KR100692951B1 - A composition comprising cathepsin B inhibitor as active ingredient for functional cosmetics - Google Patents

Abstract

The present invention relates to a cosmetic composition containing a cathepsin B inhibitor as an active ingredient, wherein the cathepsin B inhibitor is a compound represented by the following general structural formula (I).

General Structural Formula (I)

Wherein R ₁ is a guanidino or amino group. The cosmetic composition containing the cathepsin non-inhibitor according to the present invention as an active ingredient is excellent in the production of collagen, prevention of skin aging and wrinkle removal, and thus development as a functional cosmetic containing the compound of the present invention as an active ingredient is possible. Do.

Functional cosmetics, cathepsin B inhibitor, wrinkle removal, collagen, MMP

Description

A composition comprising cathepsin B inhibitor as active ingredient for functional cosmetics}             

1 is a view showing the skin structure of the human body,

2 is a collagen standard graph of Experimental Example 1;

Figure 3 is a photograph of the skin cells observed under the microscope after the MMP inhibitor treatment,

4 is a standard graph of [Collagen-Ab] complex of Experimental Example 2;

FIG. 5 shows collagen concentrations discharged by treating various concentrations of MMP inhibitors at 1 × 10 5 cells / well.

  The present invention relates to a functional cosmetic composition containing a cathepsin non-inhibitor as an active ingredient.

   The skin doesn't just cover the body, but it stimulates the touch, cold, warmth, sensation and pressure through physical stimulation, chemical stimulation, protection from bacteria, protection from light and sensory perception. It senses and secretes sweat, sebum, and wastes to maintain body temperature and acidity of the subsurface, which plays a role in waterproofing, antibacterial, moisture, respiratory, vitamin D synthesis, and nutrient storage. .

   Not only because of the important role of the skin, but also due to the improvement of economic level, a great deal of attention is being paid to aging and appearance. As an example of this global interest, the global market for skin cosmetics reaches 180 trillion, growing 5-10% annually. In the United States, the market for functional cosmetics is about $ 350 million. Among the Asian markets, the Japanese market is the world's second largest and the market for functional cosmetics is estimated to be about 14 billion yen, and the Chinese cosmetics market is growing at an average annual rate of about 13%, which is known to have great growth potential. Korea's cosmetics market is estimated to reach W2.55tr in 1998 and W100bn for functional cosmetics. (Cosmetics Association)

   Increasing demand for functional cosmetics has caused the industry's sense of focus to be concentrated in this field, and recent patent trends also show interest in functional cosmetics. This is shown in Table 1 below.

Table 1: Number of Applications by Year of Functional Cosmetics

Among the functional cosmetics, patent applications for anti-aging cosmetics (wrinkle improver, whitening agent) began to be filed in 1986 and totaled 263 cases (based on public data as of June 2001) until June 2000.

It is expected that patent applications will continue to increase in the future due to the legislation of functional cosmetics by enacting cosmetic law.

Skin structure and its mechanism of action

The structure of the skin looks like one layer, but it looks like a stack of thin sheets of paper. It consists of epidermis, epidermis, dermis, and subcutaneousfat. This is shown in FIG.

The epidermis has the function of protecting the inside from the external stimulus, and there are five layers of the stratum corneum, the transparent layer, the granule layer, the pole layer, and the basal layer. The epidermal cells include keratinocytes, melanocytes, and langerhans. There are Langerhans' cells and Merkel cells.

   The differentiation process in keratinocyte is mainly in the basal layer, and the cells made here are gradually pushed up and fall into the polar layer → granule layer → transparent layer → keratinocytes. This process is called keratinization process. In the aged skin of the human body, it takes more time for the stratum corneum to fall, so the stratum corneum becomes thicker. Therefore, the deterioration of keratinocytes causes the dead cells to increase and cause fine wrinkles and rough skin. Therefore, it is necessary to make the skin surface smooth and soft by increasing the natural moisturizing substances in the skin and making the stratum corneum compact.

   Melanocytes (melanocytes) extend between the keratinocytes of the stomach, the melanin delivered to the keratinocytes spread to the upper part of the basement layer of the epidermis to prevent damage to the cells of the basement layer by ultraviolet rays. In other words, melanin plays a role in determining skin color and hair color, and plays an important role in preventing damage to the skin from ultraviolet rays by absorbing or scattering ultraviolet rays. Keratinocytes containing melanin gradually migrate to the stratum corneum and finally fall off the stratum corneum.

