced into the protein by mixing an acid and an oxidizing agent with the liquid obtained in the reducing step.
  • the acid may be mixed before the oxidant is mixed, after the oxidant is mixed, or at the same time as the oxidant is mixed.
  • Acid is used for lowering the pH of the reaction system in the denaturation step and sufficiently introducing the unit represented by the above formula (I) into the protein.
  • One or two or more of these acids are used.
  • the acid examples include organic acids such as citric acid, lactic acid, succinic acid, and acetic acid; and inorganic acids such as hydrochloric acid. If acetic acid is used, the specific odor from CAD peptide may be a problem, but if citric acid or the like is used, the specific odor can be suppressed.
  • the amount of acid mixed is not particularly limited, but it may be blended so that the pH of the reaction system in the denaturation step is adjusted to the following range.
  • the final pH is preferably from 5 to 9, and particularly preferably from 6 to 8.
  • introduction of the unit represented by the above formula (I) into the protein can be promoted, and at the same time, disulfide group generation by the mercapto groups of the protein can occur. Can be suppressed.
  • the temperature in the reaction system when mixing the acid is preferably 10 ° C. or more and 60 ° C. or less, and particularly preferably 20 ° C. or more and 40 ° C. or less. By controlling within this temperature range, the production of by-products such as cystine monooxide can be suppressed.
  • the standing time after the mixing of the acid is completed is, for example, 1 hour to 48 hours. With this standing time, the introduction of the unit represented by the above formula (I) is sufficient.
  • the oxidizing agent is used to promote the introduction of the unit represented by the above formula (I) into the protein.
  • One or more oxidizing agents may be used.
  • oxidizing agent examples include sodium bromate, potassium bromate, sodium perborate, hydrogen peroxide, and the like.
  • the amount of the oxidizing agent used is not particularly limited, but is preferably 0.001 mol or more and 0.02 mol or less based on 1 g of the manufacturing raw material, and 0.02 mol / L based on the volume of the liquid in which the oxidizing agent is mixed.
  • the amount is preferably 1 mol / L or less.
  • the amount of the oxidizing agent used is larger than the above upper limit, by-products such as cystine monooxide, cystine dioxide and cysteic acid may be produced.
  • the amount of the oxidizing agent used is less than the above lower limit, the introduction of the unit represented by the formula (I) may be insufficient.
  • an oxidizing agent aqueous solution of about 1 mol / L to 5 mol / L is gradually mixed over, for example, 30 minutes to 6 hours. Good.
  • the temperature at the time of mixing an oxidizing agent is not specifically limited, For example, it sets below the temperature in a reduction process.
  • the unit represented by the above formula (I) is introduced into the protein.
  • the mechanism by which a carboxymethyl disulfide group, which is a type of unit represented by the above formula (I), is introduced into a protein molecule is as follows. It is as follows.
  • the protein into which the unit represented by the above formula (I) is introduced by the treatment in the denaturation step includes a protein that is soluble in water and a protein that is insoluble in water. About the liquid containing these proteins, it is good to perform desalting etc. by ion exchange, electrodialysis, etc. as needed.
  • the protein dissolved in water and the protein insoluble in water into which the unit represented by the above formula (I) obtained by the treatment in the denaturation step is introduced are hydrolyzed.
  • hydrolysis there are known hydrolysis methods such as (a1) enzyme hydrolysis, (a2) acid hydrolysis, and (a3) alkali hydrolysis.
  • the hydrolysis method with alkali (a3) the ⁇ elimination reaction of the unit represented by the above formula (I) introduced into the protein may proceed, so among the hydrolysis methods (a1) to (a3), Hydrolysis with an enzyme or acid is preferred, and an enzymatic method is more preferred.
  • (A1) Hydrolysis by enzyme examples include acidic proteolytic enzymes such as pepsin, protease A, and protease B; neutral proteolytic enzymes such as papain, promelain, thermolysin, pronase, trypsin, and chymotrypsin. .
  • acidic proteolytic enzymes such as pepsin, protease A, and protease B
  • neutral proteolytic enzymes such as papain, promelain, thermolysin, pronase, trypsin, and chymotrypsin.
  • Examples of commercially available proteolytic enzymes include “Proteerizer A” manufactured by Daiwa Chemical Industry Co., Ltd.
  • the pH at the time of hydrolysis may be adjusted to 1 or more and 3 or less in the case of acidic proteolytic enzymes, and may be adjusted to 5 or more and 9 or less in the case of neutral proteolytic enzymes.
