EP1221948A2 - Utilisation de compositions pour le traitement curatif de la peau - Google Patents

Utilisation de compositions pour le traitement curatif de la peau

Info

Publication number
EP1221948A2
EP1221948A2 EP00971338A EP00971338A EP1221948A2 EP 1221948 A2 EP1221948 A2 EP 1221948A2 EP 00971338 A EP00971338 A EP 00971338A EP 00971338 A EP00971338 A EP 00971338A EP 1221948 A2 EP1221948 A2 EP 1221948A2
Authority
EP
European Patent Office
Prior art keywords
inhibitor
skin
acid
inhibitors
use according
Prior art date
Legal status (The legal status 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 status listed.)
Withdrawn
Application number
EP00971338A
Other languages
German (de)
English (en)
Inventor
Andrea SÄTTLER
Thomas Förster
Kordula Schlotmann
Albrecht Weiss
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Henkel AG and Co KGaA
Original Assignee
Henkel AG and Co KGaA
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 Henkel AG and Co KGaA filed Critical Henkel AG and Co KGaA
Publication of EP1221948A2 publication Critical patent/EP1221948A2/fr
Withdrawn legal-status Critical Current

Links

Classifications

    • 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
    • A61Q19/007—Preparations for dry skin
    • 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
    • A61K8/37—Esters of carboxylic acids
    • A61K8/375—Esters of carboxylic acids the alcohol moiety containing more than one hydroxy group
    • 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
    • A61K8/46—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds containing sulfur
    • A61K8/466—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds containing sulfur containing sulfonic acid derivatives; Salts
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
    • A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
    • A61K8/645—Proteins of vegetable origin; Derivatives or degradation products thereof
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P17/00—Drugs for dermatological disorders
    • 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
    • A61K2800/74—Biological properties of particular ingredients
    • A61K2800/78—Enzyme modulators, e.g. Enzyme agonists
    • A61K2800/782—Enzyme inhibitors; Enzyme antagonists

