EP0403530A1 - Lagerstabile zusammensetzungen und verfahren zur behandlung von keratinhaltigen geweben - Google Patents

Lagerstabile zusammensetzungen und verfahren zur behandlung von keratinhaltigen geweben

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Publication number
EP0403530A1
EP0403530A1 EP89903327A EP89903327A EP0403530A1 EP 0403530 A1 EP0403530 A1 EP 0403530A1 EP 89903327 A EP89903327 A EP 89903327A EP 89903327 A EP89903327 A EP 89903327A EP 0403530 A1 EP0403530 A1 EP 0403530A1
Authority
EP
European Patent Office
Prior art keywords
weight
agents
reducing agent
antioxidant
composition 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Withdrawn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
EP89903327A
Other languages
English (en)
French (fr)
Other versions
EP0403530A4 (en
Inventor
John Rothman
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.)
Ciro's Touch Ltd
Original Assignee
Ciro's Touch Ltd
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Filing date
Publication date
Application filed by Ciro's Touch Ltd filed Critical Ciro's Touch Ltd
Publication of EP0403530A1 publication Critical patent/EP0403530A1/de
Publication of EP0403530A4 publication Critical patent/EP0403530A4/en
Withdrawn legal-status Critical Current

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Classifications

    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q3/00—Manicure or pedicure preparations
    • 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
    • A61K8/19—Cosmetics or similar toiletry preparations characterised by the composition containing inorganic ingredients
    • A61K8/22—Peroxides; Oxygen; Ozone
    • 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
    • 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
    • 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
    • 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
    • A61K8/65—Collagen; Gelatin; Keratin; Derivatives or degradation products thereof
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q7/00—Preparations for affecting hair growth

