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WO2008054144A1 - Composition à usage externe pour la peau contenant des inhibiteurs de la cathepsine g servant à prévenir le vieillissement de la peau et procédé de criblage pour le développement de substances antivieillissement - Google Patents

Composition à usage externe pour la peau contenant des inhibiteurs de la cathepsine g servant à prévenir le vieillissement de la peau et procédé de criblage pour le développement de substances antivieillissement Download PDF

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Publication number
WO2008054144A1
WO2008054144A1 PCT/KR2007/005451 KR2007005451W WO2008054144A1 WO 2008054144 A1 WO2008054144 A1 WO 2008054144A1 KR 2007005451 W KR2007005451 W KR 2007005451W WO 2008054144 A1 WO2008054144 A1 WO 2008054144A1
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WO
WIPO (PCT)
Prior art keywords
cathepsin
skin
aging
external composition
metalloproteinase
Prior art date
Application number
PCT/KR2007/005451
Other languages
English (en)
Inventor
Eui Dong Son
Hyae Kyoung Kim
Hyun Jung Choi
So Hee Lee
Jin Young Lee
Jae Won Yoo
Jae Sung Hwang
Ih Seop Jang
Original Assignee
Amorepacific Corporation
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Amorepacific Corporation filed Critical Amorepacific Corporation
Publication of WO2008054144A1 publication Critical patent/WO2008054144A1/fr

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Classifications

    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
    • A61K8/40—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds containing nitrogen
    • A61K8/42—Amides
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K31/00—Medicinal preparations containing organic active ingredients
    • A61K31/16—Amides, e.g. hydroxamic acids
    • A61K31/165—Amides, e.g. hydroxamic acids having aromatic rings, e.g. colchicine, atenolol, progabide
    • A61K31/166—Amides, e.g. hydroxamic acids having aromatic rings, e.g. colchicine, atenolol, progabide having the carbon of a carboxamide group directly attached to the aromatic ring, e.g. procainamide, procarbazine, metoclopramide, labetalol
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
    • A61K8/33—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds containing oxygen
    • A61K8/34—Alcohols
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
    • A61K8/40—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds containing nitrogen
    • A61K8/44—Aminocarboxylic acids or derivatives thereof, e.g. aminocarboxylic acids containing sulfur; Salts; Esters or N-acylated derivatives thereof
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q19/00—Preparations for care of the skin
    • A61Q19/08—Anti-ageing preparations
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K2800/00—Properties of cosmetic compositions or active ingredients thereof or formulation aids used therein and process related aspects
    • A61K2800/40—Chemical, physico-chemical or functional or structural properties of particular ingredients
    • A61K2800/52—Stabilizers
    • A61K2800/522—Antioxidants; Radical scavengers

