EP2344117A2 - Utilisation d'hydrophobine dans la coloration non permanente de la kératine - Google Patents

Utilisation d'hydrophobine dans la coloration non permanente de la kératine

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Publication number
EP2344117A2
EP2344117A2 EP09781840A EP09781840A EP2344117A2 EP 2344117 A2 EP2344117 A2 EP 2344117A2 EP 09781840 A EP09781840 A EP 09781840A EP 09781840 A EP09781840 A EP 09781840A EP 2344117 A2 EP2344117 A2 EP 2344117A2
Authority
EP
European Patent Office
Prior art keywords
hydrophobin
keratin
permanent
hair
dye
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Withdrawn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
EP09781840A
Other languages
German (de)
English (en)
Inventor
Heiko Barg
Thomas Subkowski
Marvin Karos
Claus Bollschweiler
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.)
BASF SE
Original Assignee
BASF SE
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 BASF SE filed Critical BASF SE
Priority to EP09781840A priority Critical patent/EP2344117A2/fr
Publication of EP2344117A2 publication Critical patent/EP2344117A2/fr
Withdrawn legal-status Critical Current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
    • A61Q5/00—Preparations for care of the hair
    • A61Q5/06—Preparations for styling the hair, e.g. by temporary shaping or colouring
    • A61Q5/065—Preparations for temporary colouring the hair, e.g. direct dyes
    • 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
    • A61K2800/00—Properties of cosmetic compositions or active ingredients thereof or formulation aids used therein and process related aspects
    • A61K2800/80—Process related aspects concerning the preparation of the cosmetic composition or the storage or application thereof
    • A61K2800/88—Two- or multipart kits

Definitions

  • the present invention relates to the use of hydrophobin in the non-permanent dyeing of keratin and keratin-containing materials, especially hair, and a corresponding method of non-permanent dyeing of keratin and keratin-containing materials, especially hair. It also relates to non-permanent staining of keratin and keratin-containing materials, especially hair, containing hydrophobin.
  • Means for coloring or tinting hair are classified according to the stability of the dyeing. There are several classifications known. Usually, a subdivision into three classes: temporary hair dyes (tints in the strict sense) that last only 1-2 hair washes (level 1), semi-permanent
  • Levels 1 and 2 have in common in all of the classifications that they are washable, so they are collectively referred to herein as leachable or non-permanent dyes.
  • Semi- and demipermanent stains are summarized below as stains of stage 2, while tints of stage 1 are referred to colors washed out after 1-2 washes.
  • All commercial products for the permanent dyeing of hair of level 3 contain on the one hand a "developer", usually an oxidizing chemical, and on the other hand an alkaline component as part of their dye paste, usually ammonia or an ammonia substitute such as monoethanolamine.
  • Permanent hair dyes are also referred to as oxidative hair dyes due to this chemical process.
  • the permanent hair dyes also include the so-called "self-oxidizing dyes", which are oxidized by atmospheric oxygen.
  • non-permanent hair dyes are generally non-oxidative.
  • the dye molecules are arranged on the surface of the keratin or penetrate only a small distance into the hair. They are too big to penetrate the hair completely.
  • the resulting dye layer can be removed by washing with hair shampoo.
  • Level 1 acidic dyes are usually used, which have only a low affinity for the hair and rather accumulate on the surface of the hair.
  • the dyes in tints are generally either positively charged and then bind to negatively charged surface groups of the hair, or they are small molecules that can penetrate into the cuticle.
  • the hair shaft itself is not penetrated by temporary hair colors. Instead, these dyes remain attached to the cuticle and can often be removed with a single hair wash.
  • semipermanent hair colors can penetrate the hair because they contain smaller color molecules than the temporary hair tints. Therefore, semipermanent hair dyes last longer than temporary tints and usually need to be renewed after 8 to 10 washes. Demipermanent dyeings, whose dyes penetrate even better into the hair, last much longer, usually up to 24 washes.
  • tints by the suppliers, often even as tints of level 1, although they should be more appropriately classified as level 2.
  • Hair dyes are normally sold in the form of aqueous, concentrated solutions or emulsions and contain, in addition to the actual dyes, e.g. Fatty acid alcohols and / or other oil components, emulsifiers and surfactants, and optionally alcohols. Tints and semipermanent hair dyes are available in various product forms, i.a. as pastes, rinses, shampoos, gels and sprays.
  • Non-permanent hair dyes have a lower market share than permanent hair colors. They are nevertheless of high economic interest because they attack the hair less than permanent hair colors and do not bleach. still contain ammonia. In addition, because of some of their ingredients, especially hydrogen peroxide and ammonia, permanent hair colors have been under criticism for quite some time. Permanent paints that have not been tested for compatibility will be banned even in the EU in the future.
  • non-permanent hair dyes and methods that provide an alternative or enhancement to the existing non-permanent hair colorants and methods and, in particular, allow more stable binding of the dye to the hair as much as possible without causing damage to the hair ,
  • Hydrophobins are a class of small, cysteine-rich proteins about 100-150 amino acids in length, which in nature occur only in filamentous fungi. They are amphiphilic and can form a water-insoluble layer on the surface of an article. Their natural functions include the coating of fungal spores so that they do not stick together, the coating of aerial hyphae to reduce the surface tension of water and thus to facilitate water absorption, and possibly the Signal transduction between a fungus and its environment (Whiteford, JF Spanu, PD (2001), Fungal Genet., Biol. 32 (3): 159-168; Wösten et al. (1999) Current Biol. 19: 1985-88; Bell et al., (1992) Genes Dev. 6: 2382-2394).
  • hydrophobin genes have been identified in ascomycetes, deuteromycetes and basiodiomycetes.
  • Some fungi contain more than one hydrophobin gene, e.g. Schizophyllum commune, Coprinus cinereus and Aspergillus nidulans.
  • hydrophobins of one class can to a certain extent functionally replace hydrophobins of the other class.
  • the various hydrophobins appear to be involved in different fungal development stages and to perform different functions therein (van Wetter et al (2000) Mol Microbiol 36: 201-210, Kershaw et al (1998) Fungal Genet., Biol. 23: 18 -33).
  • Hydrophobins usually have eight cysteine units. They can be isolated from natural sources, but can also be obtained by means of genetic engineering processes, as described, for example, in WO 2006/082251 and WO 2006/131564.
  • hydrophobin in cosmetic preparations is known per se.
  • US 2003/0217419 A1 describes the use of the SC 3 hydrophobin from S. ses for the treatment of keratin-containing materials. This forms cosmetic depots that should withstand several washes with shampoo.
  • the hydrophobin is applied either simultaneously or after the cosmetically active ingredient, but not before applying the cosmetic ingredient.
  • WO 2006/136607 A2 describes the use of hydrophobin and of hydrophobin conjugates in cosmetic preparations for hair care.
  • hydrophobins can be linked to semi-permanent or permanent hair dyes and increase their concentration and action on the skin and hair.
  • permanent hair dyes one of the two dye components is bound to the hydrophobin while the other component is added to the hair after application of the conjugate. The oxidative coupling of both components then happens directly on the hair.
  • the use of hydrophobin together with temporary hair dyes of stage 1 does not describe WO 2006/136607.
  • WO 2006/082251 describes hydrophobin proteins, their production and their use for surface coating.
  • WO 96/41882 proposes the use of hydrophobins, inter alia, as surface-active substances, for hydrophilizing hydrophobic surfaces, for improving the water resistance of hydrophilic substrates and for producing hair shampoos and rinses.
  • non-permanent dyeing in particular the tinting or semi-permanent dyeing of keratin and keratin-containing materials (such as hair, skin and nails, but also wool, leather and other keratinous materials). containing textiles), especially of hair.
  • Another object is to provide a method of keratin staining, especially hair coloring, in which the keratin fiber is damaged as little as possible.
  • the dyeing of keratin made possible by the present invention should preferably be non-permanent, but exceed in their resistance and / or color intensity the hitherto available non-permanent, in particular temporary, hair dyeings.
  • the aim is further to improve the coloration of keratin by conventional non-permanent colorants, in particular to increase the color intensity and / or the resistance to tinting or dyeing without the need for the use of oxidative dyes.
  • This goal is preferably sought for tints and semi-permeable dyeings. This is intended to provide an alternative to permanent colorants which does not have the disadvantages of these colorants.