   Langerhans' cells are mostly present in the polar layer and are mainly involved in skin immunity. In other words, these cells are responsible for delivering the antigen from the outside to lymphocytes, immune cells.

   Merkel cells are located in the basal layer and sense the sense of touch in the skin.

The dermis is located under the epidermis and occupies most of the skin, which is the most important part of the skin and manages the elasticity of the entire skin. It is composed of fibrous proteins such as amorphous ground substance, collagen fiber and elastin fiber. In addition, the vascular system and lymphatic system are intricately entangled and provide nutrients to the epidermis to support the epidermis and maintain and protect other tissues of the skin by toughness.

The dermal layer can be divided into papillary dermis and reticular dermis. The cells in the dermis are predominantly made up of fibroblasts, which are widely distributed in connective tissue. These fibroblasts are responsible for the production of collagen and elastin, the extracellular matrix (ECM), and various other substrates.

   Collagen makes up most of the extracellular matrix (ECM) of several tissues, including the dermis. Thirteen types have been identified until recently, but I, III, IV, V, VI, and VII 6 are distributed in human skin, and Type I accounts for about 85%. Collagen is involved in normal or pathological biological processes such as cell binding, cell differentiation, wound healing, various fibrosis and inflammatory responses, and cancerous transformation.

   Collagen is a protein that accounts for 90% of the dermis, providing tension to the skin and 7% of the total dry weight of the skin, excluding fat. Collagen molecules are made from fibrous cells, and collagen fibers and elastin fibers are woven into each other in a mesh shape to give elasticity and elasticity to the skin. Most of the collagen in the dermis of adults is type I and about 20% is type III collagen. In the dermis, glycosaminoglycans such as muco-mucopolysaccharides (hyaluronic acid and Chondroitin sulfate), called substrates, are substances that fill between the collagen fibers of the dermis and the binding fibers of the dermis. These changes are caused by the loss of glycosaminoglycans) and their ability to bind with water and by the loss of elasticity and the reduction of hyaluronic acid, the substrate of the dermis, which leads to wrinkles and sagging skin. It is usually known to be caused by free radicals.

Subcutaneous tissue is the part between the dermis and the skeleton, which contains a large amount of fat, serves to support blood vessels and nerves, and determines human nutrition.

Causes of skin aging and improvement measures against skin aging mechanism

Skin aging refers to wrinkles, loss of elasticity and abnormal pigmentation, which can be divided into internal factors and external factors.

   Internal factors include growth hormone reduction and natural aging. External factors cause radical oxygen to be released under the influence of UV rays, which damage skin cells, resulting in wrinkles, decreased elasticity and pigmentation.

1) problems with the epidermal layer

corneous

If any of these internal and external factors cause problems with the epidermal layer of the skin It is closely related to the normal division and differentiation of keratinocytes, and recently, researches to maintain the barrier by inducing the normal formation cycle of keratinocytes as well as application of moisturizing ingredients from the outside have been conducted. Skin moisture is maintained by the sebum secreted from the sebaceous gland and the lipid layer existing between the natural moisturizing factor (NMF) of the stratum corneum. The main component of intercellular lipid is composed of a mixture of ceramide, saturated fatty acid, and cholesterol (cholesterol) by about 1 molecule. When the barrier is broken, the lamellar granules of epidermal superficial cells are initially released immediately, which then promotes the synthesis of cholesterol and fatty acids. Meanwhile, the synthesis of ceramide and DNA synthesis of the epidermis occur later, as well as the recovery of the barrier as well as thickening of the epidermis. The composition of the normal lipid layer is closely related to the normal division and differentiation of keratinocytes. Recently, studies on maintaining the barrier by inducing the normal formation cycle of keratinocytes as well as application of moisturizing components from the outside have been conducted.

   The water-soluble amino acid constituting NMF accumulates in Keratohyalin granules, binds keratin fibers, and fillaggrin of the interstitial protein present in the stratum corneum cells, the lower layer of stratum corneum cells. As it moves from to the surface layer, it is degraded by proteolytic enzymes in the stratum corneum. Filaggrin consists of 317 amino acids and is a pilaggrin unit, a pilaggrin unit (molecular weight 34kDa) consisting of 7 amino acid linker peptides sandwiched between 10 or several bundles of precursor proteins, propyllagrin (profilaggrin) (macromolecules with a molecular weight of about 400 kDa). Filaggrin is finally decomposed into amino acids by activities of amino peptidase, carboxypeptidase and the like in the process of reaching the upper stratum corneum.