Definitions

  • This invention relates to novel storage stable activated protein containing compositions comprising reducing agents, oxidizing agents and/or anti-oxidants.
  • the composi ⁇ tions are useful for conditioning horny keratinous tissue of mammals such as human hair and nails, and the hooves and fur of animals to improve their strength and appearance. In addi ⁇ tion, these compositions are useful for promoting hair growth.
  • compositions which are useful for promoting the growth of normal dermal and epidermal tissue more specifically the compositions are use ⁇ ful to promote wound healing in the soft keratinous tissue of the epidermis.
  • wound healing are provided in the specification.
  • compositions of the prior patent are described as containing defined percentages of thioglycollic acid, ammonium hydroxide, glycerine, citric acid, hydrogen peroxide, commer ⁇ cial gelatin, a lower alkanol, and a solvent such as acetone or diethyl ether.
  • the commercial grade gelatins disclosed by the patent contain do not contain sufficient cysteinyl content for use in the present invention.
  • the reducing step is believed to break the disulfide bonds of cystine disulfide bridges in the hair to form sulfh dryl groups.
  • the hair is shaped under tension or pres ⁇ sure in the presence of the reducing agent.
  • the oxidizing agent is contacted with the hair while it is still under tension to oxidize the sulfhydryl groups and reform disulfide bonds with the hair in the new shape.
  • U.S. Patent 3,842,848 describes a method of bonding especially prepared hydrolyzed peptide products of keratinaceous materials to human hair. The process is effected by conducting the reducing step of permanent waving in the presence of the peptide products and, thereafter, in a second step, oxidizing.
  • activated protein com ⁇ positions which are used to chemically bond to hair and other horny keratinous tissue may be formulated with reducing agents, oxidizing agents and/or anti-oxidant components to produce compositions for treating horny keratinous tissue.
  • reducing agents, oxidizing agents and/or anti-oxidant components to produce compositions for treating horny keratinous tissue.
  • Especially advantageous characteristics of these compounds include storage stability and the ability to effectuate a reduction and oxidation process to form covalent disulfide linkages without having to resort to two separate solutions.
  • the essential ingredients of the compositions of this invention are the reducing agent, the oxidizing agent, the protein and/or the antioxidant.
  • additional com ⁇ ponents may also be included, for example water, bases, acids, buffering agents, emulsifying agents or surfactants, thick ⁇ eners, preservatives, coloring agents and perfuming agents.
  • compositions of the present invention may be formulated in such a way that activated proteinaceous material in combination with reducing agent and oxidizing agent may produce a composition which can activate natural keratinous tissue and bind activated protein to the activated natural keratinous tissue.
  • compositions of the present invention are aqueous compositions having a pH of from about 4.0 to about 9, preferably a pH of about 7 to about 8, and most preferably a pH of about 7.6 (physiological pH) .
  • Compositions of the pres ⁇ ent invention may comprise a reducing agent, an activated protein, and an oxidizing agent, in addition to other less essential components.
  • Other embodiments of the present inven ⁇ tion may comprise a reducing agent, an activated protein, and an antioxidant.
  • the compositions containing an antioxidant may also contain an oxidizing agent. In those compositions where an anti-oxidant is used in combination with an oxidizing agent, it is preferred that the antioxidant used is a volatile antioxidant and the oxidizing agent used is a non-volatile oxidizing agent.
  • the protein used is an activated protein.
  • An activated protein is a protein which has been subjected to a reducing agent, for example a thiol-containing compound, which results in the breaking of disulfid bonds of cystine residues within the protein structure to produce free thiol or mercap- tide groups on cysteine residues.
  • a reducing agent for example a thiol-containing compound
  • the ability of a protein to bind to native keratin is believed to be related in part to the number of thiol or mercaptide groups on the protein which are free to bind to mercaptide or thiol groups on the native keratin.
  • compositions of the present inven ⁇ tion may react with and form chemical bonds with the hard keratin of human and animal hair, nails and skin, thus effect ⁇ ing decreased hair breakage, increased hair thickness, increased nail hardness, decreased nail splitting and delamination and attachment of moist hydrated proteins to skin.
  • the compositions are therefore useful for treating human hair, nails and skin to chemically bond the activated protein.
  • compositions of the present invention are useful to promote wound healing in mammals.
  • the composi ⁇ tions may also function as topical pharmaceutical carriers and vehicles»
  • the amount of activated protein that bonds to the keratinous tissue will vary with the concentration of reducing agents in the composition and the number of activated thiol or mercapto groups in the activated protein and the keratinous tissue.
  • the time that the reducing agent is in contact with the keratinous tissue is also important; the longer the keratinous tissue is in contact with the reducing agent, the greater will be likelihood of a protein-keratinous tissue covalent bond formation.
  • compositions of the present inven ⁇ tion is preferably initially conducted at ambient tempera ⁇ tures, i.e., about 20'C to about 35°C; however, higher temperatures may be used.