  • the present invention relates to the use of hydrophobin and hydrophobin-containing compositions in the non-permanent dyeing of keratin or keratin-containing material, especially hair. It further relates to a corresponding composition for coloring keratin, especially a tint or semi-permanent color. A similar method of staining keratin using hydrophobin is also presented.
  • hydrophobin preferably leads to a higher color intensity and a longer washing time of the dyeing, which suggests an improved uptake and / or addition of non-permanent dyes into / on the keratin. This applies in particular to hydrophilic dyes. The coloring becomes more intense and / or longer lasting.
  • hydrophobin may further result in improved uptake and / or addition of other cosmetic actives (besides the non-permanent dyes) into / on the keratin.
  • This preferably relates to hydrophilic cosmetically active ingredients, such as panthenol.
  • the active ingredients are thus more intense, because they arrive in higher local concentration and / or in the keratin and / or the time to complete washing out of these substances is prolonged. This can have an effect on the hair thickness, tear resistance (tensile strength improvement), combability and combing power, suppleness and other properties of the treated keratin.
  • the respective quantitative and qualitative effects are determined by the individual cosmetic active ingredients and their field of application.
  • other constituents of tints / colorations in addition to the dyes, such as care substances can also act more intense by the presence of hydrophobin.
  • the present invention relates to the following subjects or embodiments:
  • a method of non-permanent staining of keratin or keratin containing material comprising applying at least one non-permanent dye and at least one hydrophobin of structural formula (I) to the keratin or keratin containing material;
  • composition containing at least one hydrophobin of formula (I) (i) a composition containing at least one hydrophobin of formula (I), and (ii) a composition containing at least one non-permanent
  • a hydrophobin may also encompass more than one hydrophobin molecule, namely, two, three, four, five, etc. hydrophobins of a variety.
  • At least one means “one or more”, “at least” followed by a numerical value means "this or a higher numerical value”.
  • acids are present either as the free acid or as a partial or complete salt of the acid or as a mixture of the acid with its salt.
  • bases especially amines, may be present as the free base or as a partial or complete salt of the base or as a mixture of the base with its salt.
  • “Native” is synonymous with “wild type” and “naturally occurring”.
  • a “naturally” occurring linkage of two polypeptides is a linkage as it is found in naturam, that is, for example, in a wild-type protein.
  • a wild-type or native protein or polypeptide is - unless otherwise stated indicated - the usually naturally occurring form of this protein / polypeptide.
  • a "fragment" of an amino acid sequence results from the absence of one or more consecutive amino acids at the N and / or C terminus of said original sequence.
  • a "homologue" of an amino acid sequence in the context of the present invention is a protein or polypeptide which differs from the original sequence by the substitution of one or more amino acids.
  • the function and / or conformation of the protein is not affected by this substitution.
  • the amino acid substitution is a conservative amino acid substitution, so the exchanged amino acids are replaced by amino acids with similar chemical properties, e.g. VaI by AIa.
  • conservative amino acid exchanges occur between the members of the following groups: acidic amino acids (aspartate and glutamic acid); basic amino acids (lysine, arginine, histidine); hydrophobic amino acids (leucine, isoleucine, methionine, valine, alanine); hydrophilic amino acids (serine, glycine, alanine, threonine); Amino acids with aliphatic side chains (glycine, alanine, valine, leucine,
  • Amino acids with amide groups in the side chain (asparagine, glutamine); Amino acids with aromatic side chains (phenylalanine, tyrosine, tryptophan);
  • isolated means "separated or purified from the parent organism". An isolated hydrophobin is therefore no longer part of the fungus in which it occurs in nature. Recombinantly produced hydrophobins are also 'iso lated' 'hydrophobins.
  • Color Intensity is the perceived chroma which can be determined either by subjective evaluation on the face-up (if necessary in comparison with a non-stained standard), or by comparison of optical measurement data.
  • measurement data can be determined, for example, by means of a conventional photometer or colorimeter, such as the Konica Minolta CR-300, CR-310, CR-311 (Konica Minolta Sensing, Inc., Osaka, Japan), preferably with the CR-300.
  • the measured data can then be selected, for example, according to the abL system (synonym: Lab system, CIELAB system, L: brightness, a: color, b: saturation) or according to the L * a * b * system (CIE 1976) according to the L * a * b * system.
  • the evaluation according to the L * a * b * system is described, for example, in the instruction manual of the Konica Minolta CR-300, CR-310, CR-311 (Konica Minolta Sensing, Inc., Osaka, Japan), German version, version number 527 349 /9.99.
  • non-permanent dye refers to a dye whose staining effect on keratin can be reversed by single or multiple washout, ie a dye for non-permanent staining of keratin.
  • non-permanent / washable dye and “non-permanent / washable (hair) colorant” in the context of the present invention include tints, semi-and demipermanent dyes and keratin stainers, ie, all stains and stains that are leachable from keratin or no permanent hair dye.
  • tint is used in the context of the present invention synonymously with “temporary tint”, “temporary tinting agent”, “temporary tinting”, “temporary tinting”. Due to the non-uniform language usage of the manufacturer (see above, background), in its further meaning it includes all non-permanent, washable hair colorants, ie temporary colorants (tints in the true sense), semi- and demipermanent colorants. In the narrower, preferred sense it includes tints and semi-permanent colorants, in the most preferred and narrowest sense tints in the true sense. A tint in the true sense is a means for nonpermanent coloring of hair that can be washed out by 1-2 washes. Further definitions and explanations can be found in the section "Background”.
  • ⁇ E (synonym: Delta E ”) is a measure of the color difference or the color difference (DIN 5033-1: 1979-03) between a sample color and a comparison color or between two colors. ⁇ E can be determined photometrically according to various industrial standards, usually by measurement according to the standards DIN5033 and
  • ⁇ E is preferably determined according to standard DIN 5033 part 1 and DIN 6174, based on the L * a * b * color space, e.g.
  • a colorimeter such as the Konica Minolta CR-300, CR-310, CR-311 (Konica Minolta Sensing, Inc., Osaka, Japan), preferably with the CR-300, and as described in the Konica Minolta CR 300, CR-310, CR-311 (Konica Minolta Sensing, Inc., Osaka, Japan), German version,
  • ⁇ E values for perceptible color differences are usually between 2 and 5, with a very good result above 5, indicating a clear color difference (the presence of a different color) with the naked eye (http://de.wikipedia.org/ wiki / Delta E): ⁇ E rating
  • hydrophilic and hydrophobic have the usual meaning in the chemical jargon.
  • a “hydrophilic” dye is thus a dye which is preferably soluble in water or polar solvents. Hydrophilic dyes are typically polar compounds that are either ionic, have a dipole moment, and / or contain electronegative groups. In contrast, a “hydrophobic” dye dissolves preferentially in non-polar media and has no ionic functional groups and only weakly electronegative functional groups.
  • the present invention relates to the use of hydrophobin in the non-permanent staining of keratin and keratin-containing materials, as well as corresponding hydrophobin-containing cosmetic compositions and kits.
  • the color difference between hydrophobin-treated and untreated dyed hair expressed as ⁇ E and preferably determined according to DIN 5033 and / or calculated according to DIN 6174, eg according to the instructions in the Konica Minolta CR-300, CR-310, CR-311 (Konica Minolta Sensing, Inc., Osaka, Japan), German version, version number 527 349 / 9.99 (see Section "Definitions" and Ex. 6), can be more than 2, preferably more than 4, more preferably more than 5
  • This effect of the hydrophobin may be due to the fact that the hydrophobin can increase the hydrophilicity of a keratin-containing surface, especially the surface of hair.
  • compositions according to embodiments (2) and (3) and the use according to embodiment (4) preferably serve only for the cosmetic coloring of keratin and thus do not represent a therapeutic treatment of the human or animal body.
  • the object of the present invention is the coloring of keratin.
  • the keratin is present either as pure keratin or is part of keratin-containing materials.
  • Preferred keratins or keratin-containing materials are skin, hair, nails, horns, wool, leather, fur, fur and feathers. Particularly preferred are keratinic fibers, especially hair and wool.
  • the method according to embodiment (1) is used for coloring hair, especially hair of the main hair, and the compositions according to embodiments (2) and (3) and the use (4) for dyeing hair, especially hair of the head.
