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US20060171885A1 - Skin or hair binding peptides - Google Patents

Skin or hair binding peptides Download PDF

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Publication number
US20060171885A1
US20060171885A1 US10/533,701 US53370103A US2006171885A1 US 20060171885 A1 US20060171885 A1 US 20060171885A1 US 53370103 A US53370103 A US 53370103A US 2006171885 A1 US2006171885 A1 US 2006171885A1
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Prior art keywords
seq
binding peptide
skin
hair
sequence
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Inventor
Giselle Janssen
Christopher Murray
Deborah Winetzky
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Danisco US Inc
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Individual
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Priority to US10/533,701 priority Critical patent/US20060171885A1/en
Assigned to GENENCOR INTERNATIONAL, INC. reassignment GENENCOR INTERNATIONAL, INC. ASSIGNMENT OF ASSIGNORS INTEREST (SEE DOCUMENT FOR DETAILS). Assignors: JANSSEN, GISELLE, WINETZKY, DEBORAH, MURRAY, CHRISTOPHER J.
Publication of US20060171885A1 publication Critical patent/US20060171885A1/en
Priority to US12/534,695 priority patent/US8546528B2/en
Priority to US14/012,863 priority patent/US8816048B2/en
Priority to US14/307,876 priority patent/US20140364584A1/en
Abandoned legal-status Critical Current

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    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
    • C07K7/04—Linear peptides containing only normal peptide links
    • C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
    • 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
    • A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q5/00—Preparations for care of the hair
    • A61Q5/02—Preparations for cleaning the hair
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
    • C07K1/04—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length on carriers
    • C07K1/047—Simultaneous synthesis of different peptide species; Peptide libraries
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
    • C07K7/04—Linear peptides containing only normal peptide links
    • C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09—Recombinant DNA-technology
    • C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
    • C12N15/1034—Isolating an individual clone by screening libraries
    • C12N15/1037—Screening libraries presented on the surface of microorganisms, e.g. phage display, E. coli display

Definitions

  • anti-targets Various methods may be used for the selection and identification of compounds capable of binding specifically to a target in the presence of undesired background targets (anti-targets) using libraries of similar compounds.
  • This invention is directed to peptides that bind specifically to a target such as skin or hair in the presence of an anti-target.
  • the anti-target is hair when the target is skin and the anti-target is skin when the target is hair.
  • Biopanning in its simplest form is an in vitro selection process in which a library of phage-displayed peptides is incubated with a target. The target and phage are allowed to bind and unbound phage are washed away. The specifically bound phage are then acid eluted. The eluted pool of phage is amplified in vivo and the process is repeated. After a number of rounds individual clones are isolated and sequenced.
  • WO 98/54312 discloses selection of antibodies under mild conditions with high affinities for antigens using antibody libraries displayed on ribosomes.
  • the invention concerns a peptide which binds to skin but not to hair, and in a second aspect the invention concerns a peptide which binds to hair but not to skin.
  • the invention concerns a skin binding peptide including (a) any one of SEQ ID NOs. 1-24 or (b) an amino acid sequence having at least 50% sequence identity to any one sequence of SEQ ID NOs. 1-24 and including a sequence cluster selected from the group consisting of APQQRPMXTXXX (SEQ ID NO. 25); PPWXXXL (SEQ ID NO. 26); XXTXLTS (SEQ ID NO. 27); XPPLLXL (SEQ ID NO. 28); SXPSGAX (SEQ ID NO. 29); XQATFXXNXXXX (SEQ ID NO. 30); VXTSQLXXXXXX (SEQ ID NO. 31); LXXRMK (SEQ ID NO. 32), and HXXXYLT (SEQ ID NO. 33), wherein X represents any L-amino acid.
  • a skin binding peptide of the invention includes a C-C derivative.
  • Particularly preferred skin binding peptides of the invention include a peptide having the amino acid sequence of SEQ ID NO. 1; a peptide including the sequence cluster of sequence XQATFXXNXXXX (SEQ ID NO. 30); a peptide having the amino acid sequence of SEQ ID NO. 5; a peptide having the sequence cluster of sequence LXXXRMK (SEQ ID NO. 32) and a peptide having the sequence cluster of APQQRPMXTXXX (SEQ ID NO. 25).
  • the invention concerns a composition comprising one or more skin binding peptides as disclosed herein.