  • the reaction temperature at the time of hydrolysis is preferably
  • reaction time is preferably 10 minutes or more and 24 hours or less (the longer the reaction time, the lower the CAD peptide can be produced).
  • (A2) Hydrolysis with acid examples include inorganic acids such as hydrochloric acid, sulfuric acid, phosphoric acid, nitric acid, and hydrobromic acid; and organic acids such as formic acid and oxalic acid.
  • the hydrolysis conditions are, for example, pH 4 or lower, reaction temperature 40 ° C. or higher and 100 ° C. or lower, and reaction time 2 hours or longer and within 24 hours (the longer the reaction time, the lower the CAD peptide can be produced). .
  • alkali examples include sodium hydroxide, potassium hydroxide, lithium hydroxide, barium hydroxide, sodium carbonate, potassium carbonate, lithium carbonate, sodium silicate, sodium borate and the like.
  • the hydrolysis conditions are, for example, alkali 1% by mass or more and 20% by mass or less, reaction temperature 15 ° C. or more and 100 ° C. or less, reaction time 30 minutes or more and 24 hours or less with respect to the total mass of the reaction system (reaction time). The longer CAD is, the smaller the CAD peptide can be produced.
  • a solution in which CAD peptide having a molecular weight range of less than 40000 is dissolved is obtained.
  • the solid content may be separated by a known solid-liquid separation means such as filtration, centrifugal separation, squeezing separation, sedimentation separation, and flotation separation.
  • a CAD peptide having a molecular weight range of less than 40000 (1) freeze drying of the CAD peptide solution, (2) spray drying of the CAD peptide solution, and (3) the pH of the CAD peptide solution.
  • a method such as the formation of a CAD peptide precipitate by adding an acid so that the concentration is from 2.5 to 4.0 (the smaller the molecular weight of the CAD peptide, the more the CAD peptide It is difficult to produce a precipitate.)
  • the production method (B) is a method in which the water-insoluble protein obtained in the same reduction step and denaturation step as in the production method (A) is separated and treated in the hydrolysis step.
  • the protein insoluble in water can be recovered by a known solid-liquid separation means, and the hydrolysis step in the production method (B) is the same as the hydrolysis step in the production method (A).
  • the means of the production method (A) may be employed as a means for obtaining a solid CAD peptide.
  • the hydrolysis step in the production method (B) is mainly performed with the water-soluble protein derived from microfibrils as the hydrolysis target.
  • the insoluble protein derived from the matrix is the main hydrolysis target. That is, the production method (B) is suitable for producing a CAD peptide having a high sulfur content.
  • the production method (C) is a method in which the protein dissolved in water obtained in the same reduction step and denaturation step as in the production method (A) is separated and treated in the hydrolysis step. Proteins dissolved in water can be recovered by known solid-liquid separation means, and the hydrolysis step in the production method (C) is the same as the hydrolysis step in the production method (A). Moreover, as a means for obtaining a solid CAD peptide, the means of the production method (A) may be employed.
  • Method for producing CAD peptide having a molecular weight range of 40,000 to 67,000 examples include a method in which the hydrolysis step of the production method (C) is omitted.
  • the hair treatment agent according to this embodiment is not particularly limited, and is a hair care agent, a permanent agent, a coloring agent, a bleaching agent, a styling agent, or the like.
  • Hair care agent is a hair treatment agent used for the care and care of hair.
  • Hair care agents include, for example, shampoos, rinses, conditioners, treatments (for example, non-washing treatments, flushing treatments, combined hair treatments, a component of multi-drug treatments, treatments for pre-treatment of perms, post-treatments of perms.
  • a “perm agent” is a hair treatment agent that is used to change the hair shape using a chemical reaction such as a reduction reaction or an oxidation reaction.
  • the permanent agent examples include a wave agent for forming the hair into a wave shape, and a straight agent for bringing the wave-like hair close to straight hair, and a reducing agent for a one-component permanent agent and a two-component permanent agent.
  • Both of the first agent formulated with and the second agent formulated with the oxidizing agent of the two-part permanent agent correspond to the hair treatment agent according to this embodiment.
  • the “coloring agent” is a hair treatment agent used for coloring hair. Examples of coloring agents include hair dyes containing direct dyes, hair dyes containing reactive dyes that require a reaction when hair is dyed, and hair colorants that temporarily color hair. Can be mentioned.