  • the keratin dyed according to the invention may be of human or animal origin and is preferably of human origin.
  • the method according to embodiment (1) and the use according to embodiment (4) of the present invention requires applying at least one hydrophobin to the keratin to be dyed.
  • the at least one hydrophobin is preferably part of a composition which contains further cosmetically acceptable ingredients.
  • hydrophobin or “hydrophobins” are preferably polypeptides of the general formula (I)
  • X is for each of the 20 naturally occurring amino acids (Phe, Leu, Ser, Tyr, Cys, Trp, Pro, His, GIn, Arg, He Met, Thr, Asn, Lys, VaI, Ala, Asp, Glu, Gly) can stand.
  • the radicals X may be the same or different. In this case, the indices standing at X each represent the number of amino acids in the respective subsequence X.
  • indices n and m independently represent natural numbers. In general, neither m nor n are zero, but are usually 1 or more.
  • m and n can be independently from 1 to 500. Preferably, m and n are independently from 15 to 300.
  • the amino acids designated C * to C ° are preferably cysteines; but they can also be replaced by other amino acids of similar space filling, preferably by alanine, serine, threonine, methionine or glycine. However, at least four, preferably at least five, particularly preferably at least six, and in particular at least seven, of the positions C * to C ° should be occupied by cysteine.
  • Cysteines at the positions C * to C ° may either be reduced in the proteins according to the invention or form disulfide bridges with one another.
  • the intramolecular formation of CC bridges in particular the formation of at least one, preferably two, more preferably three and most preferably four intramolekularischen Disulf ⁇ dmaschinen.
  • cysteines by amino acids of similar space filling, it is advantageous to replace those C-positions in pairs, which can form intramolecular disulfide bridges with one another in the presence of Cys at the positions concerned.
  • positions indicated by X are also a cysteine, serine, alanine, glycine, methionine or threonine, the numbering of the individual C positions in the general hydrophobin formulas may change accordingly. Additional cysteines at X positions are also capable of forming disulfide bridges.
  • the indices n and m stand for natural numbers including the number zero. In general, neither m nor n are zero, but are usually 1 or more. For example, m and n can be independently from 1 to 500.
  • m and n are independently from 15 to 300.
  • at least six of the radicals named C are cysteine, more preferably all of C is cysteine.
  • Most preferably, at least a pair of these cysteines form a disulfide bridge, and the formation of more than one disulfide bridge, that is, 2, 3, or 4 of these bridges, is most preferred.
  • Particular preference is given to hydrophobins of the general formula (III)
  • the indices n and m are natural numbers from 1 to 200.
  • at least six of the radicals named C are cysteine. Most preferably, all of the C radicals are cysteine. Most preferably, at least a pair of these cysteines form a disulfide bridge, and the formation of more than one disulfide bridge, that is, 2, 3, or 4 of these bridges, is most preferred.
  • Peptide sequences that are naturally linked to the other components of the hydrophobin may be peptide sequences that are not naturally linked to the other components of the hydrophobin. These are also to be understood as meaning those groups X n and / or X m in which a peptide sequence occurring naturally in the protein is extended by a peptide sequence which does not occur naturally in the protein.
  • the group X n and / or X m may contain, wholly or in part, peptide sequences which do not naturally occur in the hydrophobin protein.
  • fusion partner The non-naturally occurring in the protein peptide sequences from which the group X n and / or m X can be partially or entirely consist shall be referred to hereinafter also as a fusion partner.
  • These fusion partners are usually at least 20, preferably at least 35 amino acids long. They may, for example, be sequences from 20 to 500, preferably from 30 to 400 and particularly preferably from 35 to 100 amino acids.
  • Suitable fusion partners have been disclosed, for example, in WO 2006/082251, WO 2006/082253, WO 2006/131564 and WO 2007/014897. These fusion partners are preferred fusion partners in the context of the present invention.
  • the fusion partner can be selected from a variety of proteins.
  • fusion partners Only a single fusion partner can be linked to the remainder of the polypeptide, or multiple fusion partners can be linked to the remainder of the polypeptide. For example, two fusion partners at one of the X n or X m positions may be linked to the rest of the polypeptide, or there may be one or more fusion partners at each of the two positions.
  • Particularly suitable fusion partners are proteins which occur naturally in microorganisms, preferably in prokaryotes, in particular in Escherichia coli or Bacillus subtilis.
  • particularly suitable fusion partners are the polypeptides having the sequences yaad (SEQ ID NO: 16 in WO 2006/082251, SEQ ID NO: 15 or 16 in WO 2007/014897), yaae (SEQ ID NO: 18 in WO
  • fusion partners are yaad and truncated sequences derived therefrom, as described in the present description and in WO 2006/082251 and WO 2007/014897.
  • yaad and yaad40 are also suitable.
  • fragments or homologs of said sequences which comprise only one contiguous portion, for example from 70 to 99%, preferably from 5 to 50%, and more preferably from 10 to 40% of the amino acids of said sequences, or in which individual Amino acids, or nucleotides are exchanged with respect to the said sequence, wherein the percentages in each case refers to the total number of amino acids.
  • the hydrophobin optionally in addition to one of the aforementioned fusion partners - as one of the groups X n or X m or as a terminal component of such a group still a so-called affinity domain (affinity tag / aff ⁇ nity tail) on.
  • affinity domains include (His) k, (Arg) k, (Asp) k, (Phe) k or (Cys) k
  • k is generally a natural number from 1 to 10. It is preferably a (His) k group, where k is one of the numbers four to six.
  • the group X n and / or X m can consist exclusively of such an affinity domain or of naturally or not naturally linked to the rest of the polypeptide amino acids or polypeptides and such an affinity domain.
  • the hydrophobin is additionally modified on its polypeptide sequence, for example by glycosylation, acetylation or else by chemical cross-linking, for example with glutaric dialdehyde.
  • Hydrophobins their sequences and their preparation are disclosed, for example, in WO 2006/082251, the contents of which are hereby expressly incorporated into the present invention. Those described in WO2006 / 082251
  • Hydrophobins are preferred for the practice of the present invention.
  • hydrophobins for practicing the present invention are the hydrophobins of the dewA, rodA, hypA, hypB, sc3, basF, basf2 types, more particularly dewA hydrophobins (in the examples in the fusion proteins
  • Hydrophobins of type dewA These hydrophobins and their sequences are disclosed, for example, in WO 2006/082251 and WO 2007/014897, the contents of which are hereby expressly incorporated into the present invention. Unless otherwise indicated, the sequence names given below and SEQ ID NOs refer to sequences disclosed in WO 2006/082251. An overview table with the SEQ ID numbers can be found in WO 2006/082251 on page 20.
  • hydrophobins selected from the group consisting of yaad-Xa-dewA-his (SEQ ID NO: 20), yaad-Xa-rodA-his (SEQ ID NO: 22) and yaad-Xa-basfl-his (SEQ ID NO: 24) with the polypeptide sequences shown in parentheses and the coding therefor
  • Nucleic acid sequences in particular the sequences according to SEQ ID NO: 19, 21, 23. Particularly preferred may yaad-Xa-dewA-his (SEQ ID NO: 20 in WO 2006/082251 or SEQ ID NO: 19 and 20 WO 2007/014897 ) are used. Also, proteins which, starting from the polypeptide sequences shown in SEQ ID NO: 20, 22 or 24, by exchange, insertion or deletion of at least one, preferably up to 5% of all amino acids, more preferably up to ten, most preferably to to give five amino acids, and which still possess at least 50% of the biological property of the starting proteins, are particularly preferred embodiments. The biological property of the proteins is understood here to mean the change in the contact angle described below and / or the effect on keratin described below.
  • Hydrophobins particularly suitable for carrying out the present invention are further derived from yaad-Xa-dewA-his (SEQ ID NO: 20), yaad-Xa-rodA-his (SEQ ID NO: 22) or yaad-Xa-basfl-his ( SEQ ID NO: 24) hydrophobins derived by truncation of the yaad fusion partner.
  • a shortened yaad residue can advantageously be used.
  • the truncated residue should, however, comprise at least 20, preferably at least 35, contiguous amino acids of the yaad sequence.
  • a truncated radical having 20 to 293, preferably 25 to 250, more preferably 35 to 150 and most preferably 35 to 100 amino acids can be used.
