KR101951923B1 - Hair treatment agent and starting material for hair treatment agent - Google Patents
Hair treatment agent and starting material for hair treatment agent Download PDFInfo
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- KR101951923B1 KR101951923B1 KR1020117029136A KR20117029136A KR101951923B1 KR 101951923 B1 KR101951923 B1 KR 101951923B1 KR 1020117029136 A KR1020117029136 A KR 1020117029136A KR 20117029136 A KR20117029136 A KR 20117029136A KR 101951923 B1 KR101951923 B1 KR 101951923B1
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- A—HUMAN NECESSITIES
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- 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
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
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Abstract
A hair treatment agent comprising 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 side chain group in the peptide is preferably at least one member selected from a carboxymethyl disulfide group, a salt of a carboxymethyl disulfide group, a carboxyethyl disulfide group, and a salt of a carboxyethyl disulfide group. The molecular weight range of the peptide is preferably less than 40,000. It is preferable that the peptide has hair permeability.
Description
The present invention relates to hair treating agents used in hair care treatment, perming treatment, coloring treatment and bleaching treatment of hair, and raw materials for hair treating agents used in the production of the hair treating agents.
Physical treatments such as brushing, hand dryers, thermal irons, and chemical treatments such as coloring and perming treatments damage hair. Damaged hairs are more susceptible to hair characteristics such as hair feel (e.g., liveliness, elasticity, softness), appearance (e.g., luster, tidiness), and strength (e.g., tensile strength) It becomes worse. In order to improve hair properties or inhibit deterioration of hair characteristics, it is known that a hair treatment agent is appropriately selected from denatured peptides into which a transformant such as peptides and ester groups derived from natural products have been introduced.
As described above, it is known that, when a moderately selected modified peptide is incorporated into a hair treatment agent, it is possible to improve the hair characteristics or inhibit the deterioration of the hair characteristics, and the search for a modified peptide suitable for the combination continues.
Further, Japanese Patent Publication No. 7-126296 and No. there is disclosed a modified form of a peptide, a modified peptide that is carboxymethyl disulfide group (-SS-CH 2 COOH) a disulfide group (-SS-) of protein Which is obtained by conversion. Japanese Patent Application Laid-Open No. 7-126296 discloses that a film is formed with the modified peptide as a specific use of the modified peptide, but the hair treatment agent is not intended.
SUMMARY OF THE INVENTION In view of the above circumstances, it is an object of the present invention to provide a hair treatment agent and a raw material thereof capable of suppressing deterioration of the initial elastic modulus of the damaged hair or deterioration of the initial elastic modulus of the hair.
The inventors of the present invention have focused on the initial modulus of elasticity of the hair and have studied the hair treatment agent. As a result, it has been found that the initial elastic modulus of the hair is improved by treating the hair with water containing a peptide having a predetermined side chain. Based on this finding, the present invention has been completed.
That is, the hair treatment agent according to the present invention is characterized by comprising 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.)
Herein, the term " peptide " in the present invention refers to a peptide in which two or more amino acids are bound by peptide bonds, and proteins such as keratin proteins and collagen proteins also correspond to peptides.
The side chain group in the peptide may be one or more selected from a carboxymethyl disulfide group, a salt of a carboxymethyl disulfide group, a carboxyethyl disulfide group, and a salt of a carboxyethyl disulfide group.
The molecular weight of the peptide is preferably less than 40,000, more preferably 20,000 or less. When the peptide of the present invention has a molecular weight in a range of less than 40,000, it is advantageous not only to improve or deteriorate the initial elastic modulus of the hair, but also to improve the fracture strength of the hair or suppress deterioration of the hair.
It is preferable that the peptide has hair permeability. If the peptide has permeability to hair, the initial elastic modulus and fracture strength of the hair are improved or the deterioration inhibiting action is better.
Among these peptides, the molecular weight range of those having a high molecular weight is, for example, from 40,000 to 67,000, and from 49,000 to 64,000. Even when a peptide having such a molecular weight range is blended, improvement or deterioration of the initial elastic modulus of the hair described above effectively appears.
The hair treatment agent according to the present invention is used as a hair care agent, a pharmacological agent, a coloring agent, a bleaching agent or a styling agent.
The hair treatment agent according to the present invention is produced, for example, by using a hair treatment agent raw material in which a peptide having a group having a unit represented by the following formula (I) as a side chain group is dissolved in a solvent such as water.
-SS- (CH 2 ) n COO- (I)
(In the formula (I), n is 1 or 2.)
According to the hair treatment agent according to the present invention in which a predetermined peptide is blended, it is possible to realize an improvement in initial elasticity of hair or inhibition of deterioration.
FIG. 1 is a fluorescence microscope photograph of hair having peptides penetrating therein. FIG.
FIG. 2 is a fluorescence microscope photograph of hair in which peptides do not penetrate inside. FIG.
3 is a MALDI-TOFMS analysis chart of a CAD peptide (1a) compounded in the hair treatment agent of the Example.
FIG. 4 is a photograph of the electrophoresis gel of CAD peptide (3) blended with the hair treatment agent of the example by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).
5 is a graph showing the calibration curve of the molecular weight marker in the sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE method) of the CAD peptide (3) blended with the hair treatment agent of the example.
The present invention is described below on the basis of embodiments.
The hair treatment agent according to the present embodiment is prepared by blending a peptide having a predetermined side chain (hereinafter referred to as " a peptide having a predetermined side chain group "
(CAD peptides)
The CAD peptide has a main chain formed by peptide bonding of a plurality of amino acids and a side chain group bonded to the main chain.
The backbone of the CAD peptide is not particularly limited. Examples of the main chain include the same as the main chain of a peptide in which cysteine is a constituent amino acid. Examples of peptides having cysteine as a constituent amino acid 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 for efficiently obtaining the CAD peptide. From this viewpoint, the main chain of the CAD peptide is preferably the same as the main chain of the keratin.
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 such side chains are present in the CAD peptide. When the group represented by the formula (I) is dissociated (ionized) to form a carboxylato anion, it is referred to as 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 are 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) And a salt of a carboxyethyl disulfide group represented by the following formula (IIB) or (IIC).
-SS-CH 2 COOH (IA)
-SS-CH 2 COOR 1 (IB)
(R 1 represents ammonium such as NH 4 )
-SS-CH 2 COOM 1 (IC)
(M < 1 > represents a metal atom such as Na or K).
-SS-CH 2 CH 2 COOH (IIA)
-SS-CH 2 CH 2 COOR 2 (IIB)
(R 2 represents ammonium such as NH 4 )
-SS-CH 2 CH 2 COOM 2 (IIC)
(M 2 represents a metal atom such as Na or K).
The preferred group is the following formula as a side chain group (Ia), (Ib), (Ic), (IIa), (IIb), and R 1 in one or two or more than (the following formula selected from (IIc), M 1 , R 2 , and M 2 are the same as above).
-CH 2 -SS-CH 2 COOH (Ia)
-CH 2 -SS-CH 2 COOR 1 (Ib)
-CH 2 -SS-CH 2 COOM 1 (Ic)
-CH 2 -SS-CH 2 CH 2 COOH (IIa)
-CH 2 -SS-CH 2 CH 2 COOR 2 (IIb)
-CH 2 -SS-CH 2 CH 2 COOM 2 (IIc)
When the hair is treated with a hair treating agent containing CAD peptides having two or more side chain groups, it is considered that the mercapto groups constituting the hair are crosslinked through the CAD peptides. In addition to the crosslinking, it is also possible that only one side chain group in the CAD peptide reacts with the mercapto group of the hair, or the polymerization reaction of the CAD peptide reacted with the mercapto group of the hair and another CAD peptide Polymerization of CAD peptides in the hair is also considered. It is presumed that the cross-linking and the reaction thereof realize the following (1) or (2).
(1) Improvement or deterioration of initial elastic modulus of hair.
(2) improvement or deterioration of the initial elastic modulus of the hair, and improvement or deterioration of the breaking strength of the hair.
The above (1) and (2) indicate that it is preferable to use a hair treatment agent containing a CAD peptide for hair having increased mercapto groups due to damage.
Hereinafter, the crosslinking mechanism through a CAD peptide between a pair of mercapto groups will be described in detail.
A CAD peptide having two -CH 2 -SS-CH 2 COOH as a side chain group is exemplified as a crosslinking mechanism through a CAD peptide between mercapto groups in hair as an example.