  • the “bleaching agent” is a hair treatment agent used for decolorizing hair pigments.
  • a “styling agent” is a hair treatment agent used to temporarily hold a hairstyle.
  • the dosage form at the time of using the hair treatment agent is not particularly limited, and examples thereof include liquid, emulsion, lotion, cream, wax, gel, solid, foam (foam), and mist.
  • CAD peptide is mix
  • blended it corresponds to the hair treatment agent of this embodiment.
  • the hair treatment agent in which CAD peptide is blended as an additional blending raw material for known hair treatment agents, and the hair treatment agent in which CAD peptide is blended as an alternative raw material for blending known hair treatment agents are the hair treatment of this embodiment. It corresponds to the agent.
  • a known raw material appropriately selected according to the use of the hair treatment agent can be employed as a raw material other than the peptide blended in the hair treatment agent.
  • the known hair treatment raw materials include anionic surfactants, cationic surfactants, amphoteric surfactants, nonionic surfactants, alcohols, polyhydric alcohols, sugars, fats and oils, ester oils, fatty acids, hydrocarbons, waxes, There are silicones, synthetic polymer compounds, semi-synthetic polymer compounds, and natural polymer compounds.
  • hair treatment materials include proteins, amino acids, animal and plant extracts, microorganism-derived materials, inorganic compounds, fragrances, preservatives, sequestering agents, ultraviolet absorbers, dyes, reducing agents, oxidizing agents, Dyes, pigments, etc.
  • anionic surfactant examples include fatty acid salts, alkyl ether carboxylates, fatty acid amide ether carboxylates, fatty acid amide ether carboxylic acids, acyl lactates, alkane sulfonates, ⁇ -olefin sulfonates, ⁇ -sulfo fatty acids.
  • Methyl ester salt acyl isethionate, alkyl glycidyl ether sulfonate, alkyl sulfosuccinate, alkyl sulfoacetate, alkyl benzene sulfonate, alkyl naphthalene sulfonate, N-acyl methyl taurate, alkyl sulfate, alkyl ether sulfate Salt, alkyl aryl ether sulfate, fatty acid alkanolamide sulfate, fatty acid monoglyceride sulfate, alkyl phosphate, polyoxyethylene alkyl ether phosphate, alkyl aryl ether phosphate, Fatty acid amide ether phosphate is mentioned.
  • the compounding concentration of the anionic surfactant is appropriately set according to the use of the hair treatment agent, and is, for example, 0.1% by mass or more and 20% by mass or less.
  • 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.
  • the blending concentration of the cationic surfactant is appropriately set according to the use of the hair treatment agent, and is, for example, 0.1% by mass or more and 20% by mass or less.
  • amphoteric surfactants include alkyl glycine salts, carboxymethyl glycine salts, N-acylaminoethyl-N-2-hydroxyethyl glycine salts, alkyl polyaminopolycarboxyglycine salts, alkylaminopropionate salts, alkyliminodipropionic acid.
  • 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-H Rokishipuropiru) sulfonate.
  • the compounding concentration of the amphoteric surfactant is appropriately set according to the use of the hair treatment agent, and is, for example, from 0.1% by mass to 10% by mass.
  • 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.
  • the blending concentration of the nonionic surfactant is appropriately set according to the use of the hair treatment agent, and is, for example, 0.1% by mass or more and 20% by mass or less.
  • Examples of the alcohol include butyl alcohol, lauryl alcohol, myristyl alcohol, cetanol, stearyl alcohol, behenyl alcohol, oleyl alcohol, isopropanol, octyldodecanol, isostearyl alcohol, hexyl decanol, benzyl alcohol, cholesterol, and phytosterol.
  • the blending concentration of alcohol is appropriately set according to the use of the hair treatment agent, and is, for example, 1% by mass or more and 50% by mass or less.
  • polyhydric alcohol examples include ethylene glycol, diethylene glycol, triethylene glycol, propylene glycol, dipropylene glycol, glycerin, diglycerin, and butylene glycol.
  • the blending concentration of the polyhydric alcohol is appropriately set according to the use of the hair treatment agent, and is, for example, 1% by mass or more and 50% by mass or less.
  • saccharide examples include sorbitol, mannitol, glucose, fructose, xylitol, lactose, maltose, maltitol, and trehalose.