  • a particularly suitable protein is yaad40-Xa-dewA-his (SEQ ID NO: 25 and 26 in WO 2007/014897), which has a reduced to 40 amino acids yaad residue.
  • a cleavage site between the fusion partner or fusion partners and the remainder of the polypeptide can be used to cleave off the fusion partner (for example by BrCN cleavage on methionine, factor Xa, enterokinase,
  • Thrombin, TEV cleavage, etc. is particularly preferred.
  • an Xa site e.g. an interface of the hydrophobins used in the examples.
  • hydrophobins are surface-active polypeptides. They can be isolated from natural sources, but can also be obtained by genetic engineering. In principle, both hydrophobins of one and the other origin are suitable for carrying out the present invention.
  • hydrophobins used according to the invention can be prepared chemically by known methods of peptide synthesis, for example by solid phase synthesis according to Merrifield.
  • Naturally occurring hydrophobins can be isolated from natural sources by suitable methods. As an example, let Wösten et. al., Eur. J Cell Bio. 63, 122-129 (1994) or WO 96/41882.
  • hydrophobins from Talaromyces thermophilus which contain no fusion partner
  • the preparation of hydrophobins containing a fusion partner can preferably be carried out by genetic engineering methods in which a nucleic acid sequence coding for the fusion partner and one for the remainder of the polypeptide, in particular DNA sequence, are combined so that in a host organism by gene expression of the combined Nucleic acid sequence, the desired protein is generated.
  • a production method for example, is disclosed by WO 2006/082251 or WO 2006/082253.
  • the fusion partners greatly facilitate the production of hydrophobins. Hydrophobins containing a fusion partner are produced in genetically engineered processes with significantly better yields than hydrophobins that do not contain a fusion partner.
  • hydrophobins produced by the host organisms according to the genetic engineering process can be worked up in a manner which is known in principle and purified by means of known chromatographic methods. In general, isolated, in particular purified, hydrophobins are used to carry out the invention.
  • the fermented cells are first separated from the Fermetationsbrühe, digested and the cell debris from the inclusion bodies
  • inclusion bodies separately.
  • the latter can be done advantageously by centrifuging.
  • the inclusion bodies for example by acids, bases and / or detergents can be digested in a manner known in principle in order to liberate the hydrophobins.
  • the inclusion bodies with the hydrophobins used according to the invention can generally be completely dissolved within about 1 h already using 0.1 M NaOH.
  • the solutions obtained may, if appropriate after adjusting the desired pH, be used for carrying out this invention without further purification.
  • the hydrophobins can also be isolated from the solutions as a solid. The isolation can preferably be carried out by means of spray granulation or spray drying, as described in WO 2006/082253, page 12.
  • the products obtained by the simplified work-up and purification process comprise, in addition to residues of cell debris, usually about 80 to 90% by weight of proteins.
  • the amount of hydrophobins is generally from 30 to 80% by weight with respect to the amount of all proteins.
  • the isolated Hy drophobin- containing products can be stored as solids.
  • hydrophobins can be used as such or after cleavage and separation of the fusion partner for carrying out this invention.
  • a cleavage is advantageously carried out after the isolation of the inclusion bodies and their dissolution.
  • a biological property of the hydrophobins is the change of surface properties when a surface, e.g. a glass surface coated with hydrophobin proteins.
  • the change of the surface properties can be experimentally determined, for example, by the contact angle of a water drop before and after the
  • Coating the surface with the proteins is measured and the difference between the two measurements is determined.
  • contact angle measurements is known in principle to the person skilled in the art.
  • the measurements are carried out at room temperature with a water drop of 5 ⁇ l and using glass slides as substrate.
  • the exact experimental conditions for an example suitable method for measuring the contact angle are shown in Example 10 of WO 2006/136607.
  • the hydrophobins used can increase the contact angle.
  • the hydrophobins can reduce the contact angle by at least 20 °, preferably at least 25 °, particularly preferably at least 30 °; at least 40 °; at least 45 °; in particular at least 50 °, in each case compared with the contact angle of a water droplet of the same size with the uncoated glass surface.
  • the present invention relates to the effect of hydrophobin on the binding of tinting dyes and semipermanent dyes to hair.
  • the binding of hydrophobin to the skin and hair can be tested as described in Examples 1 to 4 (identical to Examples 11 to 14 of WO 2006/136607).
  • compositions of the invention according to embodiments (2) and (3), and compositions for use (4) in the method of embodiment (1) preferably contain the hydrophobin in a concentration of 0.001 to 5% by weight, more preferably in an amount of 0.005 to 3% by weight %, very particularly preferably from 0.01 to 1% by weight of total hydrophobin, based on the total
  • composition Most preferred is a hydrophobin concentration of up to 0.2% by weight, more preferably from 0.01 to 0.05% by weight, most preferably 0.025% by weight.
  • the total hydrophobin is the total amount of hydrophobin molecules of one or more hydrophobin molecular species in the composition. These concentration ranges also indicate the preferred concentrations at which the hydrophobin is applied to the keratin or keratin-containing material in the method of embodiment (1).
  • the said hydrophobin concentrations are either already present in the inventive compositions according to embodiments (2) and (3), or the compositions for use (4) in the process according to embodiment (1), or they are prepared by diluting a concentrate before use of the Composition obtained.
  • the hydrophobin is preferably present in a composition which preferably also contains a cosmetically acceptable carrier medium. This composition may contain only one hydrophobin or else a combination of different hydrophobins, eg a composition comprising two or three hydrophobins.
  • the non-permanent staining of keratin according to the present invention further requires the application of at least one non-permanent dye, more specifically a non-permanent keratin dye, to the keratin to be stained.
  • the non-permanent dye is applied as a component of a composition (colorant) containing the dye.
  • the composition according to embodiment (2) and the kit according to embodiment (3) also relate to such a colorant.
  • This colorant contains either one or more non-permanent dyes, typically several non-permanent dyes, preferably from 2 to 20 or any natural integer, more preferably from 4 to 10 non-permanent dyes.
  • Commercially available tints and non-permanent colorants typically contain more than three different non-permanent dyes to achieve a particular hue (see the colorants used in the examples).
  • non-permanent dyes is expressly referred to the monograph Ch. Zviak, The Science of Hair Care, Chapter 7 (pages 248-250, direct dyes), published as volume 7 of the series 'Oematology' (eds .: Ch., Culnan and H.
  • Non-permanent dyes mentioned in these works are non-permanent dyes suitable for practicing the present invention.
  • Non-permanent dyes in the context of the present invention are preferably substantive dyes.
  • As direct dyes all direct dyes commonly used in hair dyeing can be used.
  • Such substantive dyes are usually nitrophenylenediamines, nitroaminophenols, azo dyes, anthraquinones, tri-phenylmethane dyes, indoanilines or indophenols.
  • Preferred substantive dyes are those under the international designations or trade names HC Yellow 2, HC Yellow 4, HC Yellow 5, HC Yellow 6, HC Yellow 9, HC Yellow 12, HC Yellow 13, Acid Yellow 1, Acid Yellow 10, Acid Yellow 23, Acid Yellow 36, HC Orange 1, Disperse Orange 3, Acid Orange 7, HC Red 1, HC Red 3, HC Red 10, HC Red 11, HC Red 13, Acid Red 33, Acid Red 52, HC Red BN, Pigment Red 57: 1, HC Blue 2, HC Blue 12, Disperse Blue 3, Acid Blue 7, Acid Green 50, HC Violet 1, Disperse Violet 1, Disperse Violet 4, Acid Violet 43, Disperse Black 9, Acid Black 1, and Acid Black 52 known compounds as well as 1,4-diamino-2-nitrobenzene, 2-amino-4-nitrophenol, 1,4-bis ( ⁇ -hydroxyethyl) amino-2-nitrobenzene, 3-nitro-4- ( ⁇ -hydroxyethyl) aminophenol, 2- (2'-hydroxyethyl) amino-4,6-dinitrophenol, 1- (2'-hydroxyethy
  • Preferred substantive dyes are also cationic substantive dyes. Particularly preferred are (a) cationic
  • Triphenylmethane dyes such as Basic Blue 7, Basic Blue 26, Basic Violet 2 and Basic Violet 14, (b) aromatic systems substituted with a quaternary nitrogen group such as Basic Yellow 57, Basic Red 76, Basic Blue 99, Basic Brown 16 and Basic Brown 17, as well as (c) direct dyes containing a heterocycle containing at least one quaternary
  • Nitrogen atom such as Basic Yellow 87, Basic Orange 31 and Basic Red 51.