  • the keratinous tissue may be treated over a period of time ranging from about 10 minutes to about 6 hours.
  • the compositions of the present invention may also be formulated as sustained or controlled release formula ⁇ tions for prolonging treatment beyond 6 hours. Reaction" is effected by bringing the compositions of the present invention into contact with the keratinous substrate to be treated and allowing the treated tissue to dry. The time of contact may be varied at will.
  • compositions may employ non-volatile oxidizing agents which may promote oxidation after the volatile antioxidants are removed from the formulations.
  • exemplary embodiments comprise about 0.01 to about 12.0% by weight of an activated protein component, about 0.1 to about 15% by weight of a compatible reducing agent, about 0.001 to about 4.0% by weight of an oxidizing agent, and at least one component selected from the group consisting of water, acids, bases, buffering agents, emulsifying agents or surfactants, thick ⁇ eners, preservatives, organic solvents, coloring agents and perfuming agents.
  • compositions may include an anti-oxidant instead of an oxidizing agent.
  • exemplary compositions comprise about 0.01 to about 12.0% by weight of an activated protein component, about 0.1 to about 15% by weight of a compatible reducing agent, about 0.01 to about 2.0% by weight of an antioxidant and at least one com ⁇ ponent selected from the group consisting of water, acids, bases, buffering agents, emulsifying agents or surfactants, thickeners, preservatives, organic solvents, coloring agents, preservatives and perfume agents.
  • Additional embodiments of the present invention com ⁇ prise about 0.01% to about 12.0% by weight of an activated protein component, about 0.1 to about 15% of a compatible reducing agent, about 0.001 to about 4.0% by weight of an oxidizing agent and about 0.01 to about 4.0% by weight of antioxidant, preferably a volatile antioxidant and at least one component selected from the group consisting of water, acids, bases, buffering agents, solvents, emulsifying agents or surfactants, thickeners, coloring agents, preservatives and perfume agents.
  • compositions of the present invention are for ⁇ mulated to enhance the formation of free mercaptide or thiol groups in the protein and the keratinous tissue to maximize the probability that a free thiol in the protein and a free thiol in the keratinous tissue will form a covalent disulfide bond.
  • the inclusion of an oxidizing agent in the same com ⁇ position as the reducing agent and activated protein is designed to maximize covalent disulfide formation without using a second oxidizing solution.
  • compositions of the present invention may be for ⁇ mulated as gels, creams, lotions, sprays or liquids of varying viscosities.
  • exemplary compositions are comprised of an activated protein, a com ⁇ patible reducing agent, an oxidizing agent and at least one component selected from the group consisting of water, bases, acids, buffering agents, emulsifying agents or surfactants, thickeners, preservatives, organic solvents, coloring agents and perfuming agents.
  • the activated protein comprises about 0.01 to about 12% by weight of the composition, preferably about 1.0 to about 5.0% by weight for certain formulations and about 6 to 10% by weight for other applications where more concentrated formulations are found to be advantageous.
  • Activated proteins for use in compositions of the present invention are preferably exemplified by proteins which have sufficient cysteinyl content, i.e., at least about 1 cysteine amino acid for every 200 amino acids in a peptide chain (approximately, at least about 0.5% by weight cysteine, preferably, at least about 1.0% by weight cysteine and most preferably, at least about 5% by weight cysteine) to covalently bind to the keratinous tissue of hair, skin and nails to produce a durable permanent bond to keratinous tis ⁇ sue.
  • permanent bond we mean that the protein is not easily washed or rubbed off from the keratinous tissue and becomes as permanent as normal hair and nails.
  • exemplary proteins may be used in the present invention and include keratin, food proteins, for example, casein, alpha and beta-lactalbumin, seed proteins, for example, soybean proteins, linseed protein, cotton seed protein, corn protein and peanut protein, among others, hemogrlobin, insulin, myosin, zein, ovalbumin, hemoglobin, trypsin, chymotrypsin, chymotrypsinogen, elastases, thrombins, plasminogen, fibrinogen/fibrin, lysozyme, papain, human serum albumin, heat coagulable mucoproteins isolated from cartilage, bones and skin, gamma globulin blood proteins, and a number of the blood factor proteins, including, for example, factor VIII, XII, IXa and Xa, among others.
  • the blood factor proteins including, for example, factor VIII, XII, IXa and Xa, among others.
  • Preferred proteins for use in the present invention include proteins containing high percentages by weight of cysteine, for example, ribonuclease Tl, human serum albumin and gamma globulins.
  • An especially preferred protein for use in the present invention is keratin, because of its particularly high cysteine content (about 12% to about 17% by weight of cysteine) .
  • Proteins are activated by being sub ⁇ jected to a reducing agent at a pH of about 9.0 or above for a time sufficient to produce free thiol group. This period is generally about 5 minutes up to about one hour.
  • Activation periods of greater than one hour are less preferred because although such activation periods may marginally increase the amount of activated thiol groups in the protein, such periods may also result in hydrolysis of the protein into shorter, less advantageous peptide units.
