JP7281172B2 - cosmetics - Google Patents

Description

TECHNICAL FIELD The present invention relates to a cosmetic, and more particularly to a cosmetic that is excellent in adhesion to the application site and capable of improving, protecting or repairing the function and characteristics of the application site.

Cosmetics are sometimes used not only to make the appearance beautiful, but also to protect the application site, or to improve or repair the function/characteristics of the application site. Protein is conventionally known as one of the ingredients contained in such cosmetics. It is known that proteins are easily compatible with hair and skin, and are effective in moisturizing the skin and hair, improving texture, and preventing rough skin.

For example, keratin, known as the protein that makes up hair and skin, is important for maintaining the structure of skin and hair. Keratin gives strength, body, and suppleness to fine, long hair. Keratin also provides the skin with a barrier function that protects the body from dryness and various stimuli. Collagen has a high water-retaining power, moisturizes the hair and skin, and maintains it, thereby providing homeostasis such as biological functions and metabolism. Silk protein contains a good balance of hydrophobic and hydrophilic amino acids, and coats the surface of hair and skin to improve slipperiness, giving the hair a texture that is easy to comb with fingers and a smooth texture to the skin. Are known.

Proteins exhibit various physical properties depending on their origin and composition of amino acids. There are also many proteins that are insoluble in water, such as keratin and silk. Keratin, among proteins used in cosmetics, is particularly difficult to dissolve in water. One of the reasons for this is that the amino acid composition of keratin contains a large amount of cysteine, and this cysteine forms cross-links by disulfide bonds between molecules and within molecules.

Conventionally, when water-insoluble proteins such as keratin are used in cosmetics, they are solubilized in water by hydrolysis or denaturation of the proteins. A protein having many disulfide bonds such as keratin is usually solubilized by cleaving the disulfide bonds by reducing the disulfide bonds to thiol groups (--SH) or derivatives thereof. For example, Patent Document 1 describes a hair care agent containing a peptide having —SS—(CH ₂ ) _n COO ^— as a side chain group. Patent Document 2 describes a solubilized protein obtained by reducing the disulfide bonds of a water-insoluble protein to thiol groups and converting some or all of them to carboxymethyl disulfide groups (-SSCH ₂ COOH). ing.

JP 2010-285401 A JP-A-7-126296

However, the components of cosmetics are required to have excellent adhesion on the application site (for example, skin and hair). On the other hand, the solubilized protein described in Patent Document 2 has —COOH in the side chain. Although such solubilized proteins have improved water solubility, they have the problem of being difficult to adhere to hair.

As one method for improving the water solubility of proteins, a method of reducing the molecular weight of proteins by hydrolysis is also used. However, the low-molecular-weight protein obtained by this method has a problem that it has weak covering properties on hair and skin and is easily washed away by washing or the like.

An object of the present invention is to provide a cosmetic that is excellent in adhesion to the application site and capable of improving, protecting or repairing the functions and properties of the application site.

The cosmetic of the present invention (hereinafter referred to as "this cosmetic") is a protein (hereinafter referred to as "this cosmetic") in which amidinocysteine is added to some or all of the _NH2 groups, OH groups, and SH groups of amino acids that constitute proteins (hereinafter referred to as "this cosmetic"). , referred to as "additional proteins").

Since the cosmetic of the present invention contains additional proteins and has excellent adhesion to the application site such as skin and hair, it can protect or repair the application site, or improve the function or properties of the application site.

The type, origin and structure of the protein are not particularly limited. A water-soluble or solubilized protein is preferable as the protein for incorporation into cosmetics. Specific examples of the protein include keratin, collagen, silk protein, and soybean protein.

As the protein, a purified/isolated protein may be used, or a natural component containing the protein may be used. The natural ingredients include, for example, human and bird hair (human hair, wool, feathers) containing keratin, horns and nails, scales, skins, bones and cartilage of animals and fish containing collagen, and silkworms containing silk protein. Cocoons, as well as soybean seeds containing soy protein. The hair of humans and birds and animals contains a large proportion of hydrophobic amino acids among the amino acids that constitute proteins, even when the hair is solubilized in water by hydrolysis or protein denaturation. Therefore, keratin derived from human and bird or animal hair is preferred because it has superior adhesion to hair and skin than other proteins, and keratin derived from wool or bird feathers or feathers is more preferred.

The structure of amidinocysteine is shown in formula (1). Amidinocysteine usually has a strongly basic amidino group that is cationized in the pH range of many cosmetics and a carboxyl group that contributes to the electrolyte becoming water soluble over a wide pH range.