Definitions

  • compositions for the care treatment of the skin which contain special bioactive components.
  • Skin care products are products for cleaning and care of the skin, which have the task of gently cleansing the skin, keeping it supple and supporting the skin's natural layer in its natural regenerative capacity. Since the skin is not an isolated organ, but is connected to other layers of tissue in terms of function and structure, the requirements for the composition of a skin care product are very complex.
  • the cells of the homolayer (stratum corneum) on the skin surface are desquamated, while new basal cells are supplied from the stratum.
  • the protein structures (desmosomes) which are responsible for the cohesion of the cells, must be dissolved (A. Lundström, T. Egelrud, J. Invest. Dermatol. 1988, 91, 340-343 and 1990, 94, 216-220; idem, Arch. Dermatol. Res. 1990, 282, 234-237).
  • the desmosomes are broken down by proteases contained in the stratum corneum, two of which have been characterized in more detail. These are serine proteases of the chymotrypsin and trypsin type (T. Egelrud et al., Acta Derm. Venereol. 1991, 71, 471-474; JP 8068791 A2).
  • Dry skin is characterized by increased desmosome structures in the uppermost layers of the stratum corneum (EP 0633765) and also by an increased desquamation of keratinocytes in the epidermis.
  • proteases have therefore been used as bioactive components in skin care products which break down the increased desmosome structures more quickly (WO 95/07688, EP 0 633 765, EP 0 719 132, EP 0 719 133, EP 0 719 134).
  • the use of dicarboxylic acids also leads to an accelerated breakdown of the desmosome structures (JP 10175844).
  • protease inhibitors are used for the treatment of skin diseases and for the pathologically accelerated formation of cells of the epidermis (JP 9025212, JP 9025214, US 5290762, EP 0 532 465).
  • the protease inhibitor trßrn_y-4- (aminomethyl) cyclohexanecarboxylic acid (tranexamic acid, t-AMCHA; cf. JP 9175986) inhibits the so-called tissue-type plasminogen activator (t-PA), a protease that is involved in fibrinolysis and only occurs in the epidermis if there is already an inflammatory complexion (J. Koyama et al., "The mechanism of desquamation in the stratum corneum and its relevance to skin care", Symposium paper No. 9, 19 * IFSCC Congress, Sidney 1996).
  • the components currently used in care products for the treatment of dry skin cannot yet influence the metabolic processes satisfactorily. For example, numerous active substances do not specifically inhibit the proteases involved in the desquamation reaction.
  • the task was to reduce the desquamation of the keratinocytes by targeted bioactive components, which inhibit proteases involved in construction, and in this way to achieve a significantly improved complexion.
  • the invention therefore relates to the use of a composition which contains at least one inhibitor for the proteinases involved in the desmosome degradation in a physiologically compatible carrier which can be distributed on the skin, for topical prophylactic and / or cosmetic treatment of dry skin.
  • Water-soluble inhibitors with a molecular weight of less than 5000 g / mol can be preferred in the sense of the invention, water solubility being understood as meaning a minimal solubility of the inhibitor of 0.001% by weight in 11 water at 25 ° C.
  • Inhibition or inhibition within the meaning of the invention is the decrease in activity (definition of enzyme activity, cf.
  • the inhibitor or the mixture of inhibitors can contain a concentration of 0.001-20.0% by weight, preferably 0.1-5% by weight
  • the physiologically compatible carrier can be, for example, an O / W or a W / O emulsion, a gel base or a suitable aqueous or alcoholic solution.
  • compositions which is characterized in that it contains at least one inhibitor which inhibits the serine pro- inhibiting teinases is preferred.
  • These proteinases contain an L-serine residue which is essential for catalysis in the active center.
  • Suitable inhibitors for the purposes of the invention are substances which modify the L-serine residue and / or block the substrate cleavage site by interaction with the L-serine residue or with amino acids from the environment and / or by changing the tertiary structure of the enzyme cause its inactivation.
  • an inhibitory effect in the sense of the invention is a decrease in the activity of the serine proteinases in the presence of the inhibitor in the vztro test and / or the reduced desquamation of keratinocytes on skin biopsies in the presence of the inhibitor.
  • composition which is characterized in that it contains at least one inhibitor which inhibits the trypsin or chymotrypsin-like serine proteinases involved in the desmosome breakdown.
  • Trypsin is an endopeptidase that arises in the small intestine from the precursor trypsinogen formed by the pancreas by splitting off a hexapeptide.
  • This serine proteinase is characterized by a negatively charged L-aspartate residue in the substrate binding pocket, which also determines the specificity of the enzyme. Trypsin cleaves peptide chains specifically on the carboxy side of the basic amino acids L-lysine and L-arginine.
  • Chymotrypsin arises in the pancreas from inactive precursors, so-called zymogens, through the action of trypsin. Chymotrypsin cleaves proteins, peptides, amino acid esters and amides specifically on the carboxy group of hydrophobic amino acids. Both types of enzyme are involved in the breakdown of protein structures (desmosomes), which are responsible for the cohesion of the horny cells in the skin.