  • the invention concerns a hair binding peptide including (a) any one of SEQ ID NOs. 34-56 or (b) an amino acid sequence having at least 50% sequence identity to any one sequence of SEQ ID NOs. 34-56 and including a sequence cluster selected from the group consisting of NTPXXNX (SEQ ID NO. 57); PXXXLST (SEQ ID NO. 58); TXPTHR (SEQ ID NO. 59); LXTXSTP (SEQ ID NO. 60); and TPLTXXT (SEQ ID NO. 61) and XQXHNPP (SEQ ID NO. 62), wherein X represents any L-amino acid.
  • a hair binding peptide of the invention includes a C-C derivative.
  • the invention concerns a composition comprising one or more hair binding peptides as disclosed herein.
  • FIG. 1 is a general schematic diagram of a targeting method which maybe used to select for the skin or hair binding peptides identified herein.
  • the method comprises the steps of, a) selection against anti-targets which provides a library of ligands depleted of anti-target bound ligands, b) selection for the target by formation of a target-bound ligand complex, c) separation of the target-bound ligand complex, d) identification of the target-bound ligands, and e) optionally sequencing the target-bound ligands, exposing the target-bound ligands to additional rounds of selective targeting, and/or diversification.
  • FIG. 2 illustrates the stability of phage-peptide libraries (Ph.D. 7, Ph.D. C7C and Ph.D.12) in Neutrogena® shower Shampoo.
  • FIG. 3 illustrates the stability of phage-peptide libraries (Ph.D. 7, Ph.D. C7C and Ph.D.12) in Neutrogena® Bath Gel.
  • ligand refers to a molecule or compound that is recognized by a particular target or anti-target. The term is independent of molecular size or compositional feature.
  • the ligand may serve as a substrate for an enzyme-catalyzed reaction, as an agonist, as an antagonist, act as a signal messenger, or stimulate or inhibit metabolic pathways.
  • Ligands may be nucleic acids, peptides, peptide derivatives, peptidomimetics, polypeptides, small organic molecules, carbohydrates and other molecules that are isolated from a candidate mixture that acts on a target in a desirable manner. Preferably the desirable manner is binding the target.
  • a library refers to a collection of chemical or biological entities that can be created in a single reservoir and simultaneously screened for a desired property.
  • a library can have a minimum size of at least two members and may contain as many as 10 15 members.
  • the library has at least 10 2 members.
  • the library has at least 10 3 members.
  • the library has at least 10 6 members.
  • the library has at least 10 9 members.
  • the size of a library refers to the total number of entities comprising the library whether the members are the same or different.
  • a “peptide library” refers to a set of peptides and to the peptides and any fusion proteins containing those peptides. Stochastic or random processes may be used to construct random peptides. The term “random” does not mean that the library composition is not known.
  • peptide refers to an oligomer in which the monomeric units are amino acids (typically, but not limited to L-amino acids) linked by an amide bond.
  • Peptides may be two or more amino acids in length.
  • Peptides identified according to the invention are preferably less than 50 amino acids in length, more preferably less than 30 amino acids in length, also preferably less than 25 amino acids in length, and preferably less than 20 amino acids in length.
  • the identified binding peptides are between 4 and 20 and also between 6 and 15 amino acids in length.
  • peptides may be up to 100 amino acids in length.
  • Peptides that are longer than 100 amino acids in length are generally referred to as polypeptides. Standard abbreviations for amino acids are used herein. (See Singleton et al., (1987) Dictionary of Microbiology and Molecular Biology, Second Ed., page 35, incorporated herein by reference).
  • the term “protein” is well known and refers to a large polypeptide.
  • a “binding peptide” is a peptide that binds to a target (skin or hair) with a binding affinity of at least about 10 ⁇ 2 M, at least about 10 ⁇ 3 M, at least about 10 ⁇ 4 M, at least about 10 ⁇ 5 M, at least about 10 ⁇ 7 M, at least about 10 ⁇ 9 M, and preferably between about 10 ⁇ 2 M to 10 ⁇ 15 M, between about 10 ⁇ 2 M to 10 ⁇ 10 M and between 10 ⁇ 3 to 10 ⁇ 9 M.
  • nucleic acid means DNA, RNA, single-stranded or double-stranded and chemical modifications thereof. Modifications may include but are not limited to modified bases, backbone modifications, methylations, unusual base pairing modifications, and capping modifications.
  • Percent sequence identity with respect to a peptide or nucleic acid sequence refers to the percent of residues or codons that are identical in two sequences.