Definitions

  • the present invention relates to a skin external composition for preventing skin aging, which contains a cathepsin G inhibitor as an active ingredient, and to a method for screening anti-aging substances, which are capable of inhibiting cathepsin G activity.
  • Skin aging may be divided into photoaging, resulting from external factors such as UV light, and intrinsic aging, resulting from a change in hormones and a change in internal factors such as stresses. Due to the combined action of such aging phenomena, an increase in skin wrinkles or a decrease in skin elasticity appears. As skin aging progresses for this reason, the content and arrangement of collagen, elastin, hyaluronic acid, proteoglycan, glycosaminoglycan, fibronectin and sugar protein in the skin are changed or decreased, and their ability to bind to moisture is reduced. As a result, the substrates of the skin are reduced, and thus the skin' s ability to maintain moisture, leading to conditions, such as loss of skin firmness, skin drying and skin sagging.
  • Fibronectin is an adhesion protein that connects cells with collagen in the dermal layer of the skin in a normal state and has been reported to be a mediator that is involved in the migration, proliferation or differentiation of cells and transmits intracellular and extracellular signals. Fibronectin is found in all vertebral animals and is a dimer consisting of two subunits.
  • pFN soluble plasma Fn
  • cFN cellular Fn
  • fibronectin shows various biological functions, including the promotion of cell adhesion and elongation, the promotion of cell migration, the regulation of cell differentiation and the restoration of tissue, by binding either to an integrin receptor, a glycoprotein which is expressed on the cell surface and consists of two subunits, ⁇ and ⁇ , or to a non-integrin receptor (Couchman JR, et al., Fibronectin-cell interactions. J. I. D. 1990; 94: 7s-14s; Hynes RO, et al., Fibronectin; multifunctional modular glycoprotein. J. cell boil., 1982; 92; 369-377).
  • cathepsin G has a molecular of about 30 kDa, and as substrates of cathepsin G, collagen and fibronectin have been reported.
  • cathepsin G is predominantly expressed in lesion sites such as atopy, and it is not present in the epidermis and is expressed at high levels in the dermis and the like.
  • typical in vitro screening methods for developing anti-aging substances include a method comprising irradiating skin cells with UV light and then treating the UV-irradiated skin with a candidate substance in order to inhibit the expression of metalloproteinase, and a method comprising treating normal skin fibroblasts with substances and then screening a substance increasing the production of collagen.
  • a method comprising irradiating skin cells with UV light and then treating the UV-irradiated skin with a candidate substance in order to inhibit the expression of metalloproteinase
  • a method comprising treating normal skin fibroblasts with substances and then screening a substance increasing the production of collagen.
  • the expression and activity of metalloproteinase are increased due to various factors such as inflammatory factors, in addition to direct factors such as UV light, and thus said methods are unsuitable for screening anti-aging substances against such various factors .
  • the present inventors have investigated a method of inhibiting rapid skin aging caused by UV light and of effectively controlling intrinsic aging and, as a result, have found that the degradation products of a cell adhesion protein (fibronectin) promotes the expression of metalloproteinase in skin cells and that cathepsin G is involved in the degradation of the adhesion protein. Also, the present inventors have found that a cathepsin G inhibitor, obtained through cathepsin G inhibitor screening, has the effect of inhibiting the activity of cathepsin G and the anti-aging effect of preventing the degradation of the adhesion protein to inhibit the production of metalloproteinase in skin cells.
  • fibronectin cell adhesion protein
  • the present inventors have found that the use of a skin external composition containing a cathepsin G inhibitor can prevent the adhesion protein from being degraded due to intrinsic aging and photoaging, reduce the production of metalloproteinase and inhibit the activity of metalloproteinase, and thus anti-aging substance more potent than the existing anti-aging substances can be developed, thereby completing the present invention.
  • Another object of the present invention is to provide a skin external composition for preventing skin aging, which contains a cathepsin G inhibitor as an active ingredient .