  • the blending concentration of the saccharide is appropriately set according to the use of the hair treatment agent, and is, for example, 0.1% by mass or more and 10% by mass or less.
  • fats and oils examples include almond oil, avocado oil, olive oil, shea fat oil, evening primrose oil, camellia oil, peanut oil, and rosehip oil.
  • the blending concentration of fats and oils is appropriately set according to the use of the hair treatment agent, and is, for example, 0.1% by mass or more and 10% by mass or less.
  • 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, propylene glycol di (capryl / capric acid), propylene glycol dioleate, trimethylolpropane triisostearate, pentaerythritol tetra2-ethylhexanoate Isocetyl isostearate, 2-octyldodecyl dimethyloctanoate, myristyl lactate, trioctyldodecyl
  • fatty acid examples 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.
  • the blending concentration of the fatty acid is appropriately set according to the use of the hair treatment agent, and is, for example, 0.1% by mass or more and 10% by mass or less.
  • hydrocarbons examples include liquid paraffin, squalane, pristane, ozokerite, paraffin, ceresin, petrolatum, and microcrystalline wax.
  • the blending concentration of the hydrocarbon is appropriately set according to the use of the hair treatment agent, and is, for example, 0.1% by mass or more and 20% by mass or less.
  • the wax examples include beeswax, mole, candelilla wax, and carnauba wax.
  • the blending concentration of the wax is appropriately set according to the use of the hair treatment agent, and is, for example, 0.1% by mass or more and 20% by mass or less.
  • silicone examples include dimethyl silicone, methylphenyl silicone, cyclic dimethyl silicone, alcohol-modified silicone, alkyl-modified silicone, and amino-modified silicone.
  • the compounding concentration of silicone is appropriately set according to the use of the hair treatment agent, and is, for example, 0.1% by mass or more and 50% by mass or less.
  • Examples of the synthetic polymer compound include carboxyvinyl polymer, polyvinyl alcohol, polyvinyl pyrrolidone, 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.
  • the compounding concentration of the synthetic polymer compound, the semi-synthetic polymer compound and the natural polymer compound is appropriately set according to the use of the hair treatment agent, and is, for example, 0.1% by mass or more and 15% by mass or less. .
  • the hair treatment agent of this embodiment can be blended with a CAD peptide and a known hair treatment agent material appropriately selected.
  • Examples of combinations of raw materials blended with CAD peptides are as follows.
  • Examples of combinations of raw materials for hair care agents include surfactants, silicones, polymer compounds (synthetic polymer compounds, semi-synthetic polymer compounds or natural polymer compounds), alcohols, sequestering agents, and water.
  • Examples of combinations of raw materials for permanent agents include, for example, reducing agents (thioglycolic acid, cysteine, acetylcysteine, cysteamine, etc.) and alkaline agents (ammonia, monoethanolamine, ammonium hydrogen carbonate, arginine) blended in the first permanent agent.
  • coloring agent raw materials include dyes, alcohols, polymer compounds (synthetic polymer compounds, semi-synthetic polymer compounds, or natural polymer compounds) and water.
  • combinations of the raw materials for the bleaching agent include hydrogen peroxide, a surfactant, an alkali agent, and water.
  • combinations of styling agent raw materials include styling raw materials (oils and fats, ester oils, hydrocarbons, waxes, synthetic polymer compounds, semi-synthetic polymer compounds, natural polymer compounds, etc.), surfactants, and alcohols.
  • the solvent is not particularly limited, and for example, water, ethanol or the like is used. Moreover, it is although it does not specifically limit as content of the said peptide in the said raw material for hair treatment agents, For example, it is 0.1 to 10.0 mass%.
  • the peptides dissolved in the above-mentioned solvent are, for example, those having a molecular weight range of less than 40000 and a molecular weight range of 40000 to 67000.
  • CAD peptides (1a), (1b), (2a) and (2b) having a molecular weight range of less than 40,000 and the CAD peptide (3) having a molecular weight range of 40000 to 67,000 used in the hair treatment agent of the examples are as follows: is there. CAD peptides (1a), (1b), (2a) and (2b) have hair permeability, but CAD peptide (3) is considered not to have hair permeability.
  • CAD peptide (1a) was produced according to the following reduction, denaturation and hydrolysis steps.
  • [Hydrolysis step] 100 parts by mass of the solid part filtered and separated from the mixed solution after the treatment in the denaturation step, 1 part by mass of a 3% by mass proteolytic enzyme aqueous solution (“Proteerizer A” manufactured by Yamato Chemical Co., Ltd.), and the pH is 8.0 to 8.5.