  • An inhibitory effect in the sense of the invention is a decrease in the activity of the trypsin or chymotrypsin-like serine proteinases in the presence of the inhibitor in the -vz ' tro test.
  • boric acid or its derivatives are present as an inhibitor
  • the derivatives which can be used according to the invention include esters and salts of boric acid and C, -C 5 -alkyl- or aryl-substituted boric acid derivatives, such as, for example Phenylboronic acid and / or their mono- or diesters with C, -C 5 alkyl radicals.
  • the use of boric acid acetate or phenylboronic acid acetate can be preferred for the purposes of the invention. Boric acid and phenylboronic acid have a weak antiseptic effect.
  • phenylboronic acid is known as an inhibitor of proteolytic enzymes in order to increase their storage stability.
  • phenylboronic acid C 6 H 5 B (OH) 2
  • phenylboronic acid in the in vitro test in very low concentrations (0.1%) proved to be an extremely effective inhibitor of chymotrypsin, an enzyme which is involved in the breakdown of desmosomes.
  • boric acid and phenylboronic acid (Examples 7 and 8) proved to be inhibitors and are therefore particularly suitable for use in compositions for topical treatment of dry skin.
  • compositions which is characterized in that 4- (2-aminoethyl) phenylsulfonyl fluoride is present as an inhibitor.
  • This inhibitor Two embodiments of this inhibitor are known under the trade name Pefabloc ® and Pefabloc ® SC.
  • the substance is described as a non-toxic, irreversible and effective inhibitor of serine proteases (C. Dentan et al., Biochimica et Biophysica Acta, 1996, 1299, 353-357).
  • the use of 4- (2-aminoethyl) phenylsulfonyl fluoride in compositions for the topical treatment of dry skin is suitable.
  • a composition which is characterized in that a chemical compound containing the pentapeptide sequence glycine-proline-phenylalanine-proline-leucine (GPFPL) is used as the inhibitor.
  • the pentapeptide sequence is known to be an inhibitor of serine proteinases. Claimed in For the purposes of the use according to the invention, end group-protected derivatives of this pentapeptide sequence, polypeptides, proteins and other chemical derivatives which contain this pentapeptide sequence have an inhibitory effect in the tests described overleaf.
  • Rosemary acid is known for its anti-inflammatory, cytostatic and antiviral effects.
  • rosemary acid is used as a bath additive and as an additive in hair care products.
  • rosemary acid is used together with other active ingredients as a synergistic combination of antioxidants.
  • usable derivatives are esters and salts of rosmarinic acid and C r C 5 includes alkyl or aryl esters. Almost complete inhibition of trypsin was observed in z ' w-vz ' tro tests using 0.05% rosemic acid (Example 5). When using 1.0% rosemary acid, the desquamation of the skin can be reduced by almost 70% (Example 11).
  • composition which is characterized in that the Elhibin Leguminosesamen obtained from a special procedure ® (Pentapharm AG) is contained as inhibitor.
  • Elhibin ® inhibits leukocyte elastase and fibroblast elastase, which are involved in inflammatory and aging processes of the skin.
  • the active ingredient is used in skin cosmetics to improve the general appearance of the skin.
  • Elhibin ® almost completely inhibits both trypsin and chymotrypsin in a concentration of 0.5% (Example 6).
  • the desquamation of the corneocytes is reduced by more than 90% when using 1.0% Elhibin ® (Example 12).
  • the inhibitor active ingredients are contained in the physiologically compatible carriers customary for cosmetic formulations.
  • physiologically compatible carriers customary for cosmetic formulations.
  • the composition can be formulated as an aqueous or alcoholic solution, as a gel, oil, W / O or O / W emulsion.
  • the inhibitors can also be used in personal cleansing agents such. B. soaps, shampoos, shower rooms u. ⁇ . Are used because they reduce the desquamation induced by detergents.
  • compositions for topical, prophylactic and / or cosmetic treatment of dry skin.
  • the compositions contain, in addition to the animal and / or vegetable fats and oils, which in many cases also have a care effect, also further care components.
  • a large number of caring active ingredients which can be used for this purpose are known to the person skilled in the art. These include:
  • the fatty alcohols used can be saturated or unsaturated and linear or branched.
  • the fatty alcohols are preferably derived from natural fatty acids, and it can usually be assumed that they are obtained from the esters of the fatty acids by reduction.
  • Fatty alcohol cuts can also be used according to the invention, which can be obtained by reducing naturally occurring fats and oils, such as. B. beef tallow, peanut oil, rape oil, cottonseed oil, soybean oil, sunflower oil, palm kernel oil, linseed oil, castor oil, corn oil, rapeseed oil, sesame oil, cocoa butter and coconut oil.
  • Vitamin and vitamin precursors such as tocopherols, vitamin A, niacic acid and niacic acid amide, other vitamins of the B complex, vitamin F and especially biotin.