There have been reports of filaggrin expression abnormalities in atopic dermatitis, geriatric psoriasis, and younger skin, and the expression and degradation regulation of keratinocytes in keratinocytes should be studied further in connection with the division of keratinocytes. to be.

Pigment Control

Problems such as pigmentation Melanin is made from melanocytes and delivered to keratinocytes. Most of the whitening agents developed to date are inhibitors of tyrosinase, such as hydroquinone or kojic acid. Imakawa et al. Found that endothekin-1 (ET-1), which is secreted from keratinocytes, is an important factor in the growth and differentiation of melanocytes. Cammomile extracts Reported blocking. It has been 20 years since melanocytes were reported for long-term culture in vitro by Eisinger and Marko and many studies have since been conducted. Recently, the possibility of controlling pigmentation has been sought by understanding the interaction with keratinocytes and the delivery of melanosomes rather than melanocytes alone. Recently, the melanosome transfer process from melanocytes to keratinocytes is reported to be phagocytosis by PAR-2 activity, and inhibitors of PAR-2 have been reported to inhibit it. However, the biological understanding of melanin formation is still unclear, and further studies on pigmentation disorders such as blemishes and blotch, pigmentation caused by ultraviolet rays, and the action of hormones related to pigmentation should be studied. Pigmentary dysplasia due to skin aging such as blackening of the skin by UV rays and blemishes, blemishes, and blotch is thought to be different.

2) problems with the dermis

The expression of elastin genes is markedly promoted in skin cells exposed to ultraviolet rays due to abnormalities on the dermis, and the expression of elastin genes is caused by free radicals.

   Degradation of collagen is a major factor causing light aging. In particular, the accumulation of elastic materials is a phenomenon caused by the simultaneous destruction of the surrounding collagen bundles and is evidenced by the presence of matrix metalloproteinases (MMPs) responsible for ECM degradation in photoaging. Can be.

   MMPs consist of at least 14 different kinds of degrading enzymes. Most of these proteases can degrade native collagen, modified collagen, elastin fibers, various proteoglycans, fibronectin and other dermal components.

   Ultraviolet irradiation of fibroblasts has been reported to increase the expression of proteolytic enzymes. UV-1 activates growth factors and cytokine receptors on skin cells to activate AP-1 via MAP kinase.

   AP-1 activity in the epidermis and dermis increases the expression of MMPs. Eventually, a single irradiation of UV light on human skin increases the activity of MMPs and increased enzyme activity mainly degrades collagen of type I collagen. At the same time, UV irradiation is known to induce the synthesis of specific tissue inhibitors (Tissueinhibitor of MMP, TIMP).

   Despite the exact balance of degrading enzymes and degrading enzyme inhibitors in photo-aged skin, excessive collagen production is created after UV irradiation, resulting in skin collagen loss.

   It is initiated by UV-sensing signal of photoaging, and it can prevent skin aging by antioxidants that can block it early and MMP inhibitors that inhibit MMP expression. It is becoming.

   Recent studies have shown that changes in basement membranes occur in photo-aged skin and type IV and VII collagen is reduced. This change is said to begin in the late twenties. Changes in the basement membrane lead to an increase in MMPs in the epidermis as well as in keratinocyte abnormalities.

    Recently, as the importance of skin is highlighted, researches in the physiological, immunological and molecular biological fields of the skin have been concentrated all over the world.

Skin is the widest organ of the human body and is essential for human health and life support. It is an important organ that performs a wide variety of functions such as endocrine function, immune function, absorption and secretion function, and protective function. Meanwhile, skin tissues are easier to study in vitro and in vivo than other human organs, and efforts to identify mechanisms of various diseases are increasing. In developed countries such as the United States, the importance of dermatology is recognized, and national support is extensively supported.

   The National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIMS) in the United States NIH focuses on research on the skin, muscle, and skeletal systems. NIAMS 'budgets for NIH are $ 350 million in 2000, $ 400 million in 2001, and $ 444.4 million in 2002, of which more than one third are used for dermatological research, and about 10% of the $ 800 million invested in aging in NIH. Is considered to be used for skin aging research, the skin budget is estimated to be around 250-300 billion won / year (NIH Budget Report).