Further, a CAD peptide having two -CH 2 -SS-CH 2 CH 2 COOH as a side chain group can be exemplified as a crosslinking mechanism through a CAD peptide between a pair of mercapto groups in hair as follows .
The molecular weight of the CAD peptide in the present embodiment is not particularly limited. CAD peptides are 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 to 67,000.
If the hair treatment agent is blended with a CAD peptide having a molecular weight range of less than 40,000, the initial elastic modulus and fracture strength of damaged hair can be improved or deterioration can be suppressed. The smaller the molecular weight of the CAD peptide is, the more advantageous it is to improve or deteriorate the initial elastic modulus and fracture strength of the hair. Therefore, the molecular weight range of the CAD peptide in the present embodiment is preferably 20000 or less, more preferably 10000 or less, Or less. The lower limit value of the molecular weight range of the CAD peptide is not particularly limited, but is 500, for example.
When the molecular weight range of the CAD peptide is less than 40,000, the m / z peak by time-of-flight mass spectrometry (TOFMS) employing the matrix-assisted laser desorption ionization (MALDI) method is regarded as the molecular weight of the CAD peptide, .
In the CAD peptide according to this embodiment, it is preferable that the peak of the highest intensity in the result of the TOFMS is confirmed at m / z of 20000 or less, more preferably at m / z of 10,000 or less, Is particularly preferable. The lower limit value of the peak of the highest intensity is not particularly limited, but is, for example, m / z 500.
If the CAD peptide has hair permeability (permeability into the hair), it exhibits the action of crosslinking or the like into the inside of the hair, and therefore, it is preferable that the CAD peptide in this embodiment has hair permeability.
The fact that the CAD peptide has hair permeability can be confirmed by the following procedures (1) to (4). (1) FTSC-MES is added to a CAD peptide aqueous solution. The FTSC-MES shall be prepared as follows. A MES aqueous solution having a pH of 5.5 was prepared by dropping 0.2 M-NaOH aqueous solution into a solution prepared by dissolving 1.065 parts by mass of 2- (N-Morpholino) ethanesulfonic acid (MES) in 40 parts by mass of water. Then, 0.00042 part by mass FTSC-MES is prepared by dissolving the fluorescent dye Fluorescein-5-thiosemicarbazide (FTSC) and adding water to the total amount of about 50 parts by mass. (2) The virgin hair was immersed in an aqueous solution of CAD peptide after addition of FTSC-MES for 10 minutes, and the hair was washed with water and then dried at room temperature. (3) Cut the dried hair with a microtome. (4) The cut surface of the hair is observed under a fluorescence microscope (excitation light wavelength: 340 nm). If fluorescence can be confirmed on the inner side of the cuticle in the fluorescence microscopic observation of the procedure (4) above, the hair permeability of the CAD peptide can be confirmed. Fig. 1 is a photograph of a fluorescence microscope photograph taken in the order of the above (1) to (4). Fluorescence inside hair, that is, hair permeability of CAD peptides can be confirmed. On the other hand, FIG. 2 shows a fluorescence microscopic photograph of the procedure of (1) to (4) above in which the CAD peptide was not blended. Fluorescence, that is, no CAD peptide, . This is because the fluorescence microscope observation image of FIG. 2 can not confirm the fluorescence inside the hair because even if only the fluorescent material penetrates into the virgin hair, there is no chemical damage inside the virgin hair, This is because it flows out of virgin hair.
In the case of a hair treatment agent containing a CAD peptide having a molecular weight range of 40000 or more and 67000 or less, the initial elastic modulus of damaged hair can be improved or deterioration can be performed. The molecular weight range of the CAD peptide may be 49000 or more and 64000 or less.
When the molecular weight range of the CAD peptide is 40000 or more and 67000 or less, the molecular weight calculated from the relative distance between the bands of the CAD peptide and the molecular weight marker by the sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE method) It is regarded as molecular weight, and it can be confirmed from this molecular weight range.
The lower limit of the amount of the CAD peptide in the hair treatment agent according to the present embodiment is not particularly limited, but is preferably 0.01% by mass, more preferably 0.05% by mass, and most preferably 0.10% by mass. The upper limit of the amount of the one-way CAD peptide is not particularly limited, but is preferably 15% by mass, more preferably 10% by mass, more preferably 5% by mass, still more preferably 3% by mass More preferable.
Further, if the hair treatment agent is a compound of a CAD peptide having a molecular weight range of less than 40,000, CAD peptides other than CAD peptides having a molecular weight range of less than 40,000, for example, 40,000 or more and 67,000 or less of CAD peptides may be further blended. Further, if a compound having a molecular weight range of 40,000 or more and 67,000 or less is compounded, CAD peptides other than 40,000 to 67,000 in molecular weight range, for example, 40,000 or less of CAD peptides may be added.
(A method for producing a CAD peptide having a molecular weight range of less than 40000)
Examples of the method for producing a CAD peptide having a molecular weight range of less than 40,000 include the following production methods (A), (B) and (C).
[Manufacturing method (A)]
The production method (A) comprises a reduction step of converting a disulfide group of a protein into a mercapto group; (I) is formed by a mercapto group formed on a protein molecule in the reduction process and a mercapto group of a mercaptoalkylcarboxylic acid and / or a mercapto group of a mercaptoalkylcarboxylic acid. Denaturation process; And a hydrolysis step of hydrolyzing the protein introduced with the unit represented by the formula (I) obtained by the treatment in the denaturation step.
In the reduction step, the disulfide group (-S-S-) of the protein is reduced to two mercapto groups (-SH HS-) by mixing the raw material containing protein, water and a reducing agent.
Examples of the raw materials for production include wool (merino wool, Lincoln wool, etc.), human hair, hair follicles, feathers, fingernails and the like containing keratin as a constituent protein. Among them, wool is preferably used as a raw material in order to obtain an inexpensive and stable product. The raw materials for production may be sterilized, degreased, washed, cut, pulverized, and dried in an appropriate combination beforehand.
The amount of water is not particularly limited, but may be 20 parts by mass or more and 200 parts by mass or less with respect to 1 part by mass of the raw material for production, for example. By setting the amount of water within the above range, the reduction reaction is performed well.
In the reduction of the protein in the present reduction, the mercapto group is produced by reducing the disulfide bond in the protein with one or two or more reducing agents in the alkaline solution.
The compound (alkaline compound) for making the reaction system alkaline in the reduction of the disulfide bond is added to water to make the water alkaline. Examples of the alkaline compound include lithium hydroxide, sodium hydroxide, potassium hydroxide, barium hydroxide, sodium carbonate, potassium carbonate, and ammonia. In addition, basic amino acids such as monoethanolamine, diethanolamine, arginine and lysine , Sodium bicarbonate, ammonium bicarbonate, and the like. Among them, sodium hydroxide and potassium hydroxide are preferable, and sodium hydroxide is particularly preferable from the viewpoint of efficient and inexpensive protein reduction. One or more of the alkaline compounds are used.
The mixing amount of the alkaline compound is not particularly limited, but may be adjusted so as to adjust the pH of the reduction reaction system to the following range. The lower limit of the pH is preferably 9, more preferably 10. On the other hand, as the upper limit of the pH, 13 is preferable, 12 is preferable, and 11 is particularly preferable. By adjusting the pH to be equal to or lower than the lower limit, the protein can be efficiently reduced. On the other hand, by adjusting the pH to be equal to or less than the above-mentioned upper limit, it is possible to suppress the main chain cleavage of protein molecules.
As the reducing agent, a mercaptoalkylcarboxylic acid and / or a salt thereof is used. In addition to the mercaptoalkylcarboxylic acid and / or its salt as the reducing agent, any other compound may be used. Examples of such an optional reducing agent include thiolactic acid and / or its salt, dithiothreitol, 2-mercaptoethanol, glutathione, thiourea and the like. These optional reducing agents may be used alone or in combination of two or more.
The mercaptoalkylcarboxylic acid and / or its salt is subjected to a denaturation scheme in which the unit represented by the formula (I) is formed in the denaturation step. As the mercaptoalkylcarboxylic acid and / or its salt, one or two or more selected from thioglycolic acid, thioglycolic acid salt, 3-mercaptopropionic acid and 3-mercaptopropionic acid salt is used. Examples of the thioglycolic acid salt include sodium thioglycolate, potassium thioglycolate, lithium thioglycolate and ammonium thioglycolate. Of these, sodium thioglycolate and potassium thioglycolate are preferable, and sodium thioglycolate is more preferable in that the formation of the carboxylatormethyl disulfide group can be efficiently performed. Examples of the 3-mercaptopropionate salt include sodium 3-mercaptopropionate, potassium 3-mercaptopropionate, lithium 3-mercaptopropionate and ammonium 3-mercaptopropionate. Among them, sodium 3-mercaptopropionate and potassium 3-mercaptopropionate are preferable, and sodium 3-mercaptopropionate is more preferable in that the carboxylatetoethyl disulfide group can be efficiently formed.