  • Another object of the present invention is to identify the function of cathepsin G and to provide a screening method capable of developing anti-aging substances, which effectively inhibit the quantitative and qualitative increase of metalloproteinase, resulting from the degradation of an adhesion protein by cathepsin G in skin cells without direct UV irradiation.
  • the present inventors have found that an enzyme degrading the adhesion protein is cathepsin G and that, when cells were treated with ISMD 38 as a cathepsin G inhibitor, the expression and activity of metalloproteinase in the cells were significantly decreased.
  • an enzyme degrading the adhesion protein is cathepsin G and that, when cells were treated with ISMD 38 as a cathepsin G inhibitor, the expression and activity of metalloproteinase in the cells were significantly decreased.
  • the present invention provides a skin external composition for preventing skin aging, which contains a cathepsin G inhibitor as an active ingredient. Also, the present invention aims to identify the functions of cathepsin G and provides a screening method capable of developing anti-aging substances, which effectively inhibit the quantitative and qualitative increase of metalloproteinase, resulting from the degradation of an adhesion protein by cathepsin G in skin cells without direct UV irradiation. [Advantageous Effects]
  • the cathepsin G inhibitors prevents the degradation of fibronectin to inhibit the production of metalloproteinase in skin cells so as to the quantitative and qualitative changes of metalloproteinase, resulting from enzymes in the skin in addition to the direct effect of UV light, thus reducing wrinkles which are skin aging conditions.
  • the cathepsin G inhibitor has the effect of inhibiting the activity of metalloproteinase, it can contribute to the reduction of skin wrinkles and the improvement of skin elasticity, and thus can be used as an effective substance in the future development of cosmetic materials for inhibiting skin aging.
  • the antiaging substances can be screened by adding an anti-aging candidate substance to a substrate in the presence of cathepsin G enzyme and measuring the inhibition of activity of the cathepsin G enzyme on the basis of the concentration of metalloproteinase produced.
  • FIG. 1 is a flowchart showing a process in which wrinkles are increased due to the activity of cathepsin G in aged skin.
  • FIG. 2 illustrates a graphic diagram showing an increase in the activity of cathepsin G in aged cells and UV-irradiated cells, measured in Test Example 1, and illustrates immunofluorescence photographs showing the comparison of cathepsin G between young skin and aged skin.
  • FIG. 3 is a graphic diagram showing the expression levels of metalloproteinase (MMP-I) by the degradation products of fibronectin, measured in Test Example 2.
  • MMP-I metalloproteinase
  • FIG. 4 shows the results of Western blot analysis conducted to identify a fibronectin-degrading enzyme in Test Example 3.
  • FIG. 5 shows the results of Western blot analysis conducted to examine the degradation of fibronectin in human fibroblast cells in Test Example 3.
  • FIG. 6 shows the results of Western blot analysis conducted to examine the quantitative change of fibronectin in human fibroblast cells in Test Example 3.
  • FIG. 7 is a graphic diagram showing the inhibition of cathepsin G activity, measured in Test Example 4.
  • FIG. 8 shows the results of Western blot analysis conducted to examine the inhibition of expression of MMP-I by ISMD 38 in Test Example 5.
  • FIG. 9 is a graphic diagram showing wrinkle measurement results, obtained in hairless mice as photoaging animal models in Test Example 6.
  • Rl deep wrinkles
  • R2 thin wrinkles
  • R3 middle between deep wrinkles and thin wrinkles
  • R4 weak roughness of skin surface
  • R5 strong roughness of skin surface.
  • the cathepsin G inhibitor is characterized in that it prevents the degradation of adhesion protein fibronectin to inhibit the production of metalloproteinase, which is the degradation product of fibronectin, a collagen-degrading enzyme, in skin cells.
  • metalloproteinase which is the degradation product of fibronectin, a collagen-degrading enzyme
  • FIG. 1 when the activity of cathepsin G enzyme in aged skin is increased, a cell adhesion protein will be rapidly degraded so as to increase the expression and activity of metalloproteinase, which is the degradation product of the adhesion proteins, thus increasing wrinkles.