In the added protein, amidinocysteine is added to some or all of the _NH2 groups, OH groups, and SH groups of the amino acids that constitute the protein. The added protein has high water solubility and cationicity due to the addition of amidinocysteine having an amidino group having a strong cationizing ability in the molecule, and has excellent adhesion to skin, hair, and the like. The degree of addition is not particularly limited. One molecule or two or more molecules of amidinocysteine may be added to the protein molecule.

There is no particular limitation on the specific embodiment and method of adding amidinocysteine to the protein. Amidinocysteine is usually added to the protein by reacting with _NH2 , OH and SH groups in the protein and forming amide, ester and thioester bonds. Alternatively, amidinocysteine may be added to the protein by forming a disulfide bond between the SH group of the protein and the SH group of amidinocysteine. Formation of the disulfide bond may be performed by reacting an SH group generated after reduction of a cystine bond (a disulfide bond between intermolecular or intramolecular cysteines) in the protein with amidinocysteine.

A reducing agent is usually used to reduce the cystine bond in the protein. The type of the reducing agent is not particularly limited as long as it can reduce the cystine bond. As the reducing agent, known reducing agents, for example, thiol compounds such as thioglycolic acid, cysteine, cysteamine, mercaptoethanol, thiolactic acid, thiourea or salts thereof, sulfurous acid, pyrosulfite or salts thereof, etc. can be used. .

Depending on the amount of amidinocysteine and other reaction conditions, part of the disulfide bond in the protein may be directly converted by the thiol group of amidinocysteine and added to one side of the disulfide bond (see formula (2)). Such additions are also included in the aforementioned "additions". In the following formula (2), "Cys" means a cysteine residue contained in the protein, and "R-SH" means amidinocysteine.

Cys-SS-Cys + R-SH
→ Cys-SSR + Cys-SH (2)

The protein and the additional protein may be subjected to other treatments as necessary. For example, the protein and/or the additional protein may be subjected to enzymatic, acid or alkaline hydrolysis to reduce molecular weight and size. In addition, the protein may be solubilized by conventionally known hydrolysis, protein denaturation, or the like, in order to increase water solubility. Furthermore, after obtaining the added protein, other components or insoluble matter may be removed by purification, filtration, centrifugation, or the like.

The content of the added protein in the present cosmetic is not particularly limited as long as it is an effective amount. The content of the added protein is usually 0.01 to 10% by mass.

The cosmetic may optionally contain other ingredients than the added protein as long as they do not inhibit the effects of the present invention. Examples of the other ingredients include known ingredients conventionally added to cosmetics and other functional ingredients. Specific examples of other components include fats and oils, hydrocarbon oils, higher fatty acids, higher alcohols, ester oils, silicone oils, anionic surfactants (anionic, cationic, amphoteric, nonionic), and moisturizing agents. , water-soluble polymers, film-forming agents, ultraviolet absorbers, sequestering agents, lower alcohols, polyhydric alcohols, sugars, amino acids, pH adjusters, vitamins, antioxidants, pigments, preservatives, and fragrances.

There are no particular restrictions on the dosage form and usage form of the cosmetic. The present cosmetic can be used, for example, in the form of lotion, emulsion, gel, ointment/wax, foam, solid/powder, or mist.

There is no particular limitation on the application site of the present cosmetic. The cosmetic can be applied, for example, to skin or hair. The cosmetic can be used to improve, protect or repair skin or hair.

There are no particular restrictions on the specific uses of the present cosmetic. Specific uses of the present cosmetics include, for example, basic cosmetics such as lotions, milky lotions, creams, and oils, skin cleansers, massage agents, depilatories and post-treatment agents, foundations, lipsticks, and eyelashes. Makeup cosmetics such as shadows, eyeliners and mascaras, face masks, tapes, sheets, nail repairing and protecting agents, hair growth and tonic agents, and hair treatment agents.

When hair is damaged, cysteine in the hair is converted to cysteic acid, increasing the negative charge and increasing the anionicity. As a result, the added protein with strong cationicity can adhere to the hair more strongly. As a result, the hair treatment agent containing the added protein is excellent in improving, protecting or repairing the functions and properties of damaged hair. Therefore, the present cosmetic is suitable as a hair treatment agent such as a shampoo, rinse, treatment, conditioner, hair styling agent, permanent waving agent, curling agent, hair coloring agent, or as a pre- or post-treatment agent using these agents. can be used. In addition, the present cosmetics can be used not only for humans but also for cosmetic goods for animals other than humans, quasi-drugs for animals other than humans, external preparations for skin, hair treatment agents, and the like.