  • a number of globular proteins contain cysteinyl residues within hydrophobic pock ⁇ ets. To activate these proteins and expose cysteinyl groups which exist in hydrophobic pockets to the keratinous tissue, it may be necessary to subject the proteins to denaturation and activation so that an activated cysteinyl residue of the denatured protein may be placed in proximity to the cysteinyl residues in the keratinous tissue to promote covalent binding.
  • the proteins of the present invention are preferably activated in the presence of reducing agent separately before they are formulated with the other components, because the addition of components other than a reducing agent at a pH above about 9.0 may adversely affect the rate at which cystinyl disulfide bonds (-S-S-) in the protein are converted to cysteinyl mercaptide groups (S-H) . This may lower the overall activity of the protein.
  • the activated protein is preferably a keratin, but any protein which contains sufficient cysteinyl content to promote covalent binding to activated keratinous tissue is con ⁇ templated for use in the present invention.
  • a particularly preferred keratin is Kerasol ⁇ m from Croda Chemicals Interna ⁇ tional, Chesire, England.
  • the molecular weight of proteins useful in the present invention preferably varies between about 5,000 and 500,000 Daltons, and most preferably varies between about 120,000 and 130,0-00 Daltons.
  • Reducing agents which are useful to activate protein in the present invention include sulfides, thiol-containing compositions including dithiothreitol, trithiohexitol, glutathione, cysteine, mercaptoethanol, thioglycerol, thioalkanoic acid and mercaptocarboxylic acid, for example, mercaptosuccinic acid, thiolactic acid and their pharmaceuti ⁇ cally acceptable salts, among others, including thioglycollic acid and salts of thioglycollic acid.
  • Preferred reducing agents for activating the protein are thioglycerol, cysteine, thiolactic acid and thioglycollic acid, and their pharmaceuti ⁇ cally acceptable salts.
  • An especially preferred reducing agent for use in the present invention is ammonium thioglycol ⁇ late. It is preferred that the reducing agent for activating the protein should be the same as the biologically compatible reducing agent which is used in the final formulation of the invention.
  • the use of strong biologically incompatible reduc ⁇ ing agents to activate the protein are less preferred and may make the use of the protein more difficult because the reduc ⁇ ing agent may have to be removed from the activated protein before formulation.
  • Compositions of the present invention also contain a compatible reducing agent in an amount equal to about 0.1 to about 15% by weight of the formulation.
  • Preferred composi ⁇ tions contain about 3.0 to about 10% by weight of a compatible reducing agent.
  • the amount of compatible reducing agent varies according to the therapeutic use for which the composi ⁇ tions are intended, but generally falls within the range of about 3.0 to about 10% by weight.
  • a compatible reducing agent is an agent which reduces cystinyl disulfide linkages in keratinous tissue to produce free thiol or mercaptide groups and is compatible with biological and/or pharmaceutical systems.
  • Compatible reducing agents which are contemplated for use in the present invention include mercaptoethanol, dithiothreitol, glutathione, cysteine and salts of thioglycol ⁇ lic acid.
  • An especially preferred reducing agent is ammonium thioglycollate.
  • compositions of the present invention may additionally comprise about 0.001 to about 4.0% by weight of an oxidizing agent.
  • Preferred embodiments comprise about 0.1 to about 1.0% of the oxidizing agent and most preferably comprise about 0.5% to about 1.0% of the oxidizing agent.
  • the oxidizing agent is included in compositions of the present invention to enhance oxidation and promote the formation of covalent disulfide bonds between activated protein and keratinous tissue.
  • Exemplary oxidizing agents include hydrogen peroxide (which may or may not be stabilized with known stabilizers, for exam ⁇ ple urea) and its salts including ammonium sulfate peroxide, urea peroxide, pyrophosphate peroxide, carbonate peroxide, organic peroxides including acetyl peroxide, benzoyl peroxide, among others, alkali metal perborates including sodium per ⁇ borate,, the alkali metal bromates including sodium and potas ⁇ sium bromate and sodium and potassium iodate.
  • hydrogen peroxide is the preferred oxidizing agent.
  • the amount of hydrogen peroxide should be in an amount equal, to about 0.001 to about 1.5% by weight of the composi ⁇ tion and most preferably about 0.05 to about 1.0%. Where oxidizing agents other than hydrogen peroxide are used, a higher percentage by weight is usually used compared to hydrogen peroxide which has a high oxidation equivalent per unit weight.
  • addi ⁇ tional components may be added to the formulation to enhance the effects of the compositions.
  • addi ⁇ tional components may include bases, acids, buffering agents, solvents, emulsifying agents or surfactants, thickeners, pre ⁇ servatives, organic solvents, coloring agents and perfuming agents.
  • Exemplary acids and bases are added to adjust the pH of the formulation to desired levels.
  • Preferred acids include organic acids for example acetic acid, citric acid and tartaric acid, among others, and inorganic phosphoric acid including its salts such as the salts of mono- and di- hydrogen phosphoric acid.
  • the inorganic phosphoric acid salts may also be included in the formulations as buffering agents.
  • Preferred bases include organic amines, for example. monoethanolamine, triethanolamine, trimethylamine and triethylamine. Most preferred bases include ammonium hydroxide.