  • Peptide or polynucleotides according to the invention may have at least 50%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90% and at least 95% sequence identity to a reference sequence when optimally aligned.
  • Optimal alignment of the sequences may be conducted by various known methods and computerized implementation of known algorithms (e.g. BLAST, TFASTA, BESTFIT, such as in the Wisconsin Genetics Software Package, Release 7.0, Genetics Computer Group, Madison, Wis.).
  • target or “anti-target” refers to molecules or heterogeneous molecules that have a binding affinity as defined herein, for a given ligand. Both target and anti-targets may be naturally occurring or synthetic molecules or heterogeneous molecules.
  • the target is skin or hair. Further when the target is skin, the anti-target is hair and when the target is hair, the anti-target is skin.
  • the binding affinity of a ligand for its target or anti-target may be described by the dissociation constant (K D ), concentration needed for 50% effective binding (EC 50 ), or concentration needed for 50% inhibition of binding of another compound that binds to the target (IC 50 ).
  • K D is defined by k off /k on .
  • the k off value defines the rate at which the target-ligand complex breaks apart or separates. This term is sometimes referred to in the art as the kinetic stability of the target-ligand complex or the ratio of any other measurable quantity that reflects the ratio of binding affinities, such as an enzyme-linked immunosorbent assay (ELISA) signal or radio-active label signal.
  • ELISA enzyme-linked immunosorbent assay
  • “Selectivity” is defined by the ratio of binding affinities or k off for dissociation of the ligand-complex (target K D /anti-target K D ).
  • the k on value describes the rate at which the target and ligand combine to form the target-ligand complex.
  • contacting is broadly defined to mean placing a library of ligands and a target or anti-target in immediate proximity or association and includes in vitro and in vivo contact.
  • the term includes touching, associating, joining, combining, intravenous injection, oral administration, intraperitoneally, topical application, intramuscular, inhalation, subcutaneous application and the like.
  • separating means to select, segregate, partition, isolate, collect, keep apart and disunite. Separation methods are well known to those in the art. These methods include affinity chromatography, washing, liquid transfer, centrifugation, high-performance liquid chromatography (HPLC), filtration, such as gel filtration, enzyme-linked immunosorbent assays (ELISA), and fluorescence-activator cell sorting (FACS). The choice of a separation method is well within the skill of one in the art, and a variety of instruments used for these separation methods are commercially available. (See Kenny and Fowell (eds) (1992) Practical Protein Chromatography Methods in Molecular Biology , vol. 11, Humana Press, Totowa N.J.).
  • amplification means a process or combination of process steps that increases the amount or number of copies of a molecule or class of molecules. In one aspect, amplification refers to the production of additional copies of nucleic acid sequences that is carried out using polymerase chain reaction (PCR) technology well known in the art.
  • PCR polymerase chain reaction
  • a ligand may include a plurality of ligands.
  • the skin or hair binding peptides of the invention may be obtained and identified using methods well known in the art. These methods may include use of random peptide libraries, synthetic peptide libraries, peptide loop libraries, antibody libraries and protein libraries. These libraries as well as methods for making the libraries are well known. Reference is made to Barbas, C. F. (1993) Current Opinion in Biotech., 4:526; Cwirla et al., (1990) supra; Scott and Smith, (1990) Science, 249:386; Cull et al., (1992) supra; Pinilla et al., (1994) Biochem. J.
  • ligand libraries may be obtained commercially, for example from Sigma (St. Louis Mo.) or from various public sources such as American Type Culture Collection (ATCC) and the National Institute of Health (NIH).
  • ATCC American Type Culture Collection
  • NASH National Institute of Health
  • Screening techniques may include yeast display, ribosome display, biopanning and acid elution.
  • One general method for screening a library of ligands having a binding affinity and selectivity for a selected target includes preparing or obtaining a library of ligands, preferably peptides of different sequences and more preferably a random peptide library. Deselecting ligands that bind with an anti-target by contacting the ligand library with an anti-target under conditions favorable for binding between the ligands of the library and the anti-target; allowing the anti-target to bind with the ligands; and separating the anti-target non-binders (unbound ligands) from the anti-target ligand bound molecules and any free ligands.
  • Target-bound ligand complex is then separated from the remaining mixture including the unbound ligands.
  • the target-bound ligand complex or the target-bound ligands may optionally be subjected to further rounds of selection ( FIG. 1 ).