EXAMPLES The present invention will be specifically described below with reference to Examples. It should be noted that the present invention is not limited to the forms shown in the examples. The embodiments of the present invention can be variously modified within the scope of the present invention depending on the purpose, application, and the like.

Specific compositions of the cosmetics of Formulation Examples 1 to 20 are shown below.

(Prescription example 1) Shampoo

(Prescription example 2) Shampoo

(Prescription example 3) Shampoo

(Prescription Example 4) Rinse

(Prescription Example 5) Rinse

(Prescription Example 6) Rinse

(Prescription example 7) Treatment

(Prescription Example 8) Hair conditioner

(Prescription Example 9) Hair oil

(Prescription Example 10) Hair setting lotion

(Prescription Example 11) Hair Styling Gel

(Prescription Example 12) Hair Styling Spray

(Prescription Example 13) Hair foam

(Prescription Example 14) Hair treatment agent (both pre-treatment and post-treatment)

(Prescription Example 15) Hair wax

(Prescription Example 16) Hair coloring agent

(Prescription Example 17) Hair manicure

(Prescription Example 18) Permanent wave agent

(Prescription Example 19) Straightener for curly hair

(Prescription Example 20) Curling agent

Example 1: Hair strength improvement test 1 bleaching agent (“Lecee Powder Bleach EX” manufactured by Hoyu Co., Ltd.) and 2 bleaching agents (“Ordeve Addicthy Oxidan 6%” manufactured by Milbon Co., Ltd.) were mixed at 1: 2: 5 ( mass ratio) to obtain a bleach mixture. The bleach mixture was evenly applied to a hair bundle (manufactured by Staffus Co., Ltd., "test hair bundle 1 g 10 cm, human hair, black"), left at 25°C for 30 minutes, and thoroughly washed with water. This bleaching process was performed twice. The hair tress was immersed in a 1.0% by mass sodium lauryl sulfate solution at 25° C. for 5 minutes. Then, the tress was washed with water and used as a tress for evaluation.

The following cosmetics (A) to (C) were used as sample solutions.
(A) In Formulation Example 10, water was added in place of the S-amidinocysteinyl keratin.
(B) Instead of the S-amidinocysteinyl keratin of Formulation Example 10, "Proticute C Alpha" manufactured by Ichimaru Farcos Co., Ltd. was added as cationized keratin.
(C) Formulation Example 10

After the hair tress for evaluation was immersed in the sample solution for 5 minutes, it was washed with water and dried with warm air. Using a universal tensile tester ("AG-20k NXDplus" manufactured by Shimadzu Corporation) for the treated hair bundle, the tensile breaking strength (N) and elongation rate ( %) was measured (n=10).

The results of the hair strength improvement test are as follows. Using this result as an index, hair damage was evaluated.
Cosmetic (A): Tensile strength 0.65 (N) and elongation rate 37.1 (%)
Cosmetic (B): Tensile strength 0.82 (N) and elongation rate 39.6 (%)
Cosmetic (C): Tensile strength 1.13 (N) and elongation rate 44.9 (%)

Example 2: Hair Adhesion Test Evaluation hair and sample solutions were evaluated hair tresses of Example 1 and cosmetics (A) to (C) and (D) of S-amidinocysteinyl keratin of Formulation Example 10. Instead, "Catinal HC-200" manufactured by Toho Chemical Industry Co., Ltd. (degree of cationization: 1.3 meq/g) was used.

The hair tresses for evaluation were vacuum-dried in a silica gel desiccator for 20 days, and the mass of each hair was measured. Then, the hair tresses for evaluation were immersed in the sample solution for 30 minutes, then washed with water and dried with hot air. Thereafter, the hair tresses for evaluation were vacuum-dried in a silica gel desiccator for 20 days, and the mass of each hair was measured. The hair adhesion rate (%) was calculated based on the following formula.
Hair adhesion rate (%) = (H2-H1)/H1 x 100
H1: Mass of hair before test (g)
H2: Mass of hair after test (g)

The results of the hair adhesion test are as follows. Using this result as an index, hair damage was evaluated.
Cosmetic (A): Hair adhesion rate 0.11 (%)
Cosmetic (B): Hair adhesion rate 0.84 (%)
Cosmetic (C): Hair adhesion rate 2.51 (%)
Cosmetic (D): Hair adhesion rate 1.04 (%)