  • panthenol also preferred within this group of caring active ingredients are panthenol, its derivatives, in particular the esters and ethers of panthenol, and cationically derivatized panthenols. Individual representatives are, for example, panthenol triacetate, panthenol monoethyl ether and its monoacetate and cationic panthenol derivatives.
  • Mono-, di- and oligosaccharides such as glucose, galactose, fructose, mannose, fructose and lactose.
  • Plant extracts which are usually produced by extracting the entire plant, but in some cases also exclusively from flowers and / or leaves of the plant.
  • Plant extracts are particularly referred to the extracts that are listed in the table beginning on page 44 of the 3rd edition of the Guide to the Declaration of Ingredients for Cosmetics, published by the Industrie diagramischen- und Waschstoff eV (IKW), Frankfurt.
  • the extracts from almond, aloe vera, coconut, mango, apricot, lime, wheat, kiwi and melon are particularly preferred. Mixtures of several, in particular two, different plant extracts can also be present in the agents according to the invention.
  • the plant extracts mentioned As an extractant for the production of the plant extracts mentioned, u. a. Water, alcohols and mixtures thereof can be used. Among the alcohols, lower alcohols such as ethanol and isopropanol, but especially polyhydric alcohols such as ethylene glycol, propylene glycol and butylene glycol are preferred both as the sole extracting agent and in a mixture with water. According to the invention, the plant extracts can be used both in pure and in diluted form.
  • Honey extracts which are obtained in an analogous manner to the plant extracts and usually contain 1-10% by weight, in particular 3-5% by weight, of active substance.
  • Phospholipids for example soy lecithin, egg lecithin and cephalins, • paraffin and silicone oils; the latter include dialkyl and alkylarylsiloxanes, such as dimethylpolysiloxane and methylphenylpolysiloxane, and their alkoxylated and quaternized analogs.
  • Fatty acid and fatty alcohol esters especially the monoesters of fatty acids with alcohols with 3 to 24 carbon atoms.
  • This group of substances concerns the products of the esterification of fatty acids with 8 to 24 carbon atoms such as, for example, caproic acid, caprylic acid, 2-ethylhexanoic acid, capric acid, lauric acid, isotridecanoic acid, myristic acid, palmitic acid, palmoleic acid, stearic acid, isostearic acid, oleic acid, elaidic acid, Petroselinic acid, linoleic acid, linolenic acid, elaeostearic acid, arachic acid, gadoleic acid, behenic acid and casa acid and their technical mixtures, which, for.
  • the serine proteases trypsin and chymotrypsin (Sigma) from bovine pancreas served as a model enzyme for the inhibitory effect of the inhibitors phenylboronic acid, boric acid, N-CBZ-Gly-Pro used according to the invention -Phe-Pro-Leu, Pefabloc ® and Pefabloc ® SC (Boehringer Mannheim), rosemary acid and Elhibin ® to be tested.
  • the t-AMCHA [tr ⁇ «s-4 (ammomethyl) -cyclohexane carboxylic acid] known as a t-PA inhibitor (tissue-type 7 lasminogen activator) was used as a reference.
  • the detection of the chymotrypsin enzyme activity is carried out with a modification analogous to the information in the Sigma Quality Control Test Procerfwre data sheet for chymotrypsin.
  • 1.32 ml of reagent A were added to the test batch, and 0.1 ml of a solution of the corresponding inhibitor in reagent A (concentration series).
  • the enzyme activity was determined spectrophotometrically by converting the substrate N-benzoyl-L-tyrosine ethyl ester (BTEE) to N-benzoyl-L-tyrosine and ethanol.
  • the absorption of the proteolytically cleaved N-benzoyl-L-tyrosine is measured at 256 nm.
  • the detection of trypsin enzyme activity is also carried out with a modification analogous to the information in the Sigma Quality Control Test rocedwre data sheet for trypsin.
  • aprotinin Reagent F
  • the inhibitors according to the invention were used here. A series of concentrations of the inhibitors in reagent E was set up for this. The enzyme activity was spectrophotographically converted from N ⁇ -benzoyl-DL-arginine-p-nitroaniline (BAPNA) to N ⁇ -benzoyl-DL-arginine and p-nitroaniline. determined metrically. The absorption of the proteolytically cleaved p-nitroaniline is measured at 405 nm.
  • BAPNA N ⁇ -benzoyl-DL-arginine-p-nitroaniline
  • the reaction kinetics were detected for 5 minutes at 25 ° C., the linear increase in absorption (A) per unit time (t) being a measure of the activity of the enzyme ( ⁇ A / ⁇ t).
  • the activity of the enzyme in the absence of a proteinase inhibitor, ( ⁇ A, / ⁇ t,) was set to 100%.
  • the activities in the presence of an inhibitor ( ⁇ A 2 / ⁇ t 2 ) were determined under analogous conditions.
  • the inhibitory effect or reduction of the enzyme activity then corresponds to: 100% - ( ⁇ A 2 / ⁇ t 2 ) / ( ⁇ A, / ⁇ t,)%.
  • Phenylboronic acid only moderately affects the activity of trypsin in the selected concentration range. In contrast, a clear, concentration-dependent inhibition of chymotrypsin is observed.
  • Example 2 Boric acid as an inhibitor in the enzyme test
  • the inhibitory effect of boric acid on trypsin and chymotrypsin is only weak in the tested concentration range. Chymotrypsin is inhibited more than trypsin at a lower boric acid concentration.
  • Example 3 4- (2-aminoethyl) phenylsulfonyl fluoride (Pefabloc * 1 SC) as an inhibitor in the enzyme set
  • Pefabloc ® SC shows a strong, concentration-dependent inhibition of trypsin and chymotrypsin in the tested concentration range.