  • Buffering agents for example the inorganic phosphoric acid salts indicated above as well as other buffering agents, for example the salts of organic acids such as acetic acid and citric acid may be included in the formulations of the present invention in amounts effective to maintain the pH of the for ⁇ mulation over time.
  • the amount of buffering agent is no more than about 1.5% by weight of the formulation and most preferably is less than 0.75% by weight.
  • the pH of the formulation may be a factor in determining its stability and in maintaining the activity of certain components in the for ⁇ mulation, especially the activated protein and the compatible reducing agent.
  • a buffering agent may be included within the formulation to maintain the pH at a relatively con ⁇ stant level over time.
  • organic solvents may be included.
  • solvents that may be useful in certain embodiments of the present formulation include water, soluble polar organic solvents for example, alkanols such as methanol, ethanol, propanol, butanol and carbonyl containing solvents for example acetone, butanone and the like, among others.
  • Additional solvents include ethers and amines, for example diethyl or dipropyl ether and trimethyl or triethyl amine. Trimethylamine and triethylamine may also be added as bases.
  • the solvent added to the formulation may enhance the solubility of certain components. Where liquid formulations are contemplated, it is sometimes advisable to add an organic solvent to promote the solubility of certain less polar com ⁇ ponents, which without the added organic solvent may be only marginally soluble in water resulting in formulations having more than one phase. The addition of the organic solvent may produce a uniform, homogeneous single phase.
  • Emollients may also be included, especially in lotions to produce a uniform, homgeneous single phase and provide other favorable characteristics.
  • An especially preferred emollient for use in formulations of the present invention is PPG 15-sterol ether, which also may be added to the formula ⁇ tions of the present invention for its emulsifying character ⁇ istics.
  • An emulsifying agent or surfactant is often added to embodiments of the present invention to enhance the character ⁇ istics of the formulation, to promote the solubility of the protein and other components and the phase stability of the formulation. Such agents also provide detergent-like qualities to the formulations. Suitable surfactants or emul ⁇ sifying agents may be nonionic, anionic or amphoteric.
  • Non- ionic emulsifying compositions include, for example the lower alkylene oxide condensation products of hydrophobic compounds, for example ethylene oxide condensation products with higher fatty acids, higher fatty alcohols or alkylated aromatic hydrocarbons, higher molecular weight polypropylene glycols, amide and amine condensation products of which N-bis (2- hydroxyethyl)-lauramide is exemplary.
  • Preferred nonionic emulsifying compositions include polyoxyethylene ethers including polyoxyethyleneisohexadecyl ether, for example Arlasolve 200 'tm (available from ICI Americas, Wilmington Delaware) , polyoxyethylenelauryl ether, for example Brij 35 tm (ICI) , polyoxyethylenestearyl ether, for example Brij 72 tm , and Brij 78 tm (ICI) and polyoxypropylenestearyl ether, for example PPG-15 stearyl ether (Arlamol E, ICI) .
  • Other exemplary emulsifiers include ethoxylated lanolin, for exam ⁇ ple, Lanogel 41 (Amerchol, Inc., Edison, N.J.).
  • Exemplary anionic surfactants include sulfuric acid esters of polyhydric alcohols, e.g. lauryl sulfate, cetyl sulfate, etc., higher fatty alcohol sulfates derived from coconut oil, hydroxy sul- fonated higher fatty acid esters such as, e.g., higher fatty acid esters of 2,3-dihydroxy-propane sulfonic acid, higher fatty acid esters of low molecular weight alkylol sulfonic acids, e.g., oleic acid ester of isethionic acid, sulfated higher fatty acid alkylolamides such as e.g., ethanolamide sulfates, higher fatty acid amides of amine alkyl sulfonic acids, e.g., lauric amide of taurine, among others, and aromatic containing anionic synthetic surfactants.
  • Exemplary amphoteric surfactants include the salts of N-
  • an anti-foaming agent may be added to certain compositions to promote homogeneity and prevent foam ⁇ ing from surfactant action.
  • a preferred anti-foaming agent for use in embodiments of the present invention includes, for example, Dimethicone tm , available from Dow Chemical Corp., Midland, Michigan.
  • Thickeners or gelling agents may be added to provide additional weight and a more viscous feel to the formulations.
  • Suitable thickening agents include polyvinyl pyrollidone, for example PVP K30 (GAF Charllotte, N.C.) polyacrylates, car- bomers, for example carboxyvinyl polymer such as Carbapol 940 (available from B.F.
  • polyoxyethylene stearyl ethers for example, polyoxyethylene-2 stearyl ether such as Steareth 2 tm (ICI) and polyoxyethylene- 20 stearyl ether such as Steareth 20 tm (ICI) , sodium alginate, carageenan, agar, ethoxylated polyvinyl alcohol, gums, for example methylcellulose, hydroxymethylcellulose, car- boxymethylcellulose, propylcellulose and hydroxypropylcel- lulose, acacia, tragacanth, guar, and quince, among others.
  • polyoxyethylene-2 stearyl ether such as Steareth 2 tm (ICI)
  • polyoxyethylene- 20 stearyl ether such as Steareth 20 tm (ICI)
  • sodium alginate sodium alginate
  • carageenan agar
  • ethoxylated polyvinyl alcohol ethoxylated polyvinyl alcohol
  • gums for example methylcellulose, hydroxymethylcellulose,
  • compositions which are contemplated to be formulated as a gel or lotion Isoseteth 20 tm (polyoxyethyleneisohexadecyl ether, ICI) , and Steareth 2 tm and 20 t:m are preferred for use as thickening agents.
  • preferred thickeners include Steareth 2 tm and Steareth 20 tm and the carbomer polymers, for example Carbopol 940 tm .
  • Preservatives are added for preventing microbial growth in the presence of protein nutrients.