  • a binding peptide may be sequenced, amplified or produced in bulk by any one of a number of standard techniques. Some of these techniques include polymerase chain reaction (PCR), direct amino acid sequencing of the selected peptide by using peptide sequencers, mass spectrophotometry (MS), surface plasmon resonance, immunoprecipitation and nuclear magnetic resonance (NMR) spectroscopy.
  • PCR polymerase chain reaction
  • MS mass spectrophotometry
  • MS surface plasmon resonance
  • binding peptides may be produced recombinantly using genetic engineering or the peptide may be chemically synthesized.
  • the peptide binding affinity for the target according to the present invention for K D , EC 50 or IC 50 is in the range of between about 10 ⁇ 7 M to 10 ⁇ 15 M, although higher or low binding affinities may be achieved.
  • the binding affinity is in the range of at least about 10 ⁇ 2 M, at least about 10 ⁇ 3 M, at least about 10 ⁇ 4 M, at least about 10 ⁇ 5 M, at least about 10 ⁇ 7 M, at least about 10 ⁇ 9 M and also at least about 10 ⁇ 12 M.
  • the affinity is less than about 10 ⁇ 7 M.
  • k off values for the ligand-target complex will be less than about 10 ⁇ 2 sec ⁇ 1 , less than about 10 ⁇ 3 sec ⁇ 1 , less than about 10 ⁇ 4 sec ⁇ 1 , and also less than about 10 ⁇ 5 sec ⁇ 1 .
  • the binding peptides of the invention will not bind with any significance to the anti-target.
  • a preferred binding ligand may have a K D for the anti-target greater than about 10 ⁇ 4 M, and preferably greater than about 10 ⁇ 1 M.
  • the binding peptides according to the invention may be characterized not only by the binding affinity of the ligand to a target, but also may be characterized by the selectivity of the ligand-target complex.
  • the selectivity of ligand binding for a target compared to ligand binding to an anti-target can be defined by a ratio of K D , EC 50 or IC 50 in the range of about 1.5:1 to 500:1.
  • selectivity is at least about 2:1, at least about 3:1, at least about 5:1, at least about 10:1, at least about 20:1, at least about 30:1, at least about 50:1, and at least about 100:1.
  • Methods for measuring binding affinities and selectivity are well known in the art, and these methods include but are not limited to measurement by radio-labeled release and competition assay; by isothermal titration calorimetry; biosensor binding assays (Morton & Myszka, (1998) Methods Enzymol. 295:268-294); by fluorescence and chemiluminescence spectroscopy; and by mass spectrophotometry (Gao et al., (1996), J. Med, Chem., 39:1949).
  • preferred skin binding peptides are listed in Table 1.
  • Table 1 Skin binding peptides KQATFPPNPTAY SEQ ID NO. 1 QATFMYN SEQ ID NO. 2 HGHMVSTSQLSI SEQ ID NO. 3 VLTSQLPNHSM SEQ ID NO. 4 LSPSRMK SEQ ID NO. 5 LPIPRMK SEQ ID NO. 6 HSTAYLT SEQ ID NO. 7 HQRPYLT SEQ ID NO. 8 APQQRPMKTFNT SEQ ID NO. 9 APQQRPMKTVQY SEQ ID NO. 10 PPWLDLL SEQ ID NO. 11 PPWTFPL SEQ ID NO. 12 SVTHLTS SEQ ID NO.
  • Particularly preferred embodiments include skin binding peptides having an amino acid sequence of SEQ ID NO. 1, SEQ ID NO. 3, SEQ ID NO. 5, SEQ ID NO. 6, SEQ ID NO. 8 and SEQ ID NO. 15, and particularly SEQ ID NO. 1 and SEQ ID NO. 5.
  • skin binding peptides of the invention have repeatable motifs.
  • a repeatable motif is defined as including at least three consecutive amino acid residues in a peptide string and may include four, five, six, seven, eight or nine consecutive amino acids residues wherein the repeatable motif is found in at least two of the peptides listed in Table 1 or at least two of the peptides listed in Table 2.
  • Preferred repeatable motifs for skin binding peptides include QATF, TSQL, RMK, YLT, APQQRPM, PMKT, PPW, LTS, PPLL, APQQRMKT, PSGA, PLLAL, STAYL, and YPIST.
  • skin binding and hair binding peptides of the invention include sequence clusters.