  • the cationic substantive dyes sold under the trademark Arianors® are, according to the invention, particularly preferred cationic substantive dyes.
  • the at least one non-permanent dye in embodiments (1) to (4) of the present invention is selected from the group consisting of Basic Red 51, Basic Red 76, HC Red No. 10, HC Red No.11, Basic Violet 2, hydroxyethyl 2-nitro-p-toluidine, HC Blue No.2, HC Yellow No.9, HC Yellow No.13, HC Yellow No.2, 2-amino 6-chloro-4-nitrophenol, HC Blue No.12, N, N-bis (2-hydroxyethyl) -2-nitro-p-phenylenediamine, Basic Blue 99, 4-amino-3-nitrophenol, 4-hydroxypropylamino-3-nitrophenol , 3-nitro-p-hydroxyethylaminophenol, HC Blue No.11, Basic Brown 17, HC Red No.1, HC Red No.7, HC Red No.13, HC Orange No.l and HC Red No.3, in particular from Basic Violet 2 and hydroxyethyl 2-nitro-p-toluidine.
  • a combination of several of the most preferred dyes in particular a selection (for example, those in Examples multiply used dyes) or all of the dyes mentioned in the examples.
  • preparations according to the invention may also contain naturally occurring dyes such as those found in henna red, henna neutral, henna black, chamomile flower, sandalwood, black tea, buckthorn bark, sage, bluewood, madder root, catechu, seder and alkano root.
  • naturally occurring dyes such as those found in henna red, henna neutral, henna black, chamomile flower, sandalwood, black tea, buckthorn bark, sage, bluewood, madder root, catechu, seder and alkano root.
  • the non-permanent dye may be basically hydrophobic or hydrophilic.
  • the non-permanent dye in the embodiments (1) to (4) is a hydrophilic dye.
  • the hydrophobin improves its binding to the surface of the keratin because it can make the keratin surface more hydrophilic.
  • hydrophobic dyes can penetrate a hydrophobin layer on the keratin surface and intercalate into the deeper layers. Such stabilized hydrophobic dyes remain longer on the hair. Their use as non-permanent dyes is therefore also an aspect of the present invention.
  • the use of at least one hydrophilic dye in the colorant is preferred.
  • the majority of non-permanent dyes present in the colorant are hydrophilic (greater than 50% by weight, based on the total colorants), most preferably all non-permanent dyes present in the colorant are hydrophilic.
  • the colorants according to the invention or used according to the invention preferably contain the non-permanent dyes in a concentration of 0.001 to 20% by weight, more preferably in a concentration of 0.001 to 10% by weight, very particularly preferably of 0.1 to 5% by weight. based on the total colorant. It is not necessary for the non-permanent dyes to be the same as each other. Rather, in the hair colorants according to the invention, due to the production process for the individual dyes, in minor amounts, other components may be included, as far as they do not adversely affect the dyeing result or for other reasons, eg. As toxicological, must be excluded.
  • compositions useful in the practice of the present invention may also contain one or more permanent dyes or their precursors. However, the use of compositions without such permanent dyes or their precursors is preferred.
  • the nonpermanent dye is a component of a colorant, preferably a hair colorant, a skin colorant or a nail colorant, in particular for coloring human hair, skin or nails.
  • the colorant is particularly preferably a hair colorant, very particularly preferably a hair colorant, a semi-permanent or a demipermanent hair colorant.
  • the colorant is a tint or semipermanent hair dye, most preferably a semipermanent hair dye.
  • the non-permanent dye is preferably applied to the keratin or keratin-containing material in process (1) as a component of such a composition.
  • the colorant generally contains at least one cosmetically acceptable carrier medium and may additionally contain other ingredients customary in cosmetics.
  • the colorant can - as it is often commercially available - ammonia or an ammonia salt such as NH 4 Cl included.
  • an ammonia salt such as NH 4 Cl included.
  • the presence of ammonia is not absolutely necessary.
  • the inventive Compositions and the compositions used for the process according to embodiment (1) and the use according to embodiment (4) no ammonia or no ammonia salt.
  • the hydrophobin and non-permanent dye may be applied to the keratin separately (in separate compositions) or as a combination in a single composition.
  • the hydrophobin and the non-permanent dye are preferably applied separately from each other or in separate compositions.
  • the hydrophobin and non-permanent dye may further be applied either simultaneously or sequentially to the keratin or keratin-containing material. Preferably, they are applied successively.
  • process (1) may include one or more steps.
  • process (1) comprises at least the following steps: (a) applying at least one hydrophobin of structural formula (I) to the keratin; and
  • steps (b) and (b) are performed either simultaneously or sequentially.
  • the hydrophobin or the non-permanent dye is preferably contained in a composition which contains further cosmetically acceptable ingredients.
  • steps (a) and (b) are carried out simultaneously, only one composition is applied to the hair, which then contains both the hydrophobin and the non-permanent dye.
  • This composition can be prepared by mixing two separate compositions, one containing the hydrophobin and the other the non-permanent dye.
  • the hydrophobin preferably in the form of a hydrophobin-containing composition, is first applied to the hair. This composition acts on the keratin for a certain exposure time. Thereafter, a composition is applied to the hair containing at least one non-permanent dye.
  • the application of the last-mentioned composition can be directly followed by the action time of the hydrophobin-containing composition, or further steps (ie one or more steps) for the treatment of keratin are carried out between steps (a) and (b).
  • these further steps may be any measures for the cosmetic treatment of the hair as long as they neither remove the hydrophobin layer nor affect the final result of the dyeing.
  • these further steps are selected from the group consisting of: one or more washings of the keratin, one or more times drying of the keratin at
  • Such a further step of process (1) is particularly preferably the drying of the keratin or keratin-containing material after application of the
  • the keratin is dried between steps (a) and (b).
  • the keratin to terminate the contact time of the hydrophobin-containing composition by applying warm air, for example air at a temperature of> 30 0 C, preferably from 50 0 C ⁇ 5 0 C, by means of a hot air source (such as Hair dryer or other hot air source that can generate temperatures such as a hair dryer) or dried at room temperature.
  • a hot air source such as Hair dryer or other hot air source that can generate temperatures such as a hair dryer
  • the keratin is dried immediately after the exposure time of the hydrophobin by a hair dryer, as in Example 5, variant (b) is the case before the dye is applied to the hair.
  • Dye is removed in a further preferred aspect of the method (1) not bound to the keratin part of the applied hydrophobin from the keratin to be dyed, in particular by washing. More preferably, the remainder of the applied hydrophobin-containing composition is washed out to complete its exposure time and / or after the above-described drying of the keratin at the end of the exposure time before step (b) is performed.
  • the keratin is most preferably dried after washing, but preferably not heated (ie, dried at room temperature, for example), and only then is the composition containing the dye applied to the keratin.
  • the keratin is dried immediately following the exposure time of the hydrophobin before the next steps are performed.
  • the drying is carried out by applying warm air, for example air at a temperature of> 30 0 C, preferably from 50 0 C ⁇ 5 0 C, by means of a hot air source, preferably with a hair dryer.
  • the time interval between the end of step (a) and the beginning of step (b) should not be increased unnecessarily in a sequential execution ((b) after (a)) by this further step or these further steps. It is preferably at most 2 hours, more preferably from 2 to 70 minutes, most preferably from 4 to 30 minutes, and most preferably from 5 to 15 minutes.
  • the exposure time of the hydrophobin-containing composition may be up to 2 hours. It is preferably from 2 to 90 minutes, for example from 3 to 70 minutes, from 4 to 30 minutes, or from 5 to 15 minutes.
  • step (b) is preferably carried out with a commercial colorant according to the manufacturer, but can also be carried out with other compositions containing a non-permanent dye.
  • the keratin can be washed and dried.
  • the steps of the method (1) can also be repeated several times.
  • Example 5 The sequence and nature of the individual steps in Example 5 is a preferred way of carrying out the process (1) according to the invention. From these steps, a selection can be made, as far as it meets the above requirements.
  • Both the non-permanent dye and the hydrophobin are preferably contained (separately or as a combination) in a composition.