  • exemplary pre ⁇ servatives include benzoic acid analogs including, among others, sodium benzoate.
  • Other presevatives include propyl and methyl paraben, Dowicil t ⁇ n (Dow Chemical Corp., Midland, Mi.) and formaldehyde solution.
  • An especially preferred pre ⁇ servative is Germaben II ⁇ m , available from Sutton Laboratories, New Jersey.
  • Coloring agents and perfume agents may also be added to enhance the characteristics of the formulations.
  • compositions include an antioxidant instead of an oxidizing agent.
  • These compositions comprise about 0.01 to about 10% by weight of an activated protein component, about 0.1 to about 15% by weight of a compatible reducing agent, about 0.001 to about 2.0% by weight of an antioxidant, and at least one com ⁇ ponent selected from the group consisting of water, acids, bases, buffering agents, emulsifying agents or surfactants, thickeners, coloring agents and perfume agents.
  • compositions comprising an antioxidant the antioxidant is included to promote the storage stability of the formulations.
  • exemplary antioxidants may include alpha- tocopherol, hydroxyquinone, unipherol, tocopherol ascorbate, lecithin, chlorophyll, ascorbylpalmitate, linseed oil, tongue oil, other natural product antioxidants such as the steam dis ⁇ tillation extract of rosemary as disclosed in U.S. Patent No. 4,450,097, thiazoline carboxylate, dihydroquinolines, methyl gallate, propyl gallate, alkylaryl and diarylamines.
  • Certain chelating agents for example, EDTA, may be employed to enhance the antioxidant effect of the above agents.
  • the chelating agent may function to chelate any dis- solved metals which may be responsible for the in situ gener ⁇ ation of oxygen.
  • the chelating agent comprises between about 0.001 to about 0.5% of the formulation and most preferably the chelating agent comprises no more than about 0.1% of the formulation.
  • a volatile antioxidant is used.
  • Volatile antioxidants provide the advantage of protecting the activated protein and reducing agent from oxidation during storage.
  • the antioxidants are volatile, after the compositions are placed on the treatment area and exposed to air or a heat source, the antioxidant will evaporate from the treatment area leaving the remaining protein and activated keratinous tissue to be air oxidized.
  • Volatile antioxidants include voltile carbonyl containing compounds, hindered phenolic compounds, for example 2,4,6-trialkyl phenols, buty- lated hydroxyanisole (BHA) , butylated hydroxytoluene (BHT) , p- hydroxytoluene and p-hydroxyanisole.
  • a volatile antioxidant as used in preferred embodi ⁇ ments of the present invention is an antioxidant that volatil ⁇ izes or evaporates from the treatment area under normal drying conditions.
  • Non-volatile antioxidants although useful in certain aspects of the present invention, are less preferred than are volatile antioxidants, which are added to formula ⁇ tions for their ability to stabilize the active ingredients over time while in storage and their ability to be removed from the treatment area under normal drying conditions.
  • Preferred volatile antioxidants include those that are more easily volatilized, i.e., will evaporate more quickly from the treatment surface.
  • Certain antioxidants may be formulated in combination with solvents including water. This may promote azeotrope formation and volatility of the antioxidant. Azeotrope forma ⁇ tion with water or with other solvents may result in the antioxidant volatilizing at a temperature lower than normal. Thus, by formulating the compositions with, for example, an alcoholic or other solvent, the volatilization of the antioxidant may be enhanced, resulting in an- enhanced rate of oxidation of the treated keratinous tissue.
  • an oxidizing agent when an oxidizing agent is not included in the formulation, about 0.01% to about 2.0% of antioxidant is included in the formulations. Without the additional oxidizing agent, the antioxidant is included to prevent atmospheric oxygen or oxygen dissolved in the solution from deactivating the protein during storage.
  • the oxidizing agent in compositions in which oxidizing agents are employed to promote the oxidation of free thiols or mercap- tides to covalent disulfide bonds, the oxidizing agent com ⁇ prises about 0.001% to about 4.0% by weight of an oxidizing agent and the antioxidant comprises about 0.01% to about 4.0% of the formulation.
  • the for ⁇ mulations may additionally comprise acids, bases, buffering agents, emulsifying agents or surfactants, thickeners, pre ⁇ servatives, organic solvents, coloring agents and perfume agents as described for other embodiments of the present invention.
  • a volatile antioxidant is preferred.
  • addi ⁇ tional organic solvent may be added to promote the volatiliza ⁇ tion of the antioxidant. It is recognized that the choice of additives is made to avoid any interactions that may affect the activity of the the activated protein, reducing agent, oxidizing agent or antioxidant.
  • compositions of the present invention are applied to the treatment area as a liquid, cream, gel or lotion by rubbing the compositions into the hair or other tissue to be treated. After the compositions have been in contact with the treated tissue for a time period of about 20 minutes to six hours, the treated area is then dried at ambient air tempera ⁇ ture or preferably, at elevated temperatures under a hair dryer or other heat source.
  • compositions of the present invention which do not contain an oxidizing agent or an antioxidant may be used.