-Skin aging prevention and treatment technology

Pigment Control Technology

-Development of moisturizer

Drug absorption through the skin

-Artificial skin manufacturing technology

    The present invention provides a functional cosmetic composition containing a cathepsin B inhibitor as an active ingredient.

The present inventors have continued a long research on cathepsin B inhibitors, and various inventions have been completed and patented or are pending. Patent Application No. 2002-14873 (New strain Streptomyces S. C. vivia-55 and production method of cathepsin B inhibitor derivative using this microorganism), Patent Application No. 2002-14874 (Isolation of cathepsin B inhibitor derivative And purification method), Patent Application No. 2002-17237 (new cathepsin B inhibitor derivative and preparation method thereof), 2003-18598 (arthritis therapeutic composition containing cathepsin B derivative as an active ingredient), 2003-38897 ( Burn therapeutic composition containing a cathepsin B inhibitor as an active ingredient).

    The present invention can be a raw material of functional cosmetics by containing a cathepsin B inhibitor as an active ingredient to prevent damage and degradation of collagen by MMP generated when skin cells are damaged, and is represented by the following general structural formula (I) Compound.

(I)

Wherein R ₁ is a guanidino or amino group.

The compound wherein R ₁ is guanidino is 5-acetylamino-2-isobutyl-7-methyl-4-oxo-octanophosphoric acid (1-formyl-4-guanidino-butyl) amide (Compound 1), A compound in which R ₁ is an amino group is 5-acetylamino-2-isobutyl-7-methyl-4-oxo-octanophosphoric acid (4-amino-1-formyl-1-butyl) amide (compound 2).

   The composition containing the MMP inhibitor according to the present invention as an active ingredient has multiple functions and prevents proteins such as collagen constituting most of the dermis from being damaged by external stimuli caused by environmental pollution. It can affect the regeneration effect of skin damaged by anti-aging functional cosmetics and UV rays. Therefore, the composition of the present invention can be used as a functional cosmetic raw material.

  The MMP inhibitor of the present invention is formulated in the form of an external preparation together with excipients or auxiliaries that are acceptable for ordinary cosmetics, such as powders, creams, patches, patches, lotions, gels, pastes, packs, solutions, and the like. Can be used.

An effective concentration of the MMP inhibitor of the present invention may use a formulation of about 0.1 uM to 1000 uM.

      Next, the present invention will be described in more detail as an experimental example.

Experimental Example 1

Measurement of collagen production, a skin cell protein substrate (How to use the Sircol collagen assay kit)

1) The cells used are normal human fibroblasts, and the culture medium is grown in DMEM with 10% FBS, and then 1x10 ⁵ cells / well are planted in a 6well plate.

2) After 5% CO ₂ incubator is grown at 37 ℃ until 80% confluent

(Usually 2 to 3 days) Remove the culture with an aspirator.

3) Treat the test substance to a non-toxic concentration (0-1000 uM). The test substance (MMP Inhibitor) is 0-1000uM. At this time, FBS is added without any addition of FBS to the skin cells by treating various concentrations in 1ml of DMEM.

4) After 2 days, remove the cell supernatant and perform collagen assay.

5) Collagen assay is a Sircol collagen assay kit (from biocolor com.) That uses dye reagents that specifically bind to soluble collagen and captures soluble collagen. (30 minutes mild mix)

6) Captured collagen is obtained by centrifuge 10,000g 4 ℃ for 10 minutes. After dissolving collagen, add 1ml Sircol Alkali reagent and transfer 200ul to 96well plate.

7) At this time, the concentration of standard collagen should be adjusted to 0, 6.25ug, 12.5ug, 25ug and read with ELIZA reader at 540nm with sample.

8) The experimental results are shown in Table 2, and the results obtained by observing skin cells under a microscope after the experiment are shown in FIG. 3.

9) As confirmed from Table 2, it was confirmed that the amount of collagen after treatment with the compound of the present invention was greatly increased, and the most efficient concentration for collagen production was 10 to 100 μM by the method of using a sicol collagen analysis kit. As can be seen from 10, 100, 1000uM all skin cells did not have any effect on the morphology.

Table 2: Measurement of collagen content after treatment of various concentrations of MMP inhibitor

Experimental Example 2 (a little more precise experiment)

Measurement of Collagen Production, a Skin Cell Protein Substrate

      -Procollagen Type I C-Peptide EIA Kit:

        Cat. # MK101 from TAKARA BIO INC.