  • the cathepsin G inhibitor according to the present invention is selected from among compounds represented by the following formulas 1 to 4 and is preferably contained in an amount of 0.01-10 wt% based on the total weight of the skin external composition: [Formula 1]
  • the compounds represented by the formulas 1 to 4 are contained in an amount of less than 0.01 wt% based on the total weight of the skin external composition, the effect of inhibiting the cathepsin G enzyme cannot be obtained, and if it is contained in an amount of more than 10 wt%, the skin external composition can be deteriorated, it will be difficult to control the viscosity of the skin external composition, and the economic efficiency will be reduced.
  • the compounds of the formulas 1 to 4 are derivatives of 3 , 5-dihydroxybenzoic acid and are known not only to have the effect of inhibiting elastase, but also to effectively eliminate free radicals produced by UV light.
  • the inventive skin external composition for preventing skin aging is used to increase the adhesion of skin cells and to prevent the degradation of the adhesion protein, thus inhibiting an increase in skin wrinkles, increasing skin elasticity and preventing the skin from sagging, and there is no particular limitation on the formulation of the composition.
  • the skin external composition of the present invention can be formulated into a cosmetic formulation, such as skin lotion, astringent lotion, milk lotion, nourishing cream, essence, massage cream, eye cream, pack, body lotion, body cream, body oil or body essence, or a transdermal formulation, such as lotion, ointment, gel, cream, patch or spray.
  • inventive skin external composition for preventing skin aging may contain, in addition to the cathepsin G inhibitor, other components which can increase the main effect of the present invention, within a range not to impair the main effect of the present invention.
  • the method for screening the anti-aging substance cathepsin G inhibitor showing the effect of inhibiting the degradation of the adhesion protein is performed by adding an anti-aging candidate substance to a substrate in the presence of cathepsin G enzyme and measuring the inhibition of activity of the cathepsin G enzyme, in which the inhibition of activity of the cathepsin G enzyme can be determined by measuring the concentration of metalloproteinase produced by the degradation of the adhesion protein.
  • Test Example 1 (a) change in activity of cathepsin G in aged skin cells and UV- irradiated skin cells and (b) change in activity of cathepsin G in young skin and aged skin
  • the activities of cathepsin G in young cells, a culture medium of fibroblasts intrinsically aged through passage cultures (38 passages) and a culture medium of fibroblasts irradiated three times with UV light were measured.
  • the measurement of the activities was performed by reacting 80 ⁇ g of each of culture medium proteins with 2 mM cathepsin G substrate (Suc-AAPF-pNA) in buffer solution (HEPES; pH 7.5), and then measuring the absorbance at 405 nm showing yellow color development due to the release of p-nitroaniline (pNA) from the substrate by cathepsin G.
  • human skin fibroblasts were treated with the fibronectin degradation products 2, 3 and 4 (Fn-f70, Fn-f45 and Fn-f30; 70 kDa, 40 kDa and 30 kDa) having no toxicity, and the expression levels of metalloproteinase in the fibroblasts were measured with an ELISA kit.
  • human fibroblasts were placed in a 6-well microtiter plate containing 10% fetal bovine serum-containing DMEM media (fibroblast growth media), at a cell density of 10,000 cells/well. After cell adhesion, the media were replaced with fetal bovine serum-free media, and the cells were cultured to a confluency of about 70-80%.
  • the cells were treated with the fibronectin degradation products at the concentrations shown in Table 1 below, and after 2 days, the number of viable cells was measured to analyze the toxicities of the degradation products for skin cells and to compare the quantitative change of matrix metalloproteinase (hereinafter, referred to as "MMP-I").
  • MMP-I matrix metalloproteinase
  • a group untreated with the degradation products of cell adhesion protein fibronectin was used as a control group.
  • the test results are shown in Table 1 and FIG. 3 as ratios relative to the control group taken as 100. [Table l]
  • the fibronectin degradation products increased the amount of metalloproteinase in skin fibroblasts. As shown in FIG. 3, such results were increased by a maximum of 50% compared to the case irradiated with UVB.