Example 3: Hair Frictional Damage Reduction Test As hair for evaluation, a hair bundle for evaluation "test hair bundle 1 g 10 cm, human hair, black" manufactured by Staffus Co., Ltd. was used, and the following cosmetics ( A) to (C) were used.
(A) Water was added in place of the N-amidinocysteinyl keratin of Formulation Example 6.
(B) Instead of the N-amidinocysteinyl keratin of Formulation Example 6, "Proticute C Alpha" manufactured by Ichimaru Pharcos Co., Ltd. was added.
(C) Formulation Example 6

After applying 1 g of the sample solution to the tress for evaluation, the tress was washed with water and dried with hot air. After drying, the hair was brushed 10 times. This step was defined as 1 time and was repeated 50 times. Thereafter, the tensile breaking strength (N) and elongation rate (%) per hair of the treated hair tress for evaluation were measured in the same manner as in Example 1 (n=10).

The results of the hair friction damage mitigation test are as follows. Using this result as an index, hair damage was evaluated.
Cosmetic (A): Tensile strength 0.77 (N) and elongation rate 38.2 (%)
Cosmetic (B): Tensile strength 0.98 (N) and elongation rate 42.3 (%)
Cosmetic (C): Tensile strength 1.19 (N) and elongation rate 45.1 (%)

Example 4: Hair protection test against damage by shampoo As hair for evaluation, a hair bundle for evaluation "test hair bundle 1 g 10 cm, human hair, black" manufactured by Staffus Co., Ltd. was used, and the following cosmetics were used as sample solutions: (A) to (D) were used.
(A) Water was added in place of the N-amidinocysteinyl keratin of Formulation Example 2.
(B) "Proticute C Alpha" manufactured by Ichimaru Pharcos Co., Ltd. was added in place of the N-amidinocysteinyl keratin of Formulation Example 2.
(C) Formulation Example 2
(D) Instead of the N-amidinocysteinyl keratin of Formulation Example 2, "Catinal HC-200" manufactured by Toho Chemical Industry Co., Ltd. (degree of cationization: 1.3 meq/g) was added.

After applying 1 g of each sample solution as a shampoo to the hair tress for evaluation, the hair was sufficiently foamed, rinsed with warm water, and then dried with hot air. This process was set to 1 time and was repeated 30 times. Thereafter, the tensile breaking strength (N) and elongation rate (%) per hair of the treated hair tress for evaluation were measured in the same manner as in Example 1 (n=10).

The results of the hair protection test against shampoo damage are as follows. Using this result as an index, hair damage was evaluated.
Cosmetic (A): Tensile strength 0.95 (N) and elongation rate 38.0 (%)
Cosmetic (B): Tensile strength 1.08 (N) and elongation rate 42.5 (%)
Cosmetic (C): Tensile strength 1.22 (N) and elongation rate 44.4 (%)
Cosmetic (D): Tensile strength 1.03 (N) and elongation rate 42.2 (%)

From Examples 1 and 3, the hair treated with the cosmetic (C), which is the product of the present invention, was treated with the cosmetic (A) not containing the added protein and the cosmetic containing cationized keratin instead of the added protein. Higher tensile strength and elongation compared to hair treated with (B). Similarly, from Example 4, the hair treated with the cosmetic (C), which is the product of the present invention, was treated with the cosmetic (A) not containing the additional protein and the cosmetic containing cationized keratin instead of the additional protein. Higher tensile strength and elongation compared to hair treated with ingredients (B) and (D).

Furthermore, from Example 2, the cosmetic (C), which is an embodiment of the present invention, is a cosmetic (A) that does not contain the added protein, a cosmetic (B) that contains cationized keratin instead of the added protein, and Compared to (D), the rate of adhesion to hair is at least twice as high.

These results show that the cosmetic (C), which is an embodiment of the present invention, has excellent adhesion to the application site (hair) and has a protective effect against physical hair damage from heat and friction (Examples 1 and 3). ) and a protective effect against chemical hair damage by shampoo (Example 4).

Claims (3)

A cosmetic containing a protein in which amidinocysteine is added to part or all of SH groups of amino acids constituting the protein. The cosmetic according to claim 1, wherein said protein is keratin. 3. The cosmetics according to claim 1 or 2, wherein the cosmetics are shampoos, rinses, treatments, conditioners, hair styling agents, permanent waving agents, curling agents, hair coloring agents, or pre- or post-treatment agents using these agents. cosmetics.