The amount of the mercaptoalkylcarboxylic acid and its salt to be used is preferably 0.0050 mol or more and 0.02 mol or less, more preferably 0.0075 mol or more and 0.01 mol or less, based on 1 g of the starting material. The amount to be used is preferably 0.10 mol / L or more and 0.40 mol / L or less, and particularly preferably 0.15 mol / L or more and 0.25 mol / L or less, based on the total volume of the raw material for production, water and the reducing agent. When the amount of the mercaptoalkylcarboxylic acid and its salt used is within the above range, the progress of the reduction reaction of the protein becomes better.
The lower limit of the temperature of the reaction system in the reduction step is preferably 20 占 폚, more preferably 30 占 폚, and further preferably 40 占 폚. On the other hand, the upper limit of the temperature is preferably 60 占 폚. When the temperature is lower than the lower limit, the time for reduction to convert the disulfide group of the protein to the mercapto group becomes longer, and there is a fear that sufficient reduction can not be performed. On the other hand, when the temperature is above the upper limit, the main chain of the protein molecule may be cleaved. The set time of the reduction reaction system is set to a longer time as the temperature is lower, and to a shorter time as the temperature is higher. The setting time is, for example, 20 minutes or more and 120 minutes or less.
In the denaturation step, the unit represented by the formula (I) is introduced into the protein by mixing an acid and an oxidizing agent into the solution obtained in the reducing step. The mixing of the acid may be either before the mixing of the oxidizing agent, after the mixing of the oxidizing agent, or simultaneously with the mixing of the oxidizing agent.
The acid is used for lowering the pH of the reaction system in the denaturation step and sufficiently introducing the unit represented by the formula (I) into the protein. One or more of these acids may be used.
Examples of acids include organic acids such as citric acid, lactic acid, succinic acid, and acetic acid; And inorganic acids such as hydrochloric acid. When acetic acid is used, a peculiar smell from a CAD peptide may be a problem, but when citric acid or the like is used, the peculiar smell can be suppressed.
The mixing amount of the acid is not particularly limited, but may be adjusted so that the pH of the reaction system in the denaturation step is adjusted to the following range. The final pH is preferably 5 or more and 9 or less, and particularly preferably 6 or more and 8 or less. By adjusting the final pH of the keratin mixed solution to the above range, the introduction of the unit represented by the formula (I) into the protein can be promoted, and the generation of the disulfide group by the mercapto groups of the protein can be promoted . In addition, if the pH in the reaction system is locally lowered, it is preferable that the acid is gradually mixed into the reaction system, since the possibility that the mercapto groups of the proteins become disulfide groups increases.
The temperature in the reaction system at the time of mixing the acid is preferably from 10 캜 to 60 캜, and particularly preferably from 20 캜 to 40 캜. By controlling the temperature within this range, generation of byproducts such as cysteine monoxide and the like can be suppressed. The incubation time after completion of the acid mixing is, for example, 1 hour or more and 48 hours or less. The introduction of the unit represented by the above formula (I) is sufficient in the case of this leaving time.
The oxidizing agent is used to promote the introduction of the unit represented by the formula (I) into a protein. One or more oxidizing agents may be used.
Examples of the oxidizing agent include sodium bromate, potassium bromate, sodium perborate, hydrogen peroxide and the like.
The amount of the oxidizing agent to be used is not particularly limited, but is preferably from 0.001 to 0.02 mol based on 1 g of the starting material, and is preferably 0.02 mol / L or more and 1 mol / L or less based on the capacity of the liquid to be mixed with the oxidizing agent. If the amount of the oxidizing agent used is larger than the upper limit, there is a possibility that byproducts such as cysteine monoxide, cysteine dioxide and cysteine acid are produced. On the other hand, if the amount of the oxidizing agent used is less than the above lower limit, there is a fear that the introduction of the unit represented by the formula (I) becomes insufficient. In the mixing of the oxidizing agent, an oxidizing agent solution of about 1 mol / L or more and about 5 mol / L or less may be gradually mixed over a period of, for example, 30 minutes to 6 hours to avoid local increase in the oxidizing agent concentration in the liquid.
The temperature at which the oxidizing agent is mixed is not particularly limited, but is set at, for example, below the temperature in the reducing step.
By passing through the denaturation step, the unit represented by the above formula (I) is introduced into the protein. For example, when wool is used as a raw material for production and thioglycolic acid is used as a reducing agent, a mechanism in which a carboxymethyl disulfide group as one of the units represented by the formula (I) is introduced into a protein molecule is as follows.
When wool is used as a raw material for production and 3-mercaptopropionic acid is used as a reducing agent, the mechanism by which the carboxyethyl disulfide group, which is one of the units represented by the formula (I), is introduced into the protein molecule is as follows.
The protein into which the unit represented by the formula (I) is introduced by the treatment in the denaturation step includes a protein soluble in water and a protein insoluble in water. For the solution containing these proteins, desalting by ion exchange, electrodialysis or the like may be carried out if necessary.
In the hydrolysis step, a protein soluble in water or a protein insoluble in water is hydrolyzed by the unit represented by the formula (I) obtained by the treatment in the denaturation step. The hydrolysis thereof includes known hydrolysis methods such as (a1) hydrolysis with an enzyme, (a2) hydrolysis with an acid, and (a3) hydrolysis with an alkali. In the hydrolysis method (a3) by alkali, there is a possibility that the β-elimination reaction of the unit represented by the above formula (I) introduced into the protein proceeds, so that in the hydrolysis methods (a1) to (a3) Is preferred, and a method using an enzyme is more preferable.
(a1) hydrolysis with an enzyme
Examples of the enzyme include acid proteases such as pepsin, protease A and protease B; Papain, bromelain, sumolysin, proanase, trypsin, chymotrypsin, and the like. As a commercially available protease, for example, " Protease A " The pH at the hydrolysis may be adjusted to 1 or more and 3 or less in the case of acidic protease, and 5 or more and 9 or less in the case of neutral protease. The reaction temperature at hydrolysis is preferably 30 ° C to 60 ° C, and the reaction time is preferably within 10 minutes to 24 hours. (The longer the reaction time, the lower the molecular CAD peptide can be produced). In order to stop the hydrolysis, the enzyme may be deactivated by setting the temperature to 70 ° C or higher.
(a2) Hydrolysis with acid
Examples of the acid 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 conditions for the hydrolysis are, for example,
(a3) Hydrolysis with alkali
Examples of the alkali include sodium hydroxide, potassium hydroxide, lithium hydroxide, barium hydroxide, sodium carbonate, potassium carbonate, lithium carbonate, sodium silicate and sodium borate. The conditions for the hydrolysis are, for example, 1% by mass or more and 20% by mass or less of alkali, 15% or more and 100 占 폚 or less of alkali, and 30 minutes or more and 24 hours or less of reaction time with respect to the total mass of the reaction system , A lower-molecular-weight CAD peptide can be produced).
By the treatment in the hydrolysis step, a solution in which the CAD peptide having a molecular weight range of less than 40000 is dissolved is obtained. When it is necessary to separate the solids contained in the liquid, it may be separated by a known solid-liquid separating means such as filtration, centrifugal separation, compression separation, sedimentation separation, float separation or the like. When the CAD peptide having a molecular weight in a range of less than 40,000 is required to be solid, (1) lyophilization of a CAD peptide solution, (2) spray drying of a CAD peptide solution, and (3) (The smaller the molecular weight of the CAD peptide is, the more difficult it is to produce a CAD peptide precipitate in the method (3)). The recovered solid CAD peptide may be washed and dried with water or an acidic aqueous solution as necessary.
[Manufacturing method (B)]
The production method (B) is a method in which a protein insoluble in water obtained in a reducing step and a denaturation step similar to those in the production method (A) is separated and treated in a 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). As a means for obtaining a solid CAD peptide, the means of production method (A) may be employed.
In addition, since the microfibrils and the matrix having a higher sulfur content than those of the microfibrils are composed of the constitutive keratin of wool, the water-soluble proteins derived from microfibrils are not mainly hydrolyzed in the hydrolysis step in the production method (B) The insoluble protein derived from the matrix is the main hydrolysis target. That is, the production method (B) is suitable for the production of CAD peptides having a high sulfur content.