  • the degradation products of fibronectin are reported to increase the expression of metalloproteinase in joint cells, but were not reported in skin cells. Accordingly, it can be predicted through the results in FIG. 3 that the fibronectin degradation products are important aging factors that promote skin aging by increasing metalloproteinase.
  • Test Example 3 Identification of fibronectin- degrading enzyme and increase in expression of metalloproteinase
  • a fibronectin-degrading enzyme In order to identify a fibronectin-degrading enzyme, 0.5 ⁇ g of a fibronectin protein was allowed to react with 1.5 mU of cathepsin G in an eppendorf tube at 37 ° C for 24 hours, and then the degradation of fibrobectin was observed by Western blot analysis in comparison with the case in which cathepsin G was not added (FIG. 4) .
  • fibroblasts were cultured in a 48 -well microtiter plate at a cell density of 10 4 cells/well, while the media were replaced with media containing 1 mU and 5 mU of cathepsin G. After 24 hours of the culture, the supernatant was collected, and then the degradation of fibronectin in the supernatant was analyzed by Western blot. Then, the expression level of metalloproteinase was observed by Western blot analysis, and the observation results are shown in FIG. 5 in comparison with the case in which cathepsin was not added.
  • MMP-I metalloproteinase
  • FIG. 4 when fibronectin was treated with cathepsin G, various fibronectin degradation products appeared, suggesting that cathepsin G was an enzyme degrading fibronectin. Also, as shown in FIG. 5, when skin cells were treated with cathepsin G, the degradation of fibronectin was observed. From the results in FIG. 6, it could be observed that the amount of metalloproteinase, a fibronectin degradation product, was increased due to the change in the degradation of fibronectin. That is, as can be seen in FIG.
  • cathepsin G was an enzyme promoting the degradation of fibronectin. Also, a band having a size of 42 kDa, which is the size of active metalloproteinase, was observed (FIG. 6) , and thus the size of active metalloproteinase, which was not observed in cells irradiated with UV light, could be observed.
  • cathepsin G the expression of which was promoted in aged skin without UV irradiation. Accordingly, it could be observed that the cathepsin G enzyme promoted the degradation of the cell adhesion protein in skin cells to increase the amount and activity of metalloproteinase.
  • Test Example 4 Cathepsin G activity inhibitory effect and anti-aging substance screening
  • a cathepsin G enzyme In a 96-well microtiter plate, a cathepsin G enzyme, a substrate (Sue-AAPF-pNA) , a candidate substance (ISMD 38) of the present invention or a positive control group (inhibitor; commercially available from Amersham) , shown in Table 2 below, and a buffer solution, were mixed with each other in the amounts shown in Table 3 below so as to make a total volume of 200 ⁇ lt . Then, the mixture was allowed to react at 37 ° C for 3 hours, and then the absorbance at 504 nm was measured in order to examine whether the cathepsin G enzyme had activity.
  • a group, containing only cathepsin G enzyme and substrate was used as a control group. The test results are shown in FIG. 7 as ratios relative to the control group taken as 100. Also, in FIG. 7, if the cathepsin G enzyme had activity, the substrate would be degraded to show a yellow color. [Table 2
  • the positive control group showed an IC 50 at 1 ⁇ M
  • the ISMD 38 of the present invention showed a cathepsin G inhibitory effect of 40% at 10 mM.
  • an anti-aging substance can be screened by adding an anti- aging candidate substance to a substrate and measuring the inhibition of activity of cathepsin G enzyme.
  • Test Example 5 Analysis of inhibition of MMP-I expression by ISMD 38
  • the cells were treated with each of cathepsin G (1 mU) and ISMD 38 (0, 0.1, 1 and 10 ⁇ M) , and after 2 days, the supernatants were collected, and changes in the amounts of metalloproteinase in the supernatants were observed by Western blot analysis.
  • the observation results are shown in FIG. 8.
  • a group untreated with cathepsin G or ISMD 38 was used as a control group.
  • the group treated only with cathepsin G showed increases in the expression and active form of metalloproteinase compared to the group untreated with cathepsin G. This is because cathepsin G degraded the cell adhesion protein to increase the degradation product metalloproteinase.
  • Rl indicates deep wrinkles; R2, thin wrinkles; R3, the middle between deep wrinkles and thin wrinkles; R4 and R5; roughness of skin surface; R4, weak roughness; and R5, strong roughness.
  • ISMD 38 was used alone, it showed the effect of reducing wrinkles (Rl, R2 and R3) .