1) Use cells as normal human fibroblast, and culture medium is grown in DMEM with 10% FBS, and then plant 1x10 ⁵ cells / well in 6well plate.

2) Incubate the cells at 5% CO ₂ incubator at 37 ° C until they are 80% confluent (usually 2 to 3 days) and remove the culture with an aspirator.

3) Treat the test substance to a non-toxic concentration (0.1-100 uM). The test substance is Compound 2 (MMP Inhibitor) of the present invention is 0.1-100uM, in which FBS is added to 1ml of DMEM without treatment, and treated with skin cells.

4) After 1 day, remove the cell supernatant and perform collagen assay.

5) Prepare sample concentration in 1x, 1 / 5x, 1 / 10x with sample diluent embedded in collagen assay kit.

6) Set the standard concentration to 0. 40, 80,160 ng / m.

7) Add 100µl of sample and standard to 96well plate coated with monoclonal anti-procollagen type IC peptide (PIP) antibody and incubate at 37 ℃ for 2 hours. The sample and standard solution are allowed to react within 5 minutes.

8) After the reaction, wash well three times with 400µl PBS.

9) Incubate 100 µl of monoclonal antibdy conjugated with horseradish peroxidase (POD) at 37 ° C for 1 hour in each well.

10) After the reaction, wash sufficiently with 400 µl of PBS four times.

11) Incubate 100µl of the solution containing substrate (hydrogen peroxide and tetramethylbenzidine) at room temperature for 15 minutes.

12) Add 100µl of Stop solution 1N sulfuric acid and mix well.

13) Read the OD at 450nm.

14) The results are shown in FIG. As a result of measuring the collagen amount more finely with the Procollagen Type I C-peptide EIA Kit, the treatment of MMP inhibitor 0.1μM, 1μM, 10μM on the skin cells was much better than the control level collagen amount of the untreated skin cells. At this time, the state of the saepo was all healthy.

From the above experimental results, the substance of the present invention is excellent in the effect of generation of collagen, prevention of skin aging and wrinkle removal, and thus it is possible to develop as a functional cosmetic containing the compound of the present invention as an active ingredient.

  The cathepsin non-derivatives of the present invention may be in the form of preparations of cosmetic or pharmaceutically acceptable external preparations together with conventional cosmetic or pharmaceutically acceptable excipients or auxiliaries, such as creams, patches, patches, lotions, It may be formulated into a gel, a paste, a pack, a liquid, or the like.

Next, preparation examples of the present invention are illustrated. (Parts in the present invention are parts by weight.)

Formulation Example 1

Compound 1 0.1part

Beeswax Part 7

Cetyl Alcohol7

Reduced Lanolin Part 5

Lipid-type monosteric acid glycerin part 2

Polyoxyethylene sorbitan mono-

Lauric acid ester

Quran

10 parts of propylene glycol

Spices

Antioxidant

Appropriate amount of purified water (100 parts total)

The above ingredients were prepared according to the conventional method for preparing creams.

Formulation Example 2

0.5 parts of compound

Beeswax, part eight

Cetyl Alcohol 부 Part 10

Reduced lanolin

Quran

Fatty acid glycerol 5part

Lipophilic monosorbitan glycerin part 2

Polyoxyethylene sorbitan monolauric acid

Ester # 2

Spices

Antioxidant

Appropriate amount of purified water (100 parts total)

The above ingredients were prepared according to the conventional method for preparing creams.

Formulation Example 3

Compound 1.0 1.0part

Vitamin C C0

Stranran part 5

Vaseline Part 5

Beeswax 90

Sorbitan sesquioleic acid ester x 1

Polyoxyethylene oleyl ether ether 1.5 parts

Propylene glycol7 parts

Ethanol Part 5

Carboxy vinyl polymer (1% aqueous solution) 부 15 parts

Potassium hydroxide 90.05 parts

Spices

Antioxidant

Appropriate amount of purified water (100 parts total)

The emulsion was prepared according to the conventional method for preparing the latex agent.

Formulation Example 4

Compound 2 0.2 parts

New Daum Part 6

Squalane # 3

Propylene glycol # 6

Zinc Oxide # 5

Kaolin 90

Ethanol Part 5

Spices

Preservative

Appropriate amount of purified water (100 parts total)

The pack is prepared according to the conventional method for preparing the emulsion.