  • the compositions according to the invention are preferably cosmetic
  • compositions In addition to hydrophobin and / or non-permanent dye, they generally contain a cosmetically acceptable medium and suitable further ingredients which support the cosmetic effect, in particular auxiliaries and additives customary in hair treatment compositions. These ingredients should not adversely affect the staining result.
  • suitable further ingredients which support the cosmetic effect, in particular auxiliaries and additives customary in hair treatment compositions. These ingredients should not adversely affect the staining result.
  • Such basic formulations for cosmetic compositions and the ingredients suitable therefor are well known to the person skilled in the art and can be found in cosmetics manuals, such as, for example, in Schrader, bases and formulations of cosmetics, Wegig Verlag, Heidelberg, 1989, or Umbach, cosmetics: development, production and application of cosmetic products, 2nd extended edition, 1995, Georg Thieme Verlag.
  • compositions of the invention are i.a. as cosmetic preparations, for example as creams, emulsions, gels or surfactant-containing foaming solutions, e.g. Shampoos, foam aerosols or other preparations suitable for use on the hair.
  • Usual constituents of such aqueous cosmetic preparations are, for.
  • As wetting and emulsifying agents such as anionic, nonionic and ampholytic surfactants, eg.
  • anionic, nonionic and ampholytic surfactants eg.
  • fatty alcohol sulfates, alkanesulfonates, ⁇ -olefinsulfonates, Fettalkoholpolyglykolethersulfate, Ethylenoxidenvironrungs eg.
  • fatty alcohol sulfates, alkanesulfonates, ⁇ -olefinsulfonates, Fettalkoholpolyglykolethersulfate, Ethylenoxidenvironrungs eg.
  • fatty alcohol sulfates, alkanesulfonates, ⁇ -olefinsulfonates, Fettalkoholpolyglykolethersulfate, Ethylenoxidenvironrungs eg.
  • methyl or hydroxyethyl cellulose starch, fatty alcohols, paraffin oils, fatty acids, perfume oils and hair care additives such.
  • water-soluble cationic ampholytic and anionic polymers protein derivatives, pantothenic acid, cholesterol, dyes, drugs such as panthenol, allantoin, Pyrrolidoncarbonklaren and their salts, plant extracts and vitamins, light stabilizers, bodying agents such as sugar esters, polyol esters or Polyolalkylether, waxes such as beeswax and montan wax, complexing agents such as EDTA, NTA and phosphonic acids, swelling and penetrating agents such as glycerol, propylene glycol monoethyl ether, carbonates, bicarbonates, guanidines, ureas and primary, secondary and tertiary phosphates, pearlescing agents such as ethylene glycol mono- and distearate, propellants such as propane-butane mixtures, N
  • the erf ⁇ ndungswashen compositions can, irrespective of the type of cosmetic preparation z.
  • B. as a cream, gel or shampoo have a weakly acidic, neutral or alkaline pH. Preference is given to a pH range from 6 to 8. The adjustment of the pH is carried out with the aid of customary pH adjusters, but preferably not with ammonia or other chemicals considered harmful.
  • compositions according to the invention in addition to either hydrophobin or non-permanent dye or in addition to a combination of the two said ingredients, additionally contain at least one cosmetically active ingredient, the uptake and / or effect of which is improved by the presence of hydrophobin, or this is cosmetically active Ingredient is applied separately (in pure form or as part of a composition).
  • the additional cosmetically active ingredient is preferably hydrophilic.
  • effector molecules Preferred cosmetically active ingredients whose uptake is improved by hydrophobin are described in WO 2006/136607 as "effector molecules", to the corresponding passages of which reference is expressly made.
  • effector molecules can be used as cosmetically active ingredients in the compositions according to the invention.
  • effector molecule refers to molecules which have a certain, predictable effect. These may be either proteinaceous molecules, such as enzymes, or else non-proteinogenic molecules, such as dyes, light stabilizers, vitamins and fatty acids, sugars or metal ion-containing compounds.
  • sugars are glucans and especially sugars of natural origin, such as e.g. from honey or grain, preferred.
  • enzymes peptides and antibodies are preferred.
  • oxidases peroxidases, proteases, tyrosinases, metal-binding enzymes, lactoperoxidase, lysozyme, amyloglycosidase, glucose oxidase, superoxide dismutase, photolyase, calalase.
  • Hydroxylates of proteins from plant and animal sources for example hydro lysates of proteins of marine origin, milk or silk hydrolysates, are also very suitable as proteinaceous effector molecules.
  • peptides used for anti-aging such as Matrixyl (INCI name glycerol-water-butylene glycol-carbomer-polysorbate 20-palmitoyl pentapeptide-4), Argireline (INCI name Aqua, acetyl-hexapeptide-3) , Rigin (INCI Name Water (and) Glycerin (and) Steareth-20 (and) Palmitoyl tetrapeptide-7), Eyeliss (INCI Name Water-Glycerol-Hespiridine Methyl Chalcone-Steareth-20-Dipeptide-2-Palmitoyl Tetrapeptide-7) Regu-Age (INCI Name Oxido Reductases-Soy Peptides-Hydrolyzed Rice Bran Extract) and Melanostatin 5 (INCI name aqua-dextran-nonapetide-1).
  • Matrixyl INCI name glycerol-water-butylene glycol-car
  • non-proteinaceous effector molecules are non-protein anti-aging agents, e.g. Caffeine, and antioxidants are preferred as effector molecules.
  • Antioxidants also referred to as radical scavengers, are capable of neutralizing so-called free radicals. These are aggressive compounds that are physiologically involved in numerous metabolic processes and the
  • Antioxidants include carotenoids, ascorbic acid (vitamin C, E 300) as well as sodium L-ascorbate (E 301) and calcium L-ascorbate (E 302); Ascorbyl palmitate (E 304); Butylhydroxyanisole (E 320); Butylhydroxytoluene (E 321); Calcium disodium EDTA (E 385); Gallate as well as propyl gallate (E 310), octyl gallate (E 311) and dodecyl gallate (lauryl gallate) (E 312); Isoascorbic acid (E 315) as well as sodium isoascorbate (E 316); Lecithin (E 322); Lactic acid (E 270); Multiple-
  • Phosphates such as diphosphates (E 450), triphosphates (E 451) and polyphosphates (E 452); Sulfur dioxide (E 220) as well as sodium sulphite (E 221), sodium bisulphite (E 222), sodium disulphite (E 223), potassium sulphite (E 224), calcium sulphate (E 226), calcium bisulphite (E 227) and potassium bisulphite (E 228); Selenium; Tocopherol (vitamin E, E 306) as well as alpha-tocopherol (E 307), gamma-tocopherol (E.
  • At least one compound from the above-mentioned group of antioxidants is selected as the antioxidant.
  • carotinoids are to be understood as meaning the following compounds: beta-carotene, lycopene, lutein, astaxanthin, zeaxanthin, cryptoxanthin, citranaxanthin, canthaxanthin, bixin, beta-apo-4-carotenal, beta-apo-8-carotenal, beta-apo -8-carotenoic acid ester, singly or as a mixture.
  • carotenoids are beta-carotene, lycopene, lutein, astaxanthin, zeaxanthin, citranaxanthin and canthaxanthin.
  • retinoids in the context of the present invention is meant vitamin A alcohol (retinol) and its derivatives such as vitamin A aldehyde (retinal), vitamin A acid (retinoic acid) and vitamin A esters (e.g., retinyl acetate, retinyl propionate and retinyl palmitate).
  • retinoic acid encompasses both all-trans retinoic acid and 13-eis retinoic acid.
  • the terms retinol and retinal preferably include the all-trans compounds.
  • the preferred retinoid used is all-trans retinol, referred to below as retinol.
  • effector molecules are vitamins, especially vitamin A, and their esters.
  • Vitamins are essential organic compounds which are either not synthesized in the animal and human organism or only in insufficient quantities. Based on this definition, 13 components or groups of components have been classified as vitamins.
  • the fat-soluble vitamins include vitamin A (retinol), vitamin D (calciferols), vitamin E (tocopherols, tocotrienols) and vitamin K (phylloquinone).
  • the water-soluble vitamins include vitamin B1 (thiamine), vitamin B2 (riboflavin), vitamin B6 (pyridoxal group), vitamin B12 (cobalamins), vitamin C (L-ascorbic acid), pantothenic acid, biotin, folic acid and niacin.