  • a sequence cluster includes a repeatable motif as defined herein and 1 or 2 amino acid residues identical to amino acid residues found in the binding peptides listed in Table 1 or Table 2 when the same repeatable motif in each peptide is aligned and further including 1 to 8, preferably 1 to 3 intervening amino acid residues located either before or after the repeatable motif.
  • Preferred sequence clusters for skin binding peptides include the following: APQQRPMXTXXX SEQ ID NO. 25 PPWXXXL SEQ ID NO. 26 XXTXLTS SEQ ID NO. 27 XPPLLXL SEQ ID NO. 28 SXPSGAX SEQ ID NO. 29 XQATFXXNXXXX SEQ ID NO. 30 VXTSQLXXXXX SEQ ID NO. 31 LXXXRMK SEQ ID NO. 32 HXXXYLT SEQ ID NO. 33 X represents any L-amino acid.
  • Particularly preferred skin binding peptides are peptides having the sequence cluster of APQQRPMXTXXX (SEQ ID NO. 25), the sequence cluster of XQATFXXNXXXX (SEQ ID NO. 30) or LXXXRMK (SEQ ID NO. 32).
  • preferred hair binding peptides are listed in Table 2.
  • Table 2 Hair binding peptides NTPKENW SEQ ID NO. 34 NTPASNR SEQ ID NO. 35 PRGMLST SEQ ID NO. 36 PPTYLST SEQ ID NO. 37 TIPTHRQHDYRS SEQ ID NO. 38 TPPTHRL SEQ ID NO. 39 LPTMSTP SEQ ID NO. 40 LGTNSTP SEQ ID NO. 41 TPLTGSTNLLSS SEQ ID NO. 42 TPLTKET SEQ ID NO. 43 KQSHNPP SEQ ID NO. 44 QQSHNPP SEQ ID NO. 45 TQPHNPP SEQ ID NO. 46 STNLLRTSTVHP SEQ ID NO.
  • the binding peptides identified as SEQ ID NO: 53 and SEQ ID NO. 54 may include histidine (H), arginine (R) or asparagine (N) as the second amino acid in the peptide string.
  • hair binding peptides of Table 2 have repeatable motifs.
  • Preferred repeatable motifs for hair binding peptides include STNL, LSSHA, SPSSL, SHHTH, NTP, LST, PTHR, STP, TPLT and HNPP.
  • hair binding peptides of the invention include sequence clusters.
  • Preferred sequence clusters for hair binding peptides include the following: NTPXXNX SEQ ID NO. 57 PXXXLST SEQ ID NO. 58 TXPTHRX SEQ ID NO. 59 LXTXSTP SEQ ID NO. 60 TPLTXXT SEQ ID NO. 61 XQXHNPP SEQ ID NO. 62 X represents any L amino acid.
  • a binding peptide according to the invention includes peptides having a sequence cluster or repeatable motif as disclosed above, wherein the peptide has at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, and at least 85% amino acid sequence identity with a reference binding peptide of Table 1 or Table 2.
  • the peptide, which includes a sequence cluster or repeatable motif will also have a binding affinity for the same target as the reference peptide in the range of 10 ⁇ 2 to 10 ⁇ 15 M, at least about 10 ⁇ 2 M, at least about 10 ⁇ 3 M, at least about 10 ⁇ 5 M, at least about 10 ⁇ 7 M, and at least about 10 ⁇ 9 M.
  • the binding affinity will be essentially the same or greater than the binding affinity of the reference binding peptide.
  • a skin or hair binding peptide according to the invention may include a cysteine (C) residue on either or both ends of the peptide.
  • C-C derivatives include C-SEQ ID NO. 2-C; C-SEQ ID NO. 5-C; C-SEQ ID NO. 6-C; C-SEQ ID NO. 7-C; C-SEQ ID NO.8-C; C-SEQ ID NO. 11-C; C-SEQ ID NO. 12-C; C-SEQ ID NO. 13-C; C-SEQ ID NO. 14-C; C-SEQ ID NO. 15-C; C-SEQ ID NO.
  • C-C derivative hair binding peptides include C-SEQ ID NO. 34-C; C-SEQ ID NO. 35-C; C-SEQ ID NO. 36-C; C-SEQ ID NO. 37-C; C-SEQ ID NO. 39-C; C-SEQ ID NO. 40-C; C-SEQ ID NO. 41-C; C-SEQ ID NO. 43-C; C-SEQ ID NO. 46-C; C-SEQ ID NO. 49-C; C-SEQ ID NO. 51-C; C-SEQ ID NO. 52-C; and C-SEQ ID NO. 56-C.