  • Example 4 Pentapeptide sequence GPFPL as an inhibitor in the enzyme test
  • Trypsin activity is not affected by GPFPL in the selected concentration range. A specific inhibition (27%) of chymotrypsin is detected at a concentration of the inhibitor of 0.33% by weight.
  • Rosemary acid shows a strong, concentration-dependent inhibition of trypsin. The inhibition of chymotrypsin is low at the investigable, low inhibitor concentrations.
  • Example 6 Elhibin ® as an inhibitor in the enzyme test
  • test results show that the reference inhibitor t-AMCHA (comparative example 1) only inhibits trypsin in the concentration range investigated and thus differs fundamentally from the inhibitors used according to the invention. Some of the inhibitors tested here achieve effective inhibition at very low concentrations.
  • 8mm 2 pieces of skin were punched out from fresh human skin explants (from breast reduction) and treated with a mixture of detergents (Na-dodecyl sulfate, N, N-dimethyldodecylamine oxide) in the absence and in the presence of the inhibitors.
  • a mixture of detergents Na-dodecyl sulfate, N, N-dimethyldodecylamine oxide
  • the number of desquamated horn cells was determined under the microscope in a Schilling counting chamber. A decrease in the number of corneocytes indicates an inhibitory effect of the potential inhibitors tested.
  • the inhibitors were set up in the appropriate concentrations (see tables in Examples 7-12) in the incubation buffer. This consisted of 0.1 M TRIS-HCl buffer (pH 8) with 0.1% by weight Na azide and the detergents Na dodecyl sulfate (0.2 mM) and N, N-dimethyldodecylamine oxide (8 mM) and EDTA (5 mM). These incubation buffer solutions with varying concentrations of the inhibitor are referred to below as test solutions.
  • the human skin was transported in a dry, sterile petri dish on cold packs. After removal of the subcutaneous fat and connective tissue, 8 mm 2 pieces of skin were prepared using sterile punches. These were washed in sterile, physiological NaCl (0.9%) for 15-20 minutes, added to the reaction batches (1 skin piece / reaction batch) and incubated at 37 ° C. for 44 hours. After the incubation phase had ended, the reaction vessels were shaken on a vortex mixer for 30 seconds in order to detach loosely adhering Komeozyten from the skin pieces. The skin pieces were removed and the remaining dispersion was centrifuged for 8 minutes at 11,000 rpm to isolate the coma cells.
  • Phenylboronic acid was tested in various concentrations as a desquamation inhibitor.
  • the corneocyte count of the positive control was set to 100%.
  • phenylboronic acid can significantly reduce the desquamation of the comateocytes.
  • Boric acid was tested in various concentrations as a desquamation inhibitor.
  • the positive control komeocyte value was set to 100%.
  • boric acid can halve the desquamation of the comate cells.
  • the pentapeptide N-CBZ-Gly-Pro-Phe-Pro-Leu was tested in various concentrations as a desquamation inhibitor.
  • the positive control komeocyte value was set to 100%.
  • Rosemary acid was tested in various concentrations as a desquamation inhibitor.
  • the positive control komeocyte value was set to 100%.
  • Rosmarinic acid also causes a concentration-dependent reduction in desquamation. When using 1.0% rosemary acid, the desquamation can be reduced to 33.8%.
  • Example 12 Elhibin ® as an inhibitor in the desquamation test
  • Elhibin ® has been tested in various concentrations as a desquamation inhibitor.
  • the positive control komeocyte value was set to 100%.
  • T-AMCHA was used as the reference substance.
  • the positive control komeocyte value was set to 100%.
  • the desquamation of the human skin caused by the detergent mixture can be drastically reduced by phenylboronic acid, boric acid, the pentapeptide Z-Gly-Pro-Phe-Pro-Leu, rosemary acid and Elhibin®. Concentration-dependent effects were shown, ie the corneocyte desquamation decreases with an increase in the inhibitor concentration.
  • phospholipid e.g. Sternprime ® N10
  • preservative e.g. Phenonip ®
  • cross-linked polyacrylate e.g. Carbopol ® ETD 2020
  • the liposome gel was formulated with N-CBZ-GPFPL, Pefabloc ® , Pefabloc ® SC, phenylboronic acid, boric acid, rosemic acid and Elhibin ® (0.2% by weight) as an inhibitor.
  • dicaprylyl ether e.g. Cetiol ® OE
  • dioctylcyclohexane e.g. Cetiol ® S
  • cetearyl alcohol e.g. Lanette ® O
  • ceteareth-20 e.g. Eumulgin ® B2
  • glyceryl palmitate e.g. Monomuls ® 60-35C
  • silicone oil e.g. Baysilon ® M 350
  • preservative e.g. Phenonip ®
  • the oil-in-water cream PIT was treated with N-CBZ-GPFPL, Pefabloc ®, ® Pefabloc SC, phenylboronic, boric acid, rosmarinic acid and Elhibin ® (0.2 wt.%) Formulated as an inhibitor.
  • an emulsion concentrate was prepared by the phase inversion process (PIT) (T. Förster in Surfactants in Cosmetics, ed .: MM Rieger and LD Rhein, Marcel Dekker, New York 1997, Vol. 2, pp. 105-125, "Principles of emulsion formation ”) is between 70 and 84 ° C.
  • PIT phase inversion process
  • the hot emulsion concentrate was cooled and the inhibitor was added at 40 ° C. in the form of a 5% strength aqueous solution.
  • dicaprylyl ether e.g. Cetiol ® OE
  • decyl oleate e.g. Cetiol ® V
  • preservative e.g. Phenonip ®
  • the oil constituents were heated to 40 ° C. together with the emulsifier and the aqueous solution of the further ingredients was added with stirring.
  • PEG-7-glyceryl cocoate Manufacturer Henkel KGaA