Formulation Example 5

Compound 2: 20.5 parts

Hydrogenated polyoxyethylene (60) castor oil: Part 2

Ethanol 15

Sodium citrate

１,3-butylene glycol +10 parts

Preservative

Spices

Appropriate amount of purified water (100 parts total)

The above components are prepared according to a conventional method for preparing an emulsion.

Formulation Example 6

Compound 1 0.1part

Sodium Flush Date 0.2

Beeswax Part 7

Cetyl Alcohol7

Reduced Lanolin Part 5

Lipid-type monosteric acid glycerin part 2

Polyoxyethylene sorbitan mono-

Lauric acid ester

Quran

10 parts of propylene glycol

Spices

Antioxidant

Appropriate amount of purified water (100 parts total)

The above ingredients were prepared according to the conventional method for preparing creams.

Formulation Example 7

0.5 parts of compound

Beeswax, part eight

Cetyl Alcohol 부 Part 10

Reduced lanolin

Quran

Fatty acid glycerol 5part

Lipophilic monosorbitan glycerin part 2

Polyoxyethylene sorbitan monolauric acid

Ester # 2

Spices

Antioxidant

Appropriate amount of purified water (100 parts total)

The above ingredients were prepared according to the conventional method for preparing creams.

Formulation Example 8

Compound 11 0.1part

β-sitosterol0.5part

Vitamin C C0

Stranran part 5

Vaseline Part 5

Beeswax 90

Sorbitan sesquioleic acid ester x 1

Polyoxyethylene oleyl ether ether 1.5 parts

Propylene glycol7 parts

Ethanol Part 5

Carboxy vinyl polymer (1% aqueous solution) 부 15 parts

Potassium hydroxide 90.05 parts

Spices

Antioxidant

Appropriate amount of purified water (100 parts total)

The above components are prepared according to a conventional method for preparing an emulsion.

Formulation Example 9

Compound 2 0.2 parts

Calcipotriol 0.001

New Daum Part 6

Squalane # 3

Propylene glycol # 6

Zinc Oxide # 5

Kaolin 90

Ethanol Part 5

Spices

Preservative

Appropriate amount of purified water (100 parts total)

The pack is prepared according to the above-described method for producing a pack.

Formulation Example 10

Compound 2: 20.5 parts

Betamethasone Valerate 0.005

Hydrogenated polyoxyethylene (60) castor oil: Part 2

Ethanol 15

Sodium citrate

１,3-butylene glycol +10 parts

Preservative

Spices

Appropriate amount of purified water (100 parts total)

The said component is manufactured according to the manufacturing method of a normal lotion agent.

Formulation Example 11

Compound 1 0.1part

0.1 parts hydrocortisone acetate

Beeswax Part 7

Cetyl Alcohol7

Reduced Lanolin Part 5

Lipid-type monosteric acid glycerin part 2

Polyoxyethylene sorbitan mono-

Lauric acid ester

Quran

10 parts of propylene glycol

Spices

Antioxidant

Appropriate amount of purified water (100 parts total)

The above ingredients were prepared according to the conventional method for preparing creams.

Formulation Example 11

0.5 parts of compound

Beeswax, part eight

Cetyl Alcohol 부 Part 10

Reduced lanolin

Quran

Fatty acid glycerol 5part

Lipophilic monosorbitan glycerin part 2

Polyoxyethylene sorbitan monolauric acid

Ester # 2

Spices

Antioxidant

Appropriate amount of purified water (100 parts total)

The above ingredients were prepared according to the conventional method for preparing creams.

Formulation Example 11

Compound 1.0 1.0part

Vitamin C C0

Stranran part 5

Vaseline Part 5

Beeswax 90

Sorbitan sesquioleic acid ester x 1

Polyoxyethylene oleyl ether ether 1.5 parts

Propylene glycol7 parts

Ethanol Part 5

Carboxy vinyl polymer (1% aqueous solution) 부 15 parts

Potassium hydroxide 90.05 parts

Spices

Antioxidant

Appropriate amount of purified water (100 parts total)

The above components are prepared according to a conventional method for preparing an emulsion.

The composition containing the cathepsin non-inhibitor of the present invention as an active ingredient is excellent in the production of collagen, prevention of skin aging, and wrinkle removal, and thus can be developed as a functional cosmetic containing the compound of the present invention as an active ingredient.

Claims (1)

 A cosmetic composition having an anti-aging and anti-wrinkle effect, which contains a cathepsin non-inhibitor compound represented by the following general structural formula (I) as an active ingredient.

Wherein R ₁ is a guanidino or amino group.

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