[Manufacturing method (C)]
The production method (C) is a method in which a protein dissolved in water obtained in the reducing step and the denaturation step similar to the production method (A) is separated and treated in the hydrolysis step. The protein dissolved in water can be recovered by a 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). As a means for obtaining a solid CAD peptide, the means of production method (A) may be employed.
(A method for producing a CAD peptide having a molecular weight range of 40000 or more and 67000 or less)
As a method for producing a CAD peptide having a molecular weight range of 40000 or more and 67000 or less, there can be mentioned, for example, a method in which the hydrolysis step of the above production method (C) is omitted.
(Hair treatment agent)
The hair treatment agent according to the present embodiment is not particularly limited and includes hair care agents, permers, coloring agents, bleaching agents, and styling agents.
&Quot; Hair care agent " is a hair treatment agent used for hair care, care, and the like. Hair care agents include, for example, shampoos, rinses, conditioners, treatments (for example, non-washed treatments, washing treatments, hairdressing treatments, Treatments for post-treatment of perms, treatments for pretreatment of colorings, treatments for post-treatment of colorings, treatments for pretreatment of bleaches, treatments for post-treatment of bleaches) . &Quot; Pharmase " is a hair treatment agent used for changing the shape of hair using chemical reactions such as reduction reaction and oxidation reaction. Examples of the perming agent include a straightening agent for bringing the hair such as a wave form or a wave form for forming the hair into a wave shape close to the face of the user and a hair styling agent for forming a hair- The second agent containing the oxidizing agent of the first agent and the second agent is equivalent to the hair treating agent according to the present embodiment. &Quot; Coloring agent " is a hair treatment agent used for coloring hair. Examples of the coloring agent include a salt dye containing a direct dye, a hair dye containing a reactive dye required to react with the hair, and a hair coloring agent temporarily coloring the hair. &Quot; Bleach agent " is a hair treatment agent used to decolorize the pigment of hair. The " styling agent " is a hair treatment agent used to temporarily maintain the hair shape.
When the hair treatment agent is used, the formulations are not particularly limited, and examples thereof include liquid, oil, lotion, cream, wax, gel, solid, foam (foam) and aerosol.
If a CAD peptide is incorporated, it corresponds to the hair treatment agent of the present embodiment. For example, a hair treatment agent in which a CAD peptide is blended as a further blending raw material of a known hair treatment agent, and a hair treatment agent in which a CAD peptide is blended as an alternative raw material for a blending raw material of a known hair treatment agent corresponds to the hair treatment agent of the present embodiment .
Known raw materials other than the peptide compounded to the hair treatment agent may be appropriately selected according to the use of the hair treatment agent. The known hair treatment agent raw materials include anionic surfactants, cationic surfactants, amphoteric surfactants, nonionic surfactants, alcohols, polyhydric alcohols, sugars, oils, esters, fatty acids, hydrocarbons, lead, silicones, synthetic polymers, semi-synthetic polymers Compounds, and natural polymer compounds. Other known hair treatment agent raw materials include proteins, amino acids, plant and animal extracts, microbial derivatives, inorganic compounds, fragrances, preservatives, sequestering agents, ultraviolet absorbers, pigments, reducing agents, oxidizing agents, dyes and pigments.
Examples of the anionic surfactant include fatty acid salts, alkyl ether carboxylates, fatty acid amide ether carboxylates, fatty acid amide ether carboxylic acids, acyl lactic acid salts, alkane sulfonic acid salts,? -Olefin sulfonic acid salts,? -Sulfo fatty acid methyl ester Alkyl sulfosuccinates, alkyl sulfosuccinates, alkylbenzenesulfonates, alkylnaphthalenesulfonates, N-acylmethyltaurines, alkylsulfates, alkyl ether sulfates, alkyl sulfates, alkyl sulfosuccinates, Alkyl aryl ether sulfates, fatty acid alkanol amide sulfates, fatty acid monoglyceride sulfates, alkyl phosphates, polyoxyethylene alkyl ether phosphates, alkyl aryl ether phosphates, and fatty acid amide ether phosphates. The compounding concentration of the anionic surfactant is appropriately set depending on the use of the hair treatment agent, and is, for example, from 0.1 mass% to 20 mass%.
Examples of the cationic surfactant include an alkylamine salt, a fatty acid amide amine salt, an ester-containing tertiary amine salt, an achorbic tertiary amine salt, a long-chain alkyltrimethylammonium salt, a di long-chain alkyldimethylammonium salt, Quaternary quaternary ammonium salts, and monoalkyl ether quaternary ammonium salts. The compounding concentration of the cationic surfactant is appropriately set depending on the use of the hair treatment agent, and is, for example, from 0.1 mass% to 20 mass%.
Examples of the amphoteric surfactant include alkyl glycine salts, carboxymethyl glycine salts, N-acylaminoethyl-N-2-hydroxyethyl glycine salts, alkylpolyaminopolycarboxy glycine salts, alkylaminopropionates, alkyliminodipropionates , N-acylaminoethyl-N-2-hydroxyethylpropionate, alkyldimethylaminoacetic acid betaine, fatty acid amidepropyldimethylaminoacetic acid betaine, alkyldihydroxyethylaminoacetic acid betaine, (2-hydroxypropyl) sulfonate, N-alkyl-N, N-dimethylammonium-N- -Hydroxypropyl) sulfonic acid salt. The compounding concentration of the amphoteric surfactant is suitably set depending on the use of the hair treatment agent, and is, for example, from 0.1 mass% to 10 mass%.
Examples of the nonionic surfactant include polyoxyethylene alkyl ethers, polyoxyethylene polyoxypropylene alkyl ethers, polyoxyethylene fatty acid esters, polyoxyethylene sorbitan fatty acid esters, polyoxyethylene sorbitol tetra fatty acid esters, glycerin fatty acid esters, Sorbitan fatty acid esters, polyglycerin fatty acid esters, and sucrose fatty acid esters. The compounding concentration of the nonionic surfactant is appropriately set depending on the use of the hair treatment agent, and is, for example, from 0.1 mass% to 20 mass%.
Examples of the alcohol include alcohols such as butyl alcohol, lauryl alcohol, myristyl alcohol, cetanol, stearyl alcohol, behenyl alcohol, oleyl alcohol, isopropanol, octyldodecanol, isostearyl alcohol, hexyl decanol, Cholesterol, and phytosterol. The compounding concentration of the alcohol is appropriately set depending on the use of the hair treatment agent, and is, for example, 1% by mass or more and 50% by mass or less.
Examples of polyhydric alcohols 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.
The saccharides include, for example, sorbitol, mannitol, glucose, fructose, xylitol, lactose, maltose, maltitol and trehalose. The compounding concentration of the saccharide is suitably set depending on the use of the hair treatment agent, and is, for example, from 0.1 mass% to 10 mass%.
Examples of the preservative include almond oil, avocado oil, olive oil, shea butter oil, evening primrose oil, camellia oil, peanut oil and rosehip oil. The blending concentration of the oil is appropriately set according to the use of the hair treatment agent, and is, for example, from 0.1 mass% to 10 mass%.
Examples of the ester oils include ethyl oleate, isopropyl myristate, isopropyl propyl palmitate, butyl butyl stearate, palmitoyl myristate, myristyl myristate, myristyl octyldodecyl isostearate, isopropyl myristate Propyleneglycol propyleneglycol, propyleneglycol propyleneglycol, triethyleneglycol propyleneglycol, propyleneglycol propyleneglycol, propyleneglycol propyleneglycol, propyleneglycol propyleneglycol, propyleneglycol propyleneglycol, Trimethylolpropane isostearate, pentaerythritol tetra-2-ethylhexanoate, isostearyl isostearate, 2-octyldodecyl dimethyloctanoate, myristyl lactate, trioctyldodecyl citrate, diisostearyl malate, di 2-ethylhexyl, diisobutyl adipate, and cholesteryl stearate. The compounding concentration of the ester oil is suitably set depending on the use of the hair treatment agent, and is, for example, from 0.1 mass% to 10 mass%.
Examples of the fatty acid include isostearic acid, oleic acid, capric acid, stearic acid, palmitic acid, hydroxystearic acid, behenic acid, myristic acid, lauric acid, lanolin fatty acid and linoleic acid. The compounding concentration of the fatty acid is suitably set depending on the use of the hair treatment agent, and is, for example, from 0.1 mass% to 10 mass%.