  • the treatment of the nails of humans and the hooves of animals comprises exposing the nails or hooves to a composition comprising about 0.01 to about 12% by weight of an activated protein as described hereinabove, preferably keratin, about 0.1 to about 15% by weight of a pharmaceuti ⁇ cally compatible reducing agent as described hereinabove, preferably thioglycollic acid or ammonium thioglycollate and the remainder.of the composition comprises at least one com ⁇ ponent selected from the group consisting of water, acids, bases, buffering agents, emulsifying agents or surfactants, thickeners, preservatives, organic solvents, coloring agents and perfuming agents.
  • Procedure Mix Components of A together and adjust pH with triethanolamine. Add Component B and thoroughly mix until homogeneous. Mix in fragrance until homogeneous.
  • Procedure Mix the ammonium thioglycollate, ammonium hydroxide and a small amount of water to form a mixture with a pH of about 9 to 11. About half of the protein is added to this mixture which may be agitated or stirred for about 15 minutes followed by the addition of water, hydrogen peroxide and the remaining protein. Alternatively, after the first half of the protein is added, the water, hydrogen peroxide and remaining protein may be added. The other ingredients are then added after the hydrogen peroxide and stirred or agitated sufficiently to produce a homogeneous composition.
  • Step 1 In a separate tank agitate B (water) very strongly and sprinkle B (PVP K-30) onto the Vortex. Mix until PVP K-30 solution is complete.
  • Step 2 Charge a mixing tank with water at 35-40"C. Add the A phase ingredient and mix thoroughly. Add the PVP K-30 solution and mix in well.
  • Step 3 Mix C phase together in a plastic container. Warm to 35- 40 ⁇ C. Add to step 2 and add the D phase.
  • Step 4 In a plastic container, add ammonium thioglycollate and then add ammonia solution slowly to bring the pH to 9.0. Add the Kerasol ⁇ ia. Mix this solution well and add it to the batch.
  • Procedure Charge main mixing kettle with B ingredients and heat while mixing to 80-85"C. In a separate container heat A ingredients to 80-85 ⁇ C and mix until uniform. At 80-85"C add mixed A ingredients to mixed B ingredients while thoroughly mixing. Cool to 50-55°C. At 50-55"C add Germaben and blend in very well. Continue to cool to 30°C and use at this temperature.
  • Coloring Agent 0.87 E Procedure This is a 4% Carbopol dispersion. Measure water and agitate at high speed. Add elastin and then biotin and allow them to disperse. Add Carbopol 940 to the lip of the vortex and mix well until the dispersion is complete. Add component A to the mixing kettel at 25-30°C and add B phase from above and mix until uniform. Add component C to mixture of A and B and mix until uniform. Add fragrance and coloring agent.
  • Germaben II 0 0..2 233 E
  • Example I A 63 year old Florida man with a long history of hair loss skeptically used the formulation of Example I on the top and front of his head, up to his greatly receded hairline. Within 3 weeks there was visible new growth in areas that had not grown visible hair in 20 years.
  • Example I A 27 year old male hairdresser from New York who noticed considerable hair loss due to breakage on his pillow, in his comb, in the drains, etc. began using the formulation of Example I daily. Within 3 weeks his estimates of the hair on his comb in the morning decreased from over 100 hairs to under 10 hairs. He no longer noticed hair on his pillow in the morning, and only a normal amount of hair in his drains. A 31 year old New Jersey man with very thin fly-away hair began using the formulation of Example I daily, and within one month found his hair to be thicker, with more body, and stayed where he wanted it with much less fly-away.
  • Example III A 42 year old New York man with chronically thin brittle nails began using the formulation of Example III on his nails daily. Within 1 month he reported his nails were considerably harder, less prone to breaking, and he could grow them longer; especially one nail which had been injured years ago and had developed a chronic thin spot. This thin spot persisted relative to the rest of his nails, but since all of his nails were harder and thicker it was no longer a problem. In addition, the rate of nail growth was markedly faster, based upon the frequency with which he had to file his nails before and after treatment.
  • Example IV A thoroughbred used as a carriage horse developed back rubs on the withers and back from the tack. Daily application of the formulation of Example IV resulted in 80% restoration of the acute condition within 8 days despite continued appli ⁇ cation of the tack and carriage driving. The attending veterinarian estimated that this level of fur restoration should have taken 6-8 weeks in the absence of driving and the application of tack.
  • Example IV The formulation from Example IV was used on over 8 horses at a major show barn for coat deficits due to wounds, abrasions and back rubs. In all instances, the deficits resolved at a vastly accelerated rate in the estimate of a highly experienced groom who travels with the U.S. Olympic Equestrian Team.
  • Example XXXI Grooming Daily misting gets dog coats into show condition in one to two weeks which would otherwise have taken four to six months. Beskie terriers looked "fantastic" after one month using the composition of Example X. The coats became silky and shiny and the dogs pads were strengthened with no crack ⁇ ing.
  • Example XXXIV Hoof Conditioning In a number of cases, the composition of Example XIII resulted in hoof reconditioning, and the strengthening of "shelly" hooves, and dry, brittle and/or cracking hooves.
  • Example XXXV Restoration of Chronic Coat Condition
  • Photographer for a New Jersey newspaper used the com ⁇ position of Example XV for treating hair loss on a biopsy for her Burmese mountain dog which had not grown hair at the site of biopsy for over a year and a half. After 3 days of treat ⁇ ment, the photographer reported preliminary regrowth of hair.