  • Vitamins, provitamins and vitamin precursors from groups A, C, E and F in particular 3,4-didehydroretinol, beta-carotene (provitamin of vitamin A), ascorbic acid (vitamin C), and the palmitic acid esters, glucosides or phosphates of ascorbic acid, tocopherols , in particular a-tocopherol and its esters, eg the acetate, nicotinate, phosphate and succinate; vitamin F, which is understood as meaning essential fatty acids, especially linoleic acid, linolenic acid and arachidonic acid.
  • Vitamin E is a collective term for a group of (to date) eight fat-soluble substances with antioxidant and non-antioxidant effects. Vitamin E is part of all membranes of animal cells, but is formed only by photosynthetically active organisms such as plants and cyanobacteria.
  • Four of the eight known Vita-min E forms are called tocopherols (alpha-tocopherol, beta-tocopherol, gamma-tocopherol and delta-tocopherol).
  • the other four forms of vitamin E heretofore known are tocotrienols (alpha tocotrienol, beta tocotrienol, gamma tocotrienol and delta tocotrienol).
  • derivatives of these substances such as alpha-tocopheryl acetate may also be advantageous.
  • Vitamin A and its derivatives and provitamins advantageously show a particular skin-smoothing effect.
  • vitamins, provitamins or vitamin D precursors of the vitamin B group or derivatives thereof which are preferably to be used according to the invention and the derivatives of 2-furanone include, inter alia: Vitamin Bl, common name thiamine, chemical name 3 - [(4'-amino-2'-methyl-5'-pyrimidinyl) methyl] -5- (2-hydroxyethyl) -4-methylthiazolium chloride.
  • Vitamin B2 common name riboflavin, chemical name 7,8-dimethyl-10- (l-D-ribityl) benzo [g] pteridine-2,4 (3H, 10H) -dione.
  • riboflavin z. B. in Mol-ke other riboflavin derivatives can be isolated from bacteria and yeasts.
  • a stereoisomer of riboflavin which is likewise suitable according to the invention is the lyxoflavin which can be isolated from fishmeal or liver and carries a D-arabityl residue instead of the D-ribityl.
  • Vitamin B3 the compounds nicotinic acid and nicotinamide (niacinamide) are often performed.
  • Preferred according to the invention is the nicotinic acid amide.
  • Vitamin B5 pantothenic acid and panthenol
  • Panthenol is preferably used.
  • Suitable derivatives of panthenol according to the invention are, in particular, the esters and ethers of panthenol and also cationically derivatized panthenols.
  • Particularly preferred derivatives are the substances which are also commercially available
  • Vitamin B6 which is understood hereunder no uniform substance, but the known under the common names pyridoxine, pyridoxamine and pyridoxal derivatives of 5-hydroxymethyl-2-methylpyridin-3-ols.
  • Vitamin B7 also known as vitamin H or "skin vitamin”.
  • Biotin is (3aS, 4S, 6aR) -2-oxohexahydrothienol [3,4-d] imidazole-4-valeric acid.
  • vitamins salts, esters, sugars, nucleotides, nucleosides, peptides and lipids
  • suitable derivatives of vitamins salts, esters, sugars, nucleotides, nucleosides, peptides and lipids
  • nucleic acids such as DNA and RNA may be suitable effector molecules, e.g. as a moisturizer.
  • Preferred lipophilic, oil-soluble antioxidants from this group are tocopherol and its derivatives, gallic acid esters, flavonoids and carotenoids, and butylhydroxytoluene / anisole.
  • As water-soluble antioxidants are amino acids, eg. As tyrosine and cysteine and their derivatives and tanning agents, especially those of plant origin are preferred.
  • Triterpenes in particular triterpenic acids such as ursolic acid, rosmarinic acid, betulinic acid, boswellic acid and bryonic acid.
  • Further preferred effector molecules are, preferably low-dose, fruit acids (alpha hydroxy acids) such as malic acid, citric acid, lactic acid, tartaric acid, glycolic acid. These may be present in concentrations of 0.1% to 35%, preferably 0.1% to 10%, in particular 1% to 10%, 1% to 5%, based on the total weight of the composition. Further preferred effector molecules are urea and derivatives thereof, as they can care for the scalp. These may be present in concentrations of 0.1% to 25%, preferably 0.1% to 10%, in particular 1% to 10%, 1% to 5%, based on the total weight of the composition. Urea and its derivatives are not to be equated with ammonia, which is preferably not used in the compositions and methods of the invention.
  • UV light protection filters in particular the UV filters mentioned in WO 2006/136607.
  • Such further cosmetically active ingredients are keratin-care substances and skin-care substances, in particular water-soluble vitamins, antioxidants, UV filters, glucans, flavonoids, and caffeine.
  • vitamin C niacin (nicotinic acid, vitamin B3), pantothenic acid and panthenol (vitamin B5), vitamin B6, biotin (vitamin B7, vitamin H), vitamin B9 (folic acid) and vitamin B 12 or their derivatives.
  • Panthenol, pantolactone, nicotinic acid amide, sodium ascorbyl phosphate and biotin are very particularly preferred according to the invention.
  • UV filters water-soluble UV filters are preferred, Uvinul MS 40, Uvinul P 25, Uvinul DS 49 and Z-COTE are particularly preferred, and Uvinul MS 40 and P 25 are very particularly preferred.
  • Uvinul MS 40 and P 25 are very particularly preferred.
  • antioxidants flavonoids phenolic acids and polyphenols are preferred.
  • cosmetically active ingredients selected from the group consisting of panthenol, ascorbic acid and its derivatives, water-soluble UV filters, caffeine.
  • Aqueous extracts of fruits and herbs may also be part of the compositions of the invention.
  • a specific embodiment of the present invention is the kit (3).
  • Kit comprises two separate cosmetic compositions, namely
  • the simultaneous application or application in the order (i) - (u) of the two compositions (i) and (ii) causes an increase in the color intensity and / or color stability of the dyeing compared to the sole use of the composition (ii).
  • composition (ii) is preferably a conventional colorant for tinting, semi- or demipermanent coloring of hair.
  • composition (i) or (ii) or both compositions in the kit additionally contain at least one cosmetically active ingredient, the uptake and / or effect of which is improved by the presence of hydrophobin.
  • the kit may also comprise a further composition (iii) containing such a cosmetically active ingredient.
  • hydrophobin is used to enhance the effect of nonpermanent dyeing of keratin or keratin containing material.
  • the hydrophobin used is defined as described above for the other embodiments.
  • the non-permanent dye used is as defined above.
  • hydrophobins used in the examples were prepared according to the examples of Part A of WO 2007/014897.
  • the sequence of the "hydrophobin A” used in the examples is given in WO 2007/014897 under SEQ ID NO: 19 and 20.
  • This "hydrophobin A” is the hydrophobin dewA, which was fused with the protein yaad.
  • the construct also contains an Xa interface and a tag (yaad-Xa-dewA-his).
  • hydrophobin B used in the examples is given in WO 2007/014897 under SEQ ID NO: 25 and 26.
  • This "hydrophobin B” is the hydrophobin dewA fused with the truncated yaad protein.
  • the construct also contains an Xa-interface and a His-tag (yaad40-Xa-dewA-his).
  • TBS 2OmM Tris; 15 mM NaCl pH 7.5
  • TTBS TBS + 0.05% Tween20
  • the first step is the transfer of the outer keratin layer from the skin to a stable carrier.
  • a transparent adhesive strip was firmly applied to depilated human skin and removed again.
  • the test can be performed directly on the transparent adhesive strip or through the adhering keratin layer re-gluing be transferred to a glass slide.
  • the binding was detected as follows: transfer to incubation with the different reagents
  • Washed 1x 5 min with TBS incubation with the hydrophobin to be tested (coupled to tag - e.g.
  • a blue color precipitate indicates that hydrophobin has bound to the skin.
  • the binding to nails can be determined analogously by incubating the hydrophobins to be investigated directly with the nail surface and measuring them accordingly.
  • the binding to mucous membrane can be measured by measuring mucous membrane (for example, human oral mucosa) by means of a
  • a quantitative assay was developed (Fig. 2 in WO 2006/136607).
  • hair was first incubated with hydrophobin and washed off excess hydrophobin.