Examples of the hydrocarbons include liquid paraffin, squalane, pristane, ozokerite, paraffin, ceresin, petrolatum and microcrystalline wax. The compounding concentration of the hydrocarbons is appropriately set according to the use of the hair treatment agent, and is, for example, from 0.1 mass% to 20 mass%.
Examples of the lead include beeswax, wood wax, candelilla lead, and carnauba wax. The compounding concentration of lead is appropriately set depending on the use of the hair treating agent, and is, for example, from 0.1 mass% to 20 mass%.
Examples of the silicone include dimethyl silicone, methylphenyl silicone, cyclic dimethyl silicone, alcohol denatured silicone, alkyl denatured silicone and amino denatured silicone. The compounding concentration of silicon is appropriately set depending on the use of the hair treatment agent, and is, for example, from 0.1 mass% to 50 mass%.
Examples of the synthetic polymer compound include carboxyvinyl polymer, polyvinyl alcohol, polyvinylpyrrolidone, polyacrylic acid, and methacryloylethylbetaine methacrylate ester copolymer. Examples of the semisynthetic polymer compound include methylcellulose, hydroxyethylcellulose, hydroxypropylcellulose, carboxymethylcellulose, soluble starch, and the like. Examples of natural polymers include sodium alginate, guar gum, glucan, cellulose, and sodium hyaluronate. The compounding concentration of the synthetic high molecular compound, semisynthetic high molecular compound and natural high molecular compound is suitably set depending on the use of the hair treating agent, and is, for example, from 0.1 mass% to 15 mass%.
As described above, the hair treatment agent of the present embodiment can be compounded with a CAD peptide and a well-known raw material for hair treatment agent suitably selected. Examples of combinations of raw materials to be compounded with CAD peptides are as follows. Examples of the combination of raw materials for the hair care agent include surfactants, silicones, polymer compounds (synthetic high molecular compounds, semisynthetic high molecular compounds or natural high molecular compounds), alcohols, sequestering agents and water. Examples of the combination of raw materials of the pharmacological agent include a reducing agent (thioglycolic acid, cysteine, acetylcysteine, cysteamine, etc.), an alkaline agent (ammonia, monoethanolamine, ammonium hydrogen carbonate, arginine Etc.) and water, and an oxidizing agent (bromate, hydrogen peroxide, etc.) and water mixed as a second agent for perm. Examples of the combination of raw materials for the coloring agent include dyes, alcohols, high molecular compounds (synthetic high molecular compounds, semi-synthetic high molecular compounds or natural high molecular compounds), and water. The combination of raw materials of the bleaching agent is, for example, hydrogen peroxide, a surfactant, an alkaline agent and water. Examples of the combination of the raw materials of the styling agent include raw materials for styling (oils, esters, hydrocarbons, lead, synthetic high molecular compounds, semisynthetic high molecular compounds, natural high molecular compounds, etc.), surfactants and alcohols.
As a raw material to be blended in the hair treatment agent of the present embodiment, those 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 are suitably used.
-SS- (CH 2 ) n COO- (I)
(In the formula (I), n is 1 or 2.)
The solvent is not particularly limited, and for example, water, ethanol and the like are used. The content of the peptide in the hair treatment agent raw material is not particularly limited, but is, for example, 0.1% by mass or more and 10.0% by mass or less.
The peptide to be dissolved in the solvent is, for example, one having a molecular weight in a range of less than 40,000, and a molecular weight in a range of from 40000 to 67000.
(Example)
EXAMPLES The present invention will be described in more detail with reference to the following examples. However, the present invention is not limited to the following examples without departing from the gist of the present invention.
The CAD peptides (1a), (1b), (2a) and (2b) having a molecular weight range of less than 40000 and the CAD peptides (3) having a molecular weight range of 40000 or more and 67000 or less used in the hair treatment agent of the examples are as follows. In addition, CAD peptides (1a), (1b), (2a) and (2b) have hair permeability, but CAD peptide (3) is considered to have no hair permeability.
(CAD peptide (1a))
The CAD peptide (1a) was produced according to the following reduction step, denaturation step and hydrolysis step.
[Reduction process]
The wool of Merino wool, washed and dried with a neutral detergent, was cut to about 5 mm. 5.0 parts by mass of the wool, 15.4 parts by mass of a 30% by mass aqueous sodium thioglycolate solution and 8.5 parts by mass of a 6mol / L sodium hydroxide aqueous solution were mixed and further mixed with water to prepare a mixed solution having a total amount of 150 parts by mass and a pH of 11. The resulting mixture was stirred at 45 DEG C for 1 hour. Next, water was further mixed to make the total amount to 200 parts by mass, and the mixture was allowed to stand at 45 DEG C for 2 hours. Thereafter, the mixture was naturally cooled until the liquid temperature reached room temperature.
[Denaturation process]
While stirring the mixed solution after the reduction process, 25 parts by mass of an aqueous solution containing 2.05 parts by mass of sodium bromate was added to the mixed solution over about 60 minutes. Thereafter, stirring of the mixed solution was continued at all times, and 100 parts by mass of an aqueous solution containing 7.08 parts by mass of citric acid mixed with the mixed solution was mixed over about 85 minutes. The pH of the solution after mixing citric acid was 7.
[Hydrolysis Process]
100 parts by mass of a solid portion separated by filtration from the mixed solution after the treatment in the denaturation step, 1 part by mass of a 3% by mass protease aqueous solution ("Protease A" manufactured by Daiwa Kagaku Co., Ltd.) Sodium hydrogencarbonate and water were mixed, and the hydrolysis reaction was conducted for 20 minutes in water at 50 ° C. Thereafter, proteolytic enzyme was inactivated under the condition of 80 DEG C for 5 minutes. After that, an aqueous solution of CAD peptide (1a) was obtained by filtration.
The molecular weight of the CAD peptide (1a) was analyzed and found to be within the range of approximately 1000 to 3600 (1 kDa to 3.6 kDa). In the molecular weight analysis of CAD peptide (1a), "AXIMA Performance" manufactured by Shimadzu Seisakusho Co., Ltd. was used as a laser ionization time-of-flight type mass spectrometer (MALDI-TOFMS) Linear, and the detected ions were positive. The matrix was prepared by adding 5 mg of? -Cyano-4-hydroxycinnamic acid (CHCA) to 1 mL of an aqueous solution containing 0.1% by weight of tetrafluoroacetic acid and 50% by weight of acetonitrile. FIG. 3 is a chart showing the results of MALDI-TOFMS analysis of CAD peptide (1a), with the top being a matrix only chart and the bottom being a chart containing CAD peptide (1a) in the matrix. The molecular weight of the CAD peptide (1a) was found to be within the range of approximately 1000 to 3600 (1 kDa to 3.6 kDa) as shown in Fig.
(CAD peptide (1b))
A CAD peptide (1b) having a smaller molecular weight than 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 preparation of CAD peptide (1b) is as follows.
[Hydrolysis Process]
100 parts by mass of a solid portion separated by filtration from the mixed solution after the treatment in the denaturation step, 1 part by mass of a 3% by mass protease aqueous solution ("Protease A" manufactured by Daiwa Kagaku Co., Ltd.) Sodium hydrogencarbonate and water were mixed, and the hydrolysis reaction was conducted for 20 minutes in water at 50 ° C. Thereafter, proteolytic enzyme was inactivated under the condition of 80 DEG C for 5 minutes. Then, 1 mass part of a 3 mass% protease aqueous solution ("Proteizer A" manufactured by Daiwa Kagaku Co., Ltd.) was mixed and subjected to a hydrolysis reaction at 50 ° C for 20 min. To inactivate the proteolytic enzyme. Thereafter, an aqueous solution of CAD peptide (Ib) 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 production of the CAD peptide (1a) except that the modification step was changed. The denaturation step in the production of the CAD peptide (2a) is as follows.