  • the amount of sodium hydrogen carbonate and water set in the above were mixed, and the hydrolysis reaction was allowed to proceed in water at 50 ° C. for 20 minutes. Thereafter, the proteolytic enzyme was inactivated at 80 ° C. for 5 minutes. After the deactivation, an aqueous solution of CAD peptide (1a) was obtained by filtration.
  • CAD peptide (1a) As a result of analyzing the molecular weight of the CAD peptide (1a), it was in the range of about 1000 to 3600 (1 kDa to 3.6 kDa).
  • AXIMA Performance manufactured by Shimadzu Corporation was used as a laser ionization time-of-flight mass spectrometer (MALDI-TOFMS), the extraction voltage of analysis conditions was 20 kV, and the flight mode was Linear and detection ion were set to Positive.
  • FIG. 3 is a chart showing the results of MALDI-TOFMS analysis of CAD peptide (1a), the upper chart is a chart containing only the matrix, and the lower chart is a chart when CAD peptide (1a) is included in the matrix. It can be confirmed that the molecular weight of the CAD peptide (1a) was generally in the range of 1000 to 3600 (1 kDa to 3.6 kDa) as shown in FIG.
  • CAD peptide (1b) A CAD peptide (1b) having a molecular weight smaller than that of the CAD peptide (1a) was produced in the same manner as in the production of the CAD peptide (1a) except that the hydrolysis step was changed.
  • the hydrolysis step in the production of CAD peptide (1b) was as follows.
  • [Hydrolysis step] 100 parts by mass of the solid part filtered and separated from the mixed solution after the treatment in the denaturation step, 1 part by mass of a 3% by mass proteolytic enzyme aqueous solution (“Proteerizer A” manufactured by Yamato Chemical Co., Ltd.), and the pH is 8.0 to 8.5.
  • the amount of sodium hydrogen carbonate and water set in the above were mixed, and the hydrolysis reaction was allowed to proceed for 20 minutes in water at 50 ° C. Thereafter, the proteolytic enzyme was inactivated at 80 ° C. for 5 minutes.
  • a 3% by mass aqueous protease solution (“Proteizer A” manufactured by Daiwa Chemical Co., Ltd.) is mixed and subjected to a hydrolysis reaction at 50 ° C. for 20 minutes, and then at 80 ° C. for 5 minutes. Proteolytic enzyme was inactivated under conditions. Thereafter, an aqueous solution of CAD peptide (1b) was obtained by filtration.
  • CAD peptide (2a) A CAD peptide (2a) having a molecular weight equivalent to that of the CAD peptide (1a) was produced in the same manner as the CAD peptide (1a) except that the denaturation step was changed.
  • the denaturation step in the production of CAD peptide (2a) was as follows.
  • CAD peptide (2b) A CAD peptide aqueous solution was obtained in the same manner as CAD peptide (1b) except that the denaturation step in the production of CAD peptide (2a) was employed as the denaturation step. And this aqueous solution used the semipermeable membrane, and obtained the aqueous solution of CAD peptide (2b) of the molecular weight range 1000 or less.
  • the semipermeable membrane used for obtaining the CAD peptide (2b) is “spectra / poor” manufactured by Spectrum having a molecular weight cut-off of 1000, a plane width of 10 mm, and a diameter of 6.4 mm.
  • CAD peptide (3) A liquid part filtered and separated from the mixed solution after the denaturation step treatment in the production of CAD peptide (1a) was obtained as an aqueous solution of CAD peptide (3).
  • the molecular weight of this CAD peptide (3) was confirmed by the 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.
  • the molecular weight range of (3) was confirmed to be 40000 to 67000 (40 kDa to 67 kDa).
  • the molecular weight of the CAD peptide (3) was confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE method).
  • the molecular weight band confirmation method by this Sodium Dodecyl Sulfate-polyacrylamide gel electrophoresis method (SDS-PAGE method) will be described in detail below.
  • Phosphorylase B molecular weight 97200
  • Serum Albumin molecular weight 66409
  • Ovalbumin molecular weight 44287
  • Carbonic anhydrase molecular weight 29000
  • Trypsin inhibitor molecular weight 20100
  • Sample solution CAD peptide or standard substance 1 part by mass Bromophenol blue appropriate amount 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 staining, decolorization with decoloring solution for about 6 hours (7) Analysis results Fig.