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  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Veterinary Medicine (AREA)
  • Animal Behavior & Ethology (AREA)
  • General Health & Medical Sciences (AREA)
  • Public Health (AREA)
  • Birds (AREA)
  • Epidemiology (AREA)
  • Dermatology (AREA)
  • Emergency Medicine (AREA)
  • Chemical & Material Sciences (AREA)
  • Inorganic Chemistry (AREA)
  • Cosmetics (AREA)
EP19890903327 1988-03-04 1989-03-03 Storage-stable compositions and methods for treating keratinous tissue Withdrawn EP0403530A4 (en)

Applications Claiming Priority (4)

Application Number Priority Date Filing Date Title
US16400988A 1988-03-04 1988-03-04
US164009 1988-03-04
US22329588A 1988-07-22 1988-07-22
US223295 1988-07-22

Publications (2)

Publication Number Publication Date
EP0403530A1 true EP0403530A1 (de) 1990-12-27
EP0403530A4 EP0403530A4 (en) 1991-09-11

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ID=26860168

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EP19890903327 Withdrawn EP0403530A4 (en) 1988-03-04 1989-03-03 Storage-stable compositions and methods for treating keratinous tissue

Country Status (4)

Country Link
EP (1) EP0403530A4 (de)
KR (1) KR900700075A (de)
AU (1) AU614832B2 (de)
WO (1) WO1989007930A1 (de)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP2422763A1 (de) 2010-08-27 2012-02-29 Colomer Beauty and Professional Products, S.L. Verfahren und Kit zur Haarbehandlung

Families Citing this family (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
IL97012A0 (en) * 1990-01-30 1992-03-29 Gist Brocades Nv Topical preparations for treating human nails
DE19506347A1 (de) * 1995-02-23 1996-08-29 Hartmut Sell Mittel zur äußerlichen Behandlung von Hufpilz bei Unpaarhufern, insbes. bei Pferden
US5888483A (en) * 1997-02-12 1999-03-30 Avon Products, Inc. Nail bleach
AU2002364893A1 (en) 2001-10-22 2003-06-17 University Of Mississippi Delivery of medicaments to the nail
FR2988602B1 (fr) * 2012-03-27 2014-09-05 Oreal Procede cosmetique de soin et/ou de maquillage des matieres keratiniques
BE1021016B1 (nl) * 2013-10-09 2014-12-17 Oystershell N.V. Samenstelling voor de behandeling van nagelziektes en gebruik

Family Cites Families (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4195095A (en) * 1969-04-04 1980-03-25 Sheffner Aaron L Topical application of thioglycolic acid in the treatment of dermatological conditions
JPS5716810A (en) * 1980-07-02 1982-01-28 Yoshio Murai Cosmetic
FR2522657B1 (fr) * 1982-03-05 1985-07-12 Oreal Composition de traitement d'un substrat keratinique comportant des proteines chimiquement modifiees et procede de preparation desdites proteines
US4438102A (en) * 1982-08-10 1984-03-20 Ciro's Touch, Ltd. Method of promoting tissue growth
US4530828A (en) * 1982-09-16 1985-07-23 Richardson-Vicks Inc. Nail conditioner
US4919924A (en) * 1984-11-26 1990-04-24 Repligen Corporation Use of thioredoxin, thioredoxin-derived, or thioredoxin-like dithiol peptides in hair care preparations
US5041286A (en) * 1988-07-26 1991-08-20 Yasmin Products Pty. Limited Process for reconfiguring keratin fibre

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP2422763A1 (de) 2010-08-27 2012-02-29 Colomer Beauty and Professional Products, S.L. Verfahren und Kit zur Haarbehandlung
WO2012025615A2 (en) 2010-08-27 2012-03-01 Colomer Beauty And Professional Products, S.L. Process and kit for treating hair

Also Published As

Publication number Publication date
AU614832B2 (en) 1991-09-12
AU3352389A (en) 1989-09-22
EP0403530A4 (en) 1991-09-11
WO1989007930A1 (en) 1989-09-08
KR900700075A (ko) 1990-08-11

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