[Denaturation process]
An aqueous acetic acid solution (165 parts by mass of an aqueous solution containing 7 parts by mass of acetic acid) was mixed while stirring the mixed solution after the reduction process, so that the pH of the keratin mixed solution gradually increased from 11 to 10. With regard to the mixing of hydrogen peroxide, 36 parts by mass of an aqueous solution obtained by mixing 3 parts by mass of 35 mass% aqueous hydrogen peroxide solution with stirring was carried out over about 30 minutes with stirring. After the start of the mixing of the hydrogen peroxide, the mixed solution was stirred at all times, and an aqueous acetic acid solution was mixed so that the pH was maintained at 10 or more and 11 or less. After completion of the mixing of hydrogen peroxide, about 10 parts by mass of an aqueous acetic acid solution was gradually mixed over about 5 minutes to adjust the pH of the mixture gradually to 10 to 7. [
(CAD peptide (2b))
As a modification step, a CAD peptide aqueous solution was obtained in the same manner as the CAD peptide (Ib) except that the modification step in the production of the CAD peptide (2a) was employed. Using this semipermeable membrane as the aqueous solution, an aqueous solution of CAD peptide (2b) having a molecular weight range of 1,000 or less was obtained. The semi-permeable membrane used for obtaining the CAD peptide (2b) is "spectra / por" manufactured by Spectrum, which has a fractional molecular weight of 1000, a flat width of 10 mm and a diameter of 6.4 mm.
(CAD peptide (3))
The liquid portion separated by filtration from the mixed solution after the denaturation 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 SDS-PAGE using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) using "Protein Molecular Weight Marker (Low)" manufactured by Takara Bio as a molecular weight marker. (3) had a molecular weight range of 40,000 to 67,000 (40 kDa to 67 kDa).
The molecular weight of this CAD peptide (3) was confirmed by Sodium Dodecyl Sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The molecular weight band identification method by the sodium dodecyl sulfate-polyacrylamide gel electrophoresis method (SDS-PAGE method) will be described in detail below.
(1) Molecular weight marker
Protein Molecular Weight Marker (Low) manufactured by Takara Bio Co., Ltd.
Details of the standard substances are as follows: Phosphorylase B (molecular weight 97200), Serum Albumin (molecular weight 66409), Ovalbumin (molecular weight 44287), Carbonic anhydrase (molecular weight 29000), Trypsin inhibitor (molecular weight 20100), Lysozyme
(2) Polyacrylamide gel
A concentrate gel concentration of 4.5% by mass, and a separation gel concentration of 10.0% by mass
(3) Sample solution
1 part by mass of CAD peptide or reference substance
Bromophenol blue qs
Sample solvent 1 part by mass
(Sample solvent: 1% by mass of sodium dodecyl sulfate, 1% by mass of 2-mercaptoethanol, 10 mM of tris hydrochloride (pH 6.8), 10% by mass of glycerol)
(4) Electrophoresis conditions
40 mA, 30 minutes
(5) buffer solution
A 10-fold diluted aqueous solution of " 10x (Tris / Glycine / SDS) Buffer &
(6) Dyeing condition
After staining with Kumasi Brilliant Blue solution for 1 hour, decolorization treatment with decolorant for about 6 hours
(7) Analysis result
FIG. 4 shows an electrophoresis gel photograph of the CAD peptide (3) subjected to the treatment under the above conditions (1) to (6) and the molecular weight marker. A graph of 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 is shown in FIG. 5 is calculated from the molecular weight marker spot of this graph and the molecular weight based on the distance from the predetermined position of the band of the
As in the latter case, the hair was treated according to the hair treatment agent of Example 1a or the hair treatment agent of Example 1b. The initial elastic modulus and the breaking strength of the untreated hair and the treated hair were measured.
(Example 1a)
A 3 mass% aqueous solution of CAD peptide (1a) was prepared as the hair treatment agent of Example 1a.
(Example 1b)
A 3% by mass aqueous solution of CAD peptide (3) was prepared as the hair treatment agent of Example 1b.
(Hair treatment 1)
The hair of Example 1 or Example 1b was dipped in the hair treatment agent for 10 minutes, and the hair was washed with hot air after drying.
The hair sample 1 in the present hair treatment 1 was obtained by treating the black hair of the straight hair as follows. The straight black hair was treated in the order of bleaching, perming, coloring, tanning, coloring, tanning, perming, coloring, tanning, coloring, tanning and drying.
In the bleaching treatment, the first agent and the second agent of "ProMatis Plebead" manufactured by Milbon KK were mixed at a ratio of about 1 part by mass: about 2 parts by mass, and the mixture was applied to the hair. The application amount was set to twice the hair mass. The coated hair was covered with a film, washed with shampoo after 15 minutes, and dried with warm air.
In the above-mentioned perming treatment, the hair wound on the perming rod having a diameter of 12 mm was immersed in a first agent of "Frezoom C / T" manufactured by Mitsubishi Kagaku for 10 minutes, Soaked, and washed with water. Thereafter, the hair was dried with warm air.
In the above-described color processing, the first agent and the second agent of "Ordib" manufactured by Milbon KK were mixed at a ratio of about 1 part by mass: 1 part by mass, and this was applied to the hair. The applied amount was 10 times the mass of the hair, and after the application, it was left for 10 minutes.
In the hair treatment, the hair was shampooed, treated and warm-air dried were changed to one cycle, and 60 cycles of the shampoo, treatment and warm air drying were performed. In the shampoo, shampoo ("Lux Super Riche Shine" manufactured by UniRiver Co., Ltd.) having a mass of 5 times the hair sample 1 was applied to the hair and left for 3 minutes, followed by washing with water. In the treatment, 5-fold mass of the treatment of hair sample 1 ("Lux Super Riche Shine" manufactured by Uni-River Co., Ltd.) was applied to the hair and allowed to stand for 3 minutes and then washed with water.
(Initial elastic modulus, breaking strength)
TENSILON UTM-II-20 " manufactured by Orientec Co., Ltd., and the initial elastic modulus and breaking strength per unit area were measured. Before the measurement, the hair sample 1 was immersed in water for 24 hours. At the time of measurement, the hair sample 1 was immersed in water, the temperature was 25 ° C, the tensile speed was 2 mm / min, and the tensile interval of the hair sample 1 was 20 mm.
The following Table 1 shows the initial elastic modulus and breaking strength results for the hair treated with the hair treatment 1 and the untreated hair. In Table 1, the " measurement average value " is an average value of five times of measurement, and the " rate of change " is based on untreated hair.
As shown in Table 1, in Example 1a containing the CAD peptide (1a) having a molecular weight range of 1000 to 3600, the rate of change of the initial elastic modulus and the breaking strength showed a positive value, and the CAD peptide (1a) Which is suitable for improving the initial elastic modulus and breaking strength of the hair. In Example 1b in which the CAD peptide (3) having a molecular weight range of 40000 to 67000 was blended, the change rate of the initial elastic modulus showed a positive value, confirming that the CAD peptide (3) was suitable for improving the initial modulus of elasticity. In addition, the initial elastic modulus results of Examples 1a and 1b indicate that the CAD peptide is suitable for improving the initial elastic modulus of hair or inhibiting deterioration of hair.
(Example 2a)
A 5 mass% aqueous solution of CAD peptide (2a) was prepared as the hair treatment agent of Example 2a.
(Example 2b)
A 5 mass% aqueous solution of CAD peptide (2b) was prepared as the hair treatment agent of Example 2b.
The hair was treated according to the later hair treatment 2a using the hair treatment agent of Example 2a or the hair treatment agent of Example 2b. The initial elastic modulus, breaking strength and elongation of the untreated hair and the hair after the treatment were measured, and the distance between microfibrils (IF: intermediate filament) was also calculated.
(Hair treatment 2a)
Black hair was collected from a female in their twenties, immersed in an aqueous 3% by mass sodium lauryl sulfate solution for 3 minutes, rinsed with water, and the hair was wiped off and dried to prepare a hair sample 2. One part by mass of the hair sample 2 was subjected to the following reduction treatment, cation treatment, treatment with the hair treatment agent of Example 2a or Example 2b, and oxidation treatment. In the reducing treatment, 1 part by mass of Hair Sample 2 was immersed in 30 parts by mass of a 3 mass% thioglycolic acid aqueous solution (adjusted to pH 9.3 with monoethanolamine) at 45 DEG C for 10 minutes, and then washed with hot water for 1 minute And wiped off the water. In the cation treatment, 1 part by mass of hair sample 2 was immersed in a 0.1 mass% aqueous solution of 30 parts by mass of dimethyldiallylammonium chloride-acrylic acid copolymer ("MERQUAT 550" manufactured by Narco Japan Co., Ltd.) for 10 minutes and then the surface moisture of hair sample 2 I wiped it off. In the treatment with the hair treatment agent of Example 2a or 2b, 1 part by mass of the hair sample 2 was immersed in 30 parts by mass of the hair treatment agent of Example 2a or the hair treatment agent of Example 2b for 10 minutes, I wiped off the water. In the oxidation treatment, 1 part by mass of the hair sample 2 was immersed in 30 parts by mass of a 7 mass% aqueous solution of sodium bromate (adjusted to pH 7.2 with a phosphoric acid buffer solution) for 10 minutes, then the hair sample 2 was washed with water, It was wiped off and dried.