  • FIG. 4 shows an electrophoretic gel photograph of CAD peptide (3) and molecular weight marker that had been subjected to treatment under the conditions (1) to (6) above.
  • FIG. 5 is a graph showing the relationship between the band distance X (cm) of the molecular weight marker based on the predetermined position and the logarithm Y (ln [kDa]) of the molecular weight based on the electrophoresis gel photograph.
  • the molecular weight of the CAD peptide (3) was confirmed to be in the range of 40000 to 67000 (40 kDa to 67 kDa), more specifically 49000 (49 kDa) to 64000 (64 kDa).
  • hair was treated according to hair treatment 1 using the hair treatment agent of Example 1a or the hair treatment agent of Example 1b.
  • the initial elastic modulus and breaking strength of the untreated hair and the treated hair were measured.
  • Example 1a A 3% by weight aqueous solution of CAD peptide (1a) was prepared as the hair treatment agent of Example 1a.
  • Example 1b A 3% by weight aqueous solution of CAD peptide (3) was prepared as the hair treatment agent of Example 1b.
  • the hair sample 1 in the present hair treatment 1 is obtained by treating straight black hair as follows.
  • Straight hair black hair was processed by the procedures of bleaching, perm treatment, color treatment, hair washing treatment, color treatment, hair washing treatment, perm treatment, color treatment, hair washing treatment, color treatment, hair washing treatment, and drying treatment.
  • the first agent and the second agent of “Promatis Flavor-Ad” manufactured by Milbon were mixed in a ratio of about 1 part by mass: 2 parts by mass, and this was applied to the hair.
  • the coating amount was twice the hair mass.
  • the coated hair was covered with a film, washed with shampoo after 15 minutes, and dried with warm air.
  • hair wound around a perm rod with a diameter of 12 mm is dipped in the first agent of “Pre-Cum C / T” manufactured by Milbon for 10 minutes, washed with water, and then second of “Pre-Cum C / T”. It was immersed in the agent for 10 minutes and washed with water. Thereafter, the hair was dried with warm air.
  • the first agent and the second agent of “Oldive” manufactured by Milbon were mixed in a ratio of 1 part by mass: 1 part by mass, and this was applied to the hair.
  • the coating amount was 10 times the mass of the hair, and was allowed to stand for 10 minutes after coating.
  • Table 1 below shows the initial elastic modulus and breaking strength results for hair treated according to hair treatment 1 and untreated hair.
  • Measured average value is an average value of 5 times of measurement
  • “Change rate” is based on untreated hair.
  • Example 1a in which the CAD peptide (1a) having a molecular weight range of 1000 to 3600 was blended, the initial elastic modulus and the rate of change in breaking strength showed positive values, and the CAD peptide (1a) Can be confirmed to be suitable for improving the initial elastic modulus and breaking strength of hair that has been greatly damaged.
  • Example 1b in which the CAD peptide (3) having a molecular weight range of 40,000 to 67,000 was blended, the change rate of the initial elastic modulus showed a positive value, and the CAD peptide (3) is suitable for improving the initial elastic modulus. I can confirm that.
  • the initial elastic modulus result of Example 1a and Example 1b shows that the CAD peptide is suitable for improvement or suppression of deterioration of the initial elastic modulus of hair.
  • Example 2a A 5% by weight aqueous solution of CAD peptide (2a) was prepared as the hair treatment agent of Example 2a.
  • Example 2b A 5% by weight aqueous solution of CAD peptide (2b) was prepared as the hair treatment agent of Example 2b.
  • the hair was treated according to the hair treatment 2a described later. Moreover, about the untreated hair and the hair after a process, the initial elastic modulus, breaking strength, and elongation were measured, and the distance between microfibrils (IF: intermediate filament) was also calculated.
  • IF intermediate filament
  • Camera length Approximately 2000mm Detector pixel size: 140.8 ⁇ m / pixel ⁇ 140.8 ⁇ m / pixel Image size: 1344 pixels ⁇ 1024 pixels
  • Table 2a shows the initial elastic modulus of the hair after the hair treatment 2a.
  • “Measurement average value” is an average value of 10 measurements
  • “Change rate” is based on untreated hair.
  • “Untreated” in Table 2a means that the cation treatment and the treatment with the hair treatment agent of Example 2a or Example 2b were omitted.