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  • General Health & Medical Sciences (AREA)
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  • Birds (AREA)
  • Dermatology (AREA)
  • Gerontology & Geriatric Medicine (AREA)
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  • Cosmetics (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
  • Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)

Abstract

L'invention concerne une composition à usage externe pour la peau servant à prévenir le vieillissement de la peau, laquelle contient un inhibiteur de la cathepsine G en tant qu'ingrédient actif. L'invention concerne également un procédé servant à cribler des substances antivieillissement.
PCT/KR2007/005451 2006-11-03 2007-10-31 Composition à usage externe pour la peau contenant des inhibiteurs de la cathepsine g servant à prévenir le vieillissement de la peau et procédé de criblage pour le développement de substances antivieillissement WO2008054144A1 (fr)

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KR20060108513 2006-11-03

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Cited By (4)

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WO2014139965A1 (fr) 2013-03-13 2014-09-18 Unilever Plc Compositions de photoprotection contenant des tricyclodécanes amides
WO2014139963A1 (fr) 2013-03-13 2014-09-18 Unilever Plc Compositions cosmétiques contenant des amides tricyclodécanes
US9775793B2 (en) 2013-03-13 2017-10-03 Conopco, Inc. Prolonged delivery of certain fragrance components from personal care compositions
US9840466B2 (en) 2013-12-09 2017-12-12 Conopco, Inc. Process of making adamantanamides

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CN103585040B (zh) * 2013-10-31 2015-07-22 天津郁美净集团有限公司 抗水性液晶化妆品用乳剂组合物及其应用

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EP0587799B1 (fr) * 1991-05-23 1999-07-07 Merrell Pharmaceuticals Inc. Inhibiteurs de la cathepsine g et de l'elastase empechant la degradation du tissu conjonctif
US6964654B2 (en) * 2002-04-09 2005-11-15 Roy Fanti Disposable cover for drainable stoma pouch
US7022317B2 (en) * 2003-04-25 2006-04-04 L'oreal Heterocyclic derivatives of 2-oxothiazolidine-4-carboxylic acid, and use as active photoprotective agents

Patent Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0587799B1 (fr) * 1991-05-23 1999-07-07 Merrell Pharmaceuticals Inc. Inhibiteurs de la cathepsine g et de l'elastase empechant la degradation du tissu conjonctif
US6964654B2 (en) * 2002-04-09 2005-11-15 Roy Fanti Disposable cover for drainable stoma pouch
US7022317B2 (en) * 2003-04-25 2006-04-04 L'oreal Heterocyclic derivatives of 2-oxothiazolidine-4-carboxylic acid, and use as active photoprotective agents

Cited By (10)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2014139965A1 (fr) 2013-03-13 2014-09-18 Unilever Plc Compositions de photoprotection contenant des tricyclodécanes amides
WO2014139963A1 (fr) 2013-03-13 2014-09-18 Unilever Plc Compositions cosmétiques contenant des amides tricyclodécanes
CN105307632A (zh) * 2013-03-13 2016-02-03 荷兰联合利华有限公司 具有三环癸烷甲酰胺类化合物的光防护组合物
JP2016513630A (ja) * 2013-03-13 2016-05-16 ユニリーバー・ナームローゼ・ベンノートシヤープ トリシクロデカンアミドを有する光保護組成物
US9682028B2 (en) 2013-03-13 2017-06-20 Conopco, Inc. Personal care photoprotective compositions with tricyclodecane amides
US9775793B2 (en) 2013-03-13 2017-10-03 Conopco, Inc. Prolonged delivery of certain fragrance components from personal care compositions
US9883997B2 (en) 2013-03-13 2018-02-06 Conopco, Inc. Cosmetic compositions with tricyclodecane amides
EA029496B1 (ru) * 2013-03-13 2018-04-30 Юнилевер Н.В. Фотозащитные композиции с трициклодеканамидами
EA029547B1 (ru) * 2013-03-13 2018-04-30 Юнилевер Н.В. Косметические композиции с трициклодеканамидами
US9840466B2 (en) 2013-12-09 2017-12-12 Conopco, Inc. Process of making adamantanamides

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KR20080040612A (ko) 2008-05-08

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