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  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Animal Behavior & Ethology (AREA)
  • General Health & Medical Sciences (AREA)
  • Public Health (AREA)
  • Veterinary Medicine (AREA)
  • Epidemiology (AREA)
  • Birds (AREA)
  • Dermatology (AREA)
  • Engineering & Computer Science (AREA)
  • Emergency Medicine (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Chemical & Material Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • General Chemical & Material Sciences (AREA)
  • Medicinal Chemistry (AREA)
  • Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
  • Organic Chemistry (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Cosmetics (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)

Abstract

Selon l'invention, on obtient un potentiel extrêmement prometteur pour le traitement topique de la peau sèche en utilisant des compositions qui contiennent, dans un support physiologiquement toléré pouvant être réparti sur la peau, des inhibiteurs des protéinases impliquées dans la dégradation des desmosomes. Ces inhibiteurs contribuent de façon significative à la réduction des processus de desquamation et améliorent ainsi l'aspect de la peau. Les inhibiteurs concernés sont, par exemple, l'acide borique et ses dérivés, le fluorure de 4-(2-amino-éthyl)phénylsulfonyle (Pefabloc® et Pefabloc® SC), la séquence pentapeptidique glycine-proline-phénylalanine-proline-leucine et des dérivés qui contiennent cette séquence pentapeptidique, ainsi que l'acide de romarin et le principe actif de Elhibin® extrait de graines de légumineux.
EP00971338A 1999-10-16 2000-10-07 Utilisation de compositions pour le traitement curatif de la peau Withdrawn EP1221948A2 (fr)

Applications Claiming Priority (3)

Application Number Priority Date Filing Date Title
DE19950020 1999-10-16
DE19950020A DE19950020A1 (de) 1999-10-16 1999-10-16 Verwendung von Zusammensetzungen zur pflegenden Behandlung der Haut
PCT/EP2000/009833 WO2001028536A2 (fr) 1999-10-16 2000-10-07 Utilisation de compositions pour le traitement curatif de la peau

Publications (1)

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EP1221948A2 true EP1221948A2 (fr) 2002-07-17

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EP00971338A Withdrawn EP1221948A2 (fr) 1999-10-16 2000-10-07 Utilisation de compositions pour le traitement curatif de la peau

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Country Link
EP (1) EP1221948A2 (fr)
AU (1) AU1022501A (fr)
DE (1) DE19950020A1 (fr)
WO (1) WO2001028536A2 (fr)

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FR2842209B1 (fr) 2002-07-09 2007-11-23 Nouvelle protease aspartique dite saspase et son utilisation dans le domaine cosmetique et therapeutique
EP1398019A1 (fr) * 2002-09-13 2004-03-17 Cognis France S.A. Procédé pour protéger et moduler la jonction dermo-épidermique
CA2552242C (fr) * 2004-01-07 2010-03-30 E-L Management Corporation Composition cosmetique contenant une proteine et un inhibiteur d'enzyme
FR2932087B1 (fr) * 2008-06-10 2012-10-12 Oreal Utilisation cosmetique de proteines de type desmoplakine pour le traitement de la secheresse cutanee

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WO2001028536A3 (fr) 2002-01-24
WO2001028536A2 (fr) 2001-04-26
DE19950020A1 (de) 2001-04-19
AU1022501A (en) 2001-04-30

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