  • the “inter-IF distance” is an average value of 800 samples.
  • Example 2a In Table 2a, it can be confirmed that both Example 2a and Example 2b were superior in initial elastic modulus and breaking strength compared to untreated. Moreover, the inter-IF distance in Example 2a is longer than the untreated inter-IF distance, and it is expected that CAD peptide (2a) was deposited in the hair after hair treatment 2a.
  • Example 2a Using the hair treatment agent of Example 2a or Example 2b, the hair was treated according to the hair treatment 2b described later. In addition, the initial elastic modulus, breaking strength, and elongation of untreated hair and treated hair were measured.
  • hair treatment 2b The same treatment as the hair treatment 2a was designated as the hair treatment 2b except that only the reduction treatment of the hair treatment 2a was different in the following points.
  • an aqueous solution containing 9% by mass of thioglycolic acid and 2% by mass of dithioglycolic acid (adjusted to pH 9.3 with monoethanolamine) is used instead of the 3% by mass thioglycolic acid aqueous solution. did.
  • Table 2b shows the initial elastic modulus and the like of the hair after the hair treatment 2b. “Measured average value”, “change rate”, and “untreated” in Table 2b have the same meaning as described in Table 2a.
  • Example 3a As described below, the shampoos of Example 3a, Example 3b and Comparative Example 3 were prepared, and the hair was treated according to Hair Treatment 3.
  • Example 3a The hair treatment agent of Example 3a was prepared by blending CAD peptide (1a) with “Death Shampoo S” manufactured by Milbon in an amount of 2% by mass.
  • Example 3b The hair treatment agent of Example 3b was prepared by blending CAD peptide (3) to 2% by mass with “Death Shampoo S” manufactured by Milbon.
  • Comparative Example 3 The hair treatment agent of Comparative Example 3 was “Death Shampoo S” manufactured by Milbon.
  • a professional evaluator evaluated the feel of the hair bundle treated according to Hair Treatment 3.
  • the hair bundle treated with the hair treatment agent of Example 3a and Example 3b was smoother than the hair bundle treated with the hair treatment agent of Comparative Example 3.
  • the hair bundle processed with the hair treatment agent of Example 3b had a feeling of thickness rather than the hair bundle processed with the hair treatment agent of the comparative example.
  • the “thickness” means a feeling that a substance is coated on the hair surface, and the meaning is the same in the following examples.
  • the hair treatment agents of Example 4a, Example 4b, Example 4c and Comparative Example 4 were prepared as follows, and the hair was treated according to hair treatment 4.
  • Example 4a A 0.2% by mass aqueous solution of CAD peptide (1a) was prepared as the hair treatment agent of Example 4a.
  • Example 4b A 0.2% by mass aqueous solution of CAD peptide (1b) was prepared as the hair treatment agent of Example 4b.
  • Example 4c A 0.2 mass% aqueous solution of CAD peptide (3) was prepared as the hair treatment agent of Example 4c.
  • a professional evaluator evaluated the feel of the hair bundle treated according to the hair treatment 4.
  • the hair bundle treated with the hair treatment agent of Example 4c was thicker than the hair bundle treated with the hair treatment agent of Comparative Example 4.
  • the hair bundle treated with the hair treatment agent of Example 4a and Example 4b was smoother and softer than the hair bundle treated with the hair treatment agent of Example 4c.
  • Example 5 A shampoo containing 0.2% by mass of CAD peptide (3) in the hair treatment agent of Comparative Example 5 described later was used as the hair treatment agent of Example 5.
  • Hair treatment 5 A plurality of hair bundles obtained by combining 3 g of the bleached hair were prepared and used as evaluation hair bundles.
  • the hair bundle was treated by the procedures of application of the hair treatment agent of Example 5, Comparative Example 5 or Reference Example 5, washing with water, application of treatment (hair treatment agent of Comparative Example 6 described later), washing with water and drying with warm air.
  • a professional evaluator evaluated the feel of the hair bundle treated according to the hair treatment 5 on the basis of the hair treatment agent of Comparative Example 5. The evaluation results are shown in Table 3 (Evaluation “-” in the table indicates that no evaluation was performed).
  • Example 6 A treatment comprising 0.2% by mass of CAD peptide (3) in the hair treatment agent of Comparative Example 6 described later was used as the hair treatment agent of Example 6.