(Initial elastic modulus, breaking strength, elongation)
Initial elastic modulus and breaking strength were measured in the same manner as described above. The elongation was measured at the same time as the breaking strength.
(Distance between IFs)
Using a beamline BL40XU of the large synchrotron SPring-8, the X-ray microbeam was irradiated perpendicularly to the axis of the hair sample 2 and radially stepped from the outer periphery of the hair sample 2 to measure the equatorial reflection intensity near 9 nm The measurement was carried out in a humidity of 60% atmosphere, and the direct IF distance was directly obtained. Details of the measurement conditions are as follows.
X-ray wavelength: 0.083 nm (E = 15 keV)
Camera length: about 2000mm
Detector pixel size: 140.8 m / pixel x 140.8 m / pixel
Image size: 1344 pixels × 1024 pixels
Behen acid was calibrated at a cycle of 5.838 nm (primary).
Beam size: about 5μm
1st pinhole: 5μm
2nd pin hole: 200μm
Beam stop: φ8mm
Detector: Image Intensifier
The initial elastic modulus of the hair after the treatment of the hair treatment 2a and the like are shown in Table 2a. In Table 2a, the " measurement average value " is an average value of the measurement times ten times, and the " change rate " is based on the untreated hair. The " untreated " in Table 2a means that the cation treatment and the treatment with the hair treatment agent of Example 2a or Example 2b are omitted. The " inter-IF distance " is an average value of 800 samples.
In Table 2a, it can be seen that both the initial elastic modulus and breaking strength of Examples 2a and 2b were superior to untreated. In addition, the inter-IF distance in Example 2a was longer than the untreated inter IF distance, and it was expected that the CAD peptide 2a was deposited inside the hair after the hair treatment 2a.
The hair treatment agent of Example 2a or Example 2b was used and the hair was treated according to the latter hair treatment 2b. The initial elastic modulus, breaking strength and elongation of the untreated hair and the hair after the treatment were measured.
(Hair treatment 2b)
The same treatment as that of the hair treatment 2a except that the reduction treatment of the hair treatment 2a only differed from the following point was performed as the hair treatment 2b. In the reduction treatment of hair treatment 2b, an aqueous solution (adjusted to pH 9.3 with monoethanolamine) containing 9 mass% thioglycolic acid and 2 mass% dithiolgic acid was used instead of the 3 mass% aqueous solution of thioglycolic acid .
The initial elastic modulus of the hair after the treatment of the hair treatment 2b and the like are shown in Table 2b. The " measured average value ", " rate of change ", and " untreated " in Table 2b have the same meanings as those in Table 2a.
The shampoos of Examples 3a, 3b and 3 were prepared as described below, and the hair was treated according to
(Example 3a)
A hair treating agent of Example 3a was prepared by blending CAD Sesame S (Shampoo S) manufactured by Mylon Kogyo Kabushiki Kaisha with 2% by mass of CAD peptide (1a).
(Example 3b)
A hair treating agent of Example 3b was prepared by blending CAD S-peptide (3) so as to be 2% by mass in " Disesh Shampoo S "
(Comparative Example 3)
Disesh Shampoo S "manufactured by Mylon Corp. was used as the hair treating agent of Comparative Example 3.
(Hair treatment 3)
The hair treatment agent of Example 3a, Example 3b or Comparative Example 3 was subjected to shampooing treatment. Subsequently, the mother lambs were subjected to a treatment treatment by "Disesh Treatment SF" manufactured by Yilon Kogyo Co., and the mother lambs were subjected to hot air drying.
The feel of the hair treated according to
The hair treatment agents of Examples 4a, 4b, 4c and 4 were prepared as described below, and the hair was treated according to the
(Example 4a)
A 0.2 mass% aqueous solution of CAD peptide (1a) was prepared as the hair treatment agent of Example 4a.
(Example 4b)
A 0.2 mass% aqueous solution of CAD peptide (Ib) 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.
(Comparative Example 4)
Water was used as the hair treating agent of Comparative Example 4.
(Hair treatment 4)
The hair treatment agents of Example 4a, Example 4b, Example 4c or Comparative Example 4 were sprayed onto the hair, and the hair was dried by hot air.
The feel of the hair treated according to
(Example 5)
A shampoo containing 0.2% by mass of the CAD peptide (3) in the hair treating agent of the later-described Comparative Example 5 was used as the hair treating agent of Example 5.
(Comparative Example 5)
5% by mass of sodium polyoxyethylene lauryl ether sulfate, 4% by mass of triethanolamine laurylsulfate, 2% by mass of sodium polyoxyethylene lauryl etheracetate, 0.9% by mass of sodium lauroylmethyl-beta -alanine, 4% by mass of betaine, 3% by mass of coconut oil fatty acid diethanolamide, 0.1% by mass of coconut oil fatty acid monoethanolamide, 0.2% by mass of 1,3-butylene glycol and 0- [2-hydroxy- ) Propyl] A shampoo prepared by mixing 0.4% by mass of hydroxyethyl cellulose, 0.3% by mass of a chelating agent, 0.3% by mass of an antiseptic, 0.1% by mass of an antioxidant and 0.2% by mass of a perfume in water was used as the hair treating agent of Comparative Example 5.
(Reference Example 5)
A shampoo containing 0.2% by mass of a commercially available keratin in the hair treating agent of Comparative Example 5 was used as the hair treating agent of Reference Example 5. In this commercial keratin blend, an aqueous solution containing 5% by mass of keratin ("Keratec IFP-HMW" manufactured by Kuroda Japan K.K.) was used.
(Hair treatment 5)
And 3 g of bleached hair were combined to prepare a plurality of hair bundles each having a single hair bundle, and this was used as a hair bundle for evaluation. The hair treatment agent of Example 5, Comparative Example 5 or Reference Example 5 was applied, washed with water, applied with a treatment (hair treatment agent of the latter Comparative Example 6), washed with water and dried with hot air.
The feel of the hair treated according to
(Example 6)
A hair treatment agent of Example 6 was prepared by blending 0.2% by mass of CAD peptide (3) in the hair treatment agent of the later-described Comparative Example 6.
(Comparative Example 6)
2 mass% of cetyltrimethylammonium bromide, 3 mass% of alkyltrimethylammonium chloride, 0.8 mass% of ethanol, 0.7 mass% of isopropanol, 5 mass% of cetanol, 2 mass% of stearyl alcohol, 4 mass% of concentrated glycerin, , 0.5 mass% of ether, 1 mass% of 2-ethylhexanoate, 1 mass% of dipentaerythritol fatty acid ester, 0.3 mass% of squalane, 0.3 mass% of highly polymerized methylpolysiloxane, 0.2 mass% of dimethylsiloxane methylstearoxysiloxane copolymer, , 0.2% by mass of preservative, and 0.3% by mass of fragrance in water to prepare a hair treatment agent of Comparative Example 6.
(Reference Example 6)
A hair treatment agent of Reference Example 6 was prepared by adding 0.2% by mass of commercially available keratin to the hair treatment agent of Comparative Example 6. In the commercially available keratin blend herein, an aqueous solution containing 5% by mass of keratin ("Keratec IFP-HMW" manufactured by Kuroda Japan K.K.) was used.
(Hair treatment 6)
And 3 g of bleached hair were combined to prepare a plurality of hair bundles each having a single hair bundle, and this was used as a hair bundle for evaluation. The hair was treated with the application of shampoo (hair treatment agent of Comparative Example 5), washing with water, application of hair treatment agent of Example 6, Comparative Example 6 or Reference Example 6, washing with water, and drying with warm air.
The feel of the hair treated according to hair treatment 6 was evaluated by a professional evaluator on the basis of using the hair treatment agent of comparative example 6. [ The evaluation results are shown in Table 4 (the evaluation "-" in the table indicates that evaluation is not performed).
(Example 7)
A non-washed creamy phase treatment in which 0.2% by mass of CAD peptide (3) was blended with the hair treatment agent of the later-described Comparative Example 7 was used as the hair treatment agent of Example 7. Here, in the compounding of the CAD peptide (3), a 4 mass% aqueous solution of CAD peptide (3) adjusted to pH 8.72 using arginine was used.