  • an antibody-peroxidase conjugate was coupled via the His-tag of the hydrophobin. Unbound antibody-peroxidase conjugate was rinsed off again.
  • the bound antibody-peroxidase conjugate [Monoclonal Antipoly-Histidine Peroxidase Conjugate, produced in mouse, lyophilized powder, Sigma Company] can convert a colorless substrate (TMB) into a colored product that is photometrically measured at 405 nm.
  • the amount of absorption indicates the amount of bound hydrophobin or control protein.
  • YaaD from B.subtilis was chosen as the comparison protein and likewise had a His tag for detection, as is necessary for this test.
  • His tag instead of the His tag, other specific antibodies conjugated to peroxidase may also be used.
  • BSA bovine serum albumin
  • PBS phosphate buffered saline
  • Tween 20 polyoxyethylene sorbitan monolaureate, n about 20
  • hydrophobin-based binding test on hair showed a clear superiority of the binding of hydrophobin to hair compared to a substantially poorer binding of the control protein YaaD:
  • Table 1 Quantitative Hydrophobin Activity Test Hair: 1) Buffer; 2) comparative protein yaad; 3) hydrophobin. The table shows the measured absorbance values at 405 nm.
  • Example 4 Derivatization of hydrophobin with dye "Alexa" and binding to hair
  • a coupling of dyes to hydrophobins can take place via the SH groups of the cysteines. Before coupling the dye Alexa Fluor 532, the disulfide bridges of the hydrophobin are split:
  • the coupling of the dye is carried out according to the manufacturer's instructions (Alexa 532 Protein Labeling Kit, Molecular Probes, MP-A-10236).
  • the coating of human hair with Alexa-coupled hydrophobin is performed as follows: Incubate 10 mg human hair with 50 ⁇ g / ml Alexa-hydrophobin or control protein yaad or uncoupled dye Alexa 532 in buffer TBS for 24 hours at room temperature. Wash twice with TBS / 0.05% Tween 20 - Wash Ix with TBS
  • Example 5 Improved uptake and binding of the dyes of semi-permanent hair dyes by hydrophobin-treated hair
  • step 2 Commercially available preparations (step 2) for semi-permanent hair dyeing were tested, namely
  • HC Blue No.2 HC Yellow No.13, HC Yellow No.2, hydroxyethyl 2-nitro-p-toluidine, 2-amino-6-chloro-4-nitrophenol, HC Blue No.12, N, N Bis (2-hydroxyethyl) -2-nitro-p-phenylenediamine, Basic Blue 99, 4-amino-3-nitrophenol, 4-hydroxypropylamino-3-nitrophenol, 3-nitro-p-hydroxyethylaminophenol, HC Blue No.11, Basic Brown 17, HC Red No.1, HC Red No.7, HC Red No.13, HC Orange No. 1, Basic Violet No.2, HC Red No.3. The tests were carried out as follows:
  • the hair was evaluated in comparison to hair treated with the control solution without hydrophobin. Particularly in the case of test variant (b), it was possible to detect a stronger color intensity in the hair treated with hydrophobin A and B, which is indicative of enhanced color binding and dye uptake compared to hair treated with reference solution. The dyestuff remained longer in the hair even after repeated washing out than without hydrophobin treatment.
  • test variant (a) it was also evident that the dyestuff was retained longer in the hair when washed several times than without hydrophobin.
  • the color intensity was also increased in test variant (a) compared to the comparison solution-treated hair.
  • the hydrophobin B (SEQ ID NO: 26 in WO 2007/014897) treated and untreated hair were tinted with L'Oreal Si-Naturelle Foam Tint No. 01 (composition: Aqua, laureth-12, behentrimonium chloride, dimethyl ether, cetearyl alcohol , isobutane, glycol distearate, amodimethicone, butane, propane, HC red no.3, hydroxyethyl cellulose, hydroxyanthraquinone aminopropyl methyl morpholinium, methyosulfate, HC blue no.2, sodium lauryl sulfate, basic red 51, basic blue 99, trideceth-12, methylparaben, HC yellow no.9, cetrimonium chloride, butylparaben, ethylparaben, isobutylparaben, propylparaben, perfume).
  • Minolta CR-300 and Process Unit Minolta DP-301 Konica Minolta Sensing, Inc., Osaka, Japan
  • Minolta DP-301 Konica Minolta Sensing, Inc., Osaka, Japan
  • ⁇ E is a measure of the color difference (synonym: color difference) between a sample color and a comparative color, measured and calculated according to CIE 1976,
  • ⁇ E values were determined fully automatically according to the manufacturer's instructions by the photometer CR-300 according to the Chroma-Meter CR-300 / CR-310 / CR-331, Minolta, German version, version number: 527 349 / 9.99.
  • the ⁇ E values are usually between 2 and 5 for noticeable color differences, with a very good result above 5, which indicates a clear color difference (the presence of a different color) with the naked eye (http://en.wikipedia.org/ wiki / Delta_E):

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Abstract

L'invention concerne l'utilisation d'hydrophobine dans la coloration non permanente de la kératine et de matériaux contenant de la kératine, en particulier, des cheveux, ainsi qu'un procédé correspondant de coloration non permanente de la kératine, en particulier, des cheveux. Elle concerne, de plus, des moyens de coloration non permanente de la kératine et de matériaux contenant de la kératine, en particulier, des cheveux, lesdits moyens contenant de l'hydrophobine.
EP09781840A 2008-08-18 2009-08-14 Utilisation d'hydrophobine dans la coloration non permanente de la kératine Withdrawn EP2344117A2 (fr)

Priority Applications (1)

Application Number Priority Date Filing Date Title
EP09781840A EP2344117A2 (fr) 2008-08-18 2009-08-14 Utilisation d'hydrophobine dans la coloration non permanente de la kératine

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EP08162556 2008-08-18
EP09781840A EP2344117A2 (fr) 2008-08-18 2009-08-14 Utilisation d'hydrophobine dans la coloration non permanente de la kératine
PCT/EP2009/060537 WO2010020587A2 (fr) 2008-08-18 2009-08-14 Utilisation d'hydrophobine dans la coloration non permanente de la kératine

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EP2344117A2 true EP2344117A2 (fr) 2011-07-20

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JP2010539125A (ja) * 2007-09-13 2010-12-16 ビーエーエスエフ ソシエタス・ヨーロピア 浸透増強剤としてのハイドロフォビンポリペプチドの使用
CN102341464A (zh) * 2009-03-09 2012-02-01 巴斯夫欧洲公司 水溶性聚合物和疏水蛋白的混合物在增稠水相中的用途
EP2605742A1 (fr) * 2010-08-20 2013-06-26 Unilever PLC Composition de traitement capillaire
CN105581917B (zh) * 2016-02-23 2016-08-24 广州市高姿化妆品有限公司 增加角蛋白纤维，特别是毛发的抗拉强度和延伸性的化妆品组合物
CN112336643B (zh) * 2020-10-10 2022-07-19 中芯生物科技(浙江)有限公司 蚕丝蛋白作为染发剂染料的载体的应用及毛发染色方法

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DE10019404A1 (de) * 2000-04-19 2001-10-25 Henkel Kgaa Haarfärbeverfahren
FR2833490B1 (fr) * 2001-12-14 2004-12-10 Oreal Utilisition cosmetique d'au moins une hydrophobine pour le traitement des matieres keratiniques et compositions mises en oeuvre
EP1891261A2 (fr) * 2005-06-06 2008-02-27 Basf Aktiengesellschaft Procede d'enduction de surfaces de substrats fibreux
DE102005029704A1 (de) * 2005-06-24 2007-01-11 Basf Ag Verwendung von Hydrophobin-Polypeptiden sowie Konjugaten aus Hydrophobin-Polypeptiden mit Wirk-oder Effektstoffen und ihre Herstellung sowie deren Einsatz in der Kosmetik
JP2010539125A (ja) * 2007-09-13 2010-12-16 ビーエーエスエフ ソシエタス・ヨーロピア 浸透増強剤としてのハイドロフォビンポリペプチドの使用

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JP2012500241A (ja) 2012-01-05
CN102186455A (zh) 2011-09-14
CA2733760A1 (fr) 2010-02-25
WO2010020587A3 (fr) 2011-04-21
US20110192416A1 (en) 2011-08-11

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