  • Hair treatment 6 A plurality of hair bundles obtained by combining 3 g of the bleached hair were prepared and used as evaluation hair bundles. The hair bundle was treated by applying shampoo (hair treatment agent of Comparative Example 5), washing with water, applying the hair treatment agent of Example 6, Comparative Example 6 or Reference Example 6, washing with water, and drying with warm air.
  • a professional evaluator evaluated the feel of the hair bundle treated according to the hair treatment 6 on the basis of the hair treatment agent of Comparative Example 6. The evaluation results are shown in Table 4 (Evaluation “-” in the table indicates that no evaluation was performed).
  • Example 7 A non-washing-out cream treatment in which 0.2% by mass of CAD peptide (3) was added to the hair treatment agent of Comparative Example 7 described later was used as the hair treatment agent of Example 7.
  • a 4% by mass aqueous solution of CAD peptide (3) adjusted to pH 8.72 using arginine was used.
  • Table 5 shows the evaluation results of the feeling of thickness. From the results in Table 5, it can be seen that the cream of Example 7 formulated with CAD peptide (3) has a greater sense of thickness compared to the cream of Comparative Example 7 that did not incorporate CAD peptide (3) or keratin. It was.
  • Example 8 The hair treatment agent of Example 8 was prepared by applying a cream treatment containing 2% by mass of CAD peptide (3), 2% by mass of cetyltrimethylammonium bromide, 1% by mass of ethanol, 3% by mass of cetanol and 2% by mass of stearyl alcohol in water. It was.
  • a professional evaluator evaluated the feel of the hair bundles treated according to the hair treatment 8a and the hair treatment 8b. The evaluation results are shown in Table 6.
  • Example 9 10 parts by weight of 1% by weight of CAD peptide (3) added to Milbon's “Licente 1st Agent / 9-AB”, 10 parts by weight of Milbon's “Licente 2nd Agent (Oxidane 3.0)”
  • the hair dye obtained by mixing the above was used as the hair treatment agent of Example 9.
  • a professional evaluator evaluated the feel of the hair bundle treated according to the hair treatment 9. As a result of the evaluation, the hair bundle treated with the hair treatment agent of Example 9 was good according to the finger when the hair was washed.
  • Example 10 The hair treatment agent of Example 10 was obtained by adding 0.5% by mass of the CAD peptide (3) to “Presume C / T First Agent” manufactured by Milbon (first agent of a two-agent perm agent). .
  • Comparative Example 10 The hair treatment agent of Comparative Example 10 was obtained by adding the CAD peptide (3) of Example 10 without addition, that is, “Presume C / T First Agent” alone from Milbon.
  • Example 10 (Hair treatment 10) The hair treatment agent of Example 10 or Comparative Example 10 was applied to the hair bundle, allowed to stand for 15 minutes, washed with water, and wiped with a towel. Next, apply “Presume C / T 2nd Agent” manufactured by Milbon and let it stand for 5 minutes, then wash with water, apply “Diess Neu Willowlux Treatment” manufactured by Milbon, rinse with water, The bundle was dried with warm air.
  • a professional evaluator evaluated the feel of the hair bundle treated according to the hair treatment 10. As a result of the evaluation, the hair bundle treated with the hair treatment agent of Example 10 had a feeling of thickness rather than the hair bundle treated with the hair treatment agent of Comparative Example 10.
  • the hair treatment agent of the present invention is effective for improving or suppressing the deterioration of the initial elastic modulus and breaking strength of damaged hair, and is therefore suitably used for commercial or household hair treatment. Is done.

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Abstract

L'invention porte sur un agent de traitement capillaire dans lequel un peptide comprenant un groupe comportant une unité représentée par la formule suivante (I) en tant que groupe à chaîne latérale est mélangé : -S-S-(CH2)nCOO- (I). (Dans la formule (I), n représente 1 ou 2). Le groupe à chaîne latérale dans le peptide est de préférence composé d'un ou plusieurs éléments choisis parmi des groupes bisulfure carboxyméthyl, des sels du groupe bisulfure carboxyméthyl, des groupes bisulfure carboxyméthyl et de sels de groupe bisulfure carboxyméthyl. La masse moléculaire du peptide est de préférence inférieure à 40 000. Le peptide a de préférence une perméabilité vis-à-vis des cheveux.
PCT/JP2010/057724 2009-06-12 2010-04-30 Agent de traitement capillaire et matière première pour agent de traitement capillaire Ceased WO2010143484A1 (fr)

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