(Comparative Example 7)
0.8 mass% of stearyltrimethylammonium chloride, 0.2 mass% of isopropanol, 3 mass% of cetanol, 0.8 mass% of behenyl alcohol, 0.02 mass% of propylene glycol, 2 mass% of dipropylene glycol, 0.4 mass% of soft lanolin fatty acid cholesteryl, 2 mass% of cedar butter, 0.06 mass% of hydroxyethyl cellulose, 0.2 mass% of tamarind seed gum, 1 mass% dimethiconol, 16 mass% of decamethylcyclopentasiloxane, 2 mass% of methylpolysiloxane, 0.2 mass of crosslinked methylpolysiloxane , 2% by mass of amino-modified silicone, 0.1% by mass of highly polymerized dimethylsiloxane-methyl (aminopropyl) siloxane copolymer, 0.5% by mass of cocamidopropyl dimethyl ammonium hydroxypropyloxypropylsiloxane-methylpolysiloxane copolymer acetate, 0.03% by mass of amide · 2- (acryloyloxy) ethyltrimethylammonium chloride copolymer, 0.05% by mass of antioxidant, 0.2% by mass of preservative and 0.2% by mass of fragrance were added to water As was washed to the cream that the treatment agent of the hair treatment of Comparative Example 7 was prepared.
(Reference Example 7)
A non-washed creamy phase treatment in which 0.2% by mass of a commercially available keratin was blended in the hair treating agent of Comparative Example 7 was used as the hair treating agent of Reference Example 7. In this commercial keratin blend, an aqueous solution containing 5% by mass of keratin ("Keratec IFP-HMW" manufactured by Kuroda Japan K.K.) was used.
(Hair treatment 7)
After applying the hair treatment agents of Example 7, Comparative Example 7 or Reference Example 7 to the hair of the pharynx, the sensory evaluation of the order of the thickness feeling was carried out. In addition, it was applied to the hair of the wig, and the same evaluation was made.
Table 5 shows the evaluation results of the thickness. From the results in Table 5, it was found that the cream of Example 7 containing CAD peptide (3) had a larger thickness feeling as compared with the cream of Comparative Example 7 in which neither CAD peptide (3) nor keratin was blended.
(Example 8)
A cream phase treatment in which 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 were mixed with water was applied to the hair treatment Zero.
(Reference Example 8)
2% by mass of cetyltrimethylammonium bromide, 0.05% by mass of stearyltrimethylammonium chloride, 0.08% by mass of dicocoyldimethylammonium chloride, 0.01% by mass of polyoxyethylene cetyl ether (20EO.O), 1% by mass of ethanol, By mass of aminoethylaminopropylsiloxane-dimethylsiloxane copolymer, 2% by mass of highly polymerized dimethylsiloxane, 1% by mass of aminoethylaminopropylsiloxane-dimethylsiloxane copolymer, 0.01% by mass of ethylaminopropylethyldimethylammonium ethylsulfate lanolin fatty acid, A cream phase treatment in which 0.3 mass% of a perfume was blended in water was used as the hair treatment agent of Reference Example 8. [
(Hair treatment 8a)
The hair treating agent of Example 8 or Reference Example 8 was applied to the hair, washed with water and dried by hot air.
(Hair treatment 8b)
The hair treatment agent of Example 8 was applied to the hair, and the hair treatment agent of Reference Example 8 was overlaid on the hair. Thereafter, the mother lambs were washed with water and dried by hot air.
Expert evaluators evaluated the texture of the hair treated according to hair treatment 8a and hair treatment 8b. The evaluation results are shown in Table 6.
(Example 9)
, 10 parts by mass of 1% by mass of CAD peptide (3) in Resin 1 and 9-AB manufactured by Yumec Corp., and 10 parts by mass of "Resident 2 (Oxidant 3.0) Was used as the hair treating agent of Example 9.
(Hair treatment 9)
The mother liquor was treated with the hair treatment agent of Example 9.
The feel of the hair treated according to hair treatment 9 was evaluated by a professional evaluator. As a result of evaluation, the hair treated with the hair treatment agent of Example 9 passed through the fingers well at the time of hair firing.
(Example 10)
A hair treatment agent of Example 10 was prepared by adding 0.5% by mass of CAD peptide (3) to "Frezoom C / T first agent" available from Yumemoto Co., Ltd. (first agent of the formula 2).
(Comparative Example 10)
A sample obtained by adding no CAD peptide (3) of Example 10, that is, a "Frazoom C / T first agent" manufactured by Milburn, was used as a hair treatment agent of Comparative Example 10.
(Hair treatment 10)
The hair treatment agent of Example 10 or Comparative Example 10 was applied to the hair, allowed to stand for 15 minutes, rinsed with water, and wiped off with a towel. Next, a "Frezoom C / T second agent" manufactured by Yilon Kogyo Co., Ltd. was applied, left for 5 minutes, washed with water, and further coated with "Dises noi Wylorux Treatment" The mother lambs were warm-air dried.
The feel of the hair treated according to
As described above, the hair treatment agent of the present invention is suitable for hair treatment for business use or domestic use since it is effective for improving or deteriorating the initial elastic modulus and breaking strength of damaged hair.
Claims (13)
A hair care agent characterized by containing a peptide having a group having a unit represented by the following formula (I) as a side chain group (provided that a hair care agent containing a reducing agent is excluded).
-SS- (CH 2 ) n COO- (I)
(In the formula (I), n is 1 or 2.)
Applications Claiming Priority (7)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP2009141704A JP5558034B2 (en) | 2009-06-12 | 2009-06-12 | Hair care agent and hair treatment method |
| JPJP-P-2009-141704 | 2009-06-12 | ||
| JP2010005357A JP2011144127A (en) | 2010-01-13 | 2010-01-13 | Hair-treating agent and raw material for hair-treating agent |
| JPJP-P-2010-005356 | 2010-01-13 | ||
| JPJP-P-2010-005357 | 2010-01-13 | ||
| JP2010005356A JP5611603B2 (en) | 2010-01-13 | 2010-01-13 | Hair treatment agent and raw material for hair treatment agent |
| PCT/JP2010/057724 WO2010143484A1 (en) | 2009-06-12 | 2010-04-30 | Hair treatment agent and starting material for hair treatment agent |
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| KR20120046108A KR20120046108A (en) | 2012-05-09 |
| KR101951923B1 true KR101951923B1 (en) | 2019-02-25 |
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| KR1020117029136A KR101951923B1 (en) | 2009-06-12 | 2010-04-30 | Hair treatment agent and starting material for hair treatment agent |
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| KR (1) | KR101951923B1 (en) |
| CN (1) | CN102458352A (en) |
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| WO (1) | WO2010143484A1 (en) |
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| JP5795485B2 (en) * | 2011-04-19 | 2015-10-14 | 株式会社ミルボン | Hair treatment agent |
| TWI806100B (en) * | 2021-07-16 | 2023-06-21 | 財團法人工業技術研究院 | Biological hair shape change composition and kit, and method for changing hair shape |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2009153923A1 (en) | 2008-06-16 | 2009-12-23 | 茨城県 | Process for producing soluble feather keratin protein |
| JP2010132595A (en) | 2008-12-04 | 2010-06-17 | Nicca Chemical Co Ltd | Hair-treating agent having effect of protecting hair, and damage prevention and hair restoration |
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH07126296A (en) * | 1993-05-24 | 1995-05-16 | Kao Corp | Solubilized protein |
| JP4194669B2 (en) * | 1995-10-20 | 2008-12-10 | 花王株式会社 | Hair treatment agent |
| JP5411655B2 (en) * | 2008-12-03 | 2014-02-12 | 株式会社ミルボン | Hair treatment method and hair treatment agent |
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2010
- 2010-04-30 TW TW099114015A patent/TWI523664B/en active
- 2010-04-30 WO PCT/JP2010/057724 patent/WO2010143484A1/en active Application Filing
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Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2009153923A1 (en) | 2008-06-16 | 2009-12-23 | 茨城県 | Process for producing soluble feather keratin protein |
| JP2010132595A (en) | 2008-12-04 | 2010-06-17 | Nicca Chemical Co Ltd | Hair-treating agent having effect of protecting hair, and damage prevention and hair restoration |
Non-Patent Citations (1)
| Title |
|---|
| Fiber Preprints, Japan, Vol64, No, 1. pp67.* |
Also Published As
| Publication number | Publication date |
|---|---|
| CN102458352A (en) | 2012-05-16 |
| TWI523664B (en) | 2016-03-01 |
| WO2010143484A1 (en) | 2010-12-16 |
| TW201105355A (en) | 2011-02-16 |
| KR20120046108A (en) | 2012-05-09 |
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