  • a binding peptide which comprises a sequence cluster may also include a cysteine residue on either or both ends of the peptide.
  • a linker molecule (also sometimes referred to in the art as a spacer moiety) may be added to either end of a binding peptide according to the invention.
  • a linker molecule may be any carbon containing molecule such as, a short peptide, for example GGH, GGGK, and GGHGG; a carbon chain, for example (CH 2 )n wherein n equals 1 to 10; a polymer, for example PEG(CH 2 —O)n wherein n equals 2-20; a sugar; a lipid or the like.
  • skin or hair binding peptides of the invention may be used in is compositions for personal care applications. These compositions may take the form of lotions, creams, gels, sprays, shampoos and conditioners and the like.
  • Non-limiting examples of personal care applications which include a binding peptide of the invention are the following: a) using a skin binding peptide with an emollient which may result in the enhancement of the moisturizing properties of the emollient; b) combining a skin binding peptide with a bleaching or tanning agent which may result in the enhancement of skin bleaching or tanning properties; c) combining a skin binding peptides with a sunscreen for topical application; and d) combining a hair binding peptide with a dye or oxidizing agent wherein the hair coloring properties of the hair coloring formulation may be enhanced.
  • Restriction endonucleases Eagl and Acc651, 10 ⁇ NEBuffer 3, T4 DNA ligase, alkaline calf intestinal phosphatase, E. coli ER2537 host strain, and M13KE gill cloning vector were supplied by NEB and used according to the manufacturer's instructions unless stated otherwise.
  • Taq polymerase, 10 ⁇ PCR Buffer, and dNTP mix were supplied by Roche Molecular Biochemicals (Indianapolis, Ind.).
  • the HotStart Taq Master Mix kit for PCR came from Qiagen (Valencia, Calif.).
  • PCR was carried out using a HYBAID Omn-E Thermocycler from E&K Scientific Products (Campbell, Calif.) or PTC 2000 DNA EngineTM from M. J. Research Inc. (Roche Molecular Systems, Inc. Alameda, Calif.).
  • Nondenaturing polyacrylamide gels (8%) and D-15 DNA markers were obtained from Novex (San Diego, Calif.) and 2% E-gels and TOPO cloning kits were obtained from Invitrogen (Carlsbad, Calif.). Both the QIAquick Gel Extraction Kit and QIAquick PCR Purification Kit were obtained from QIAGEN (Valencia, Calif.).
  • AmpliWaxTM PCR Gems were obtained from Perkin Elmer (Boston, Mass.).
  • Pre-equilibrated skin tissues were placed into a 6 well culture plate containing fresh 0.9 mL tissue culture media and 300 ⁇ l of a 2% Neutrogena® Bath Gel containing, 10 ⁇ L of cyclic 7-mer or linear 12-mer peptide libraries (10 10 pfu/ ⁇ l), or wild type phage (10 9 pfu/ ⁇ l) were added to the skin surface.
  • the samples were incubated at room temperature for 15 min with gentle agitation. The unbound supernatant was transferred to a new well containing skin tissue and the procedure was repeated.
  • the incubation solution was transferred to nine 3 inch dark hair (International Hair Importers & Products, White Plains, N.Y.) strands in 50 ml tubes containing 10 ml of 2% body gel for 30 minutes at room temperature with rotatory shaking (30 rpm).
  • the hair samples were then washed with 1 ⁇ 50 mls, 2 ⁇ 50 mls, or 4 ⁇ 50 mls of 2% bath gel; Wash cycles in PBS followed (1 ⁇ 25 mls for 5 min, 1 ⁇ 25 mls for 2 min, 2 ⁇ 50 mls for 5 min each, 150 mls total). After the final PBS wash, the hair samples containing bound phage peptides were frozen at ⁇ 20° C. Table 2 illustrates target bound hair peptides screened according to this example.
  • PCR was performed directly on the hair and skin samples using the following conditions in 0.5 ml PCR tubes with the following reagents:
  • PCR products were visualized on a 2% E-gel along with PCR products from dilutions of the various initial phage peptide libraries (positive control) and molecular weight markers, run under 65V for 40 min. 4 ⁇ l of the PCR products were subject to TOPO cloning and transformation according to standard protocol but all incubations were done for 30 minutes. The individual clones were submitted to PCR (12.5 ⁇ l Master Mix, 0.1 ⁇ l each of CM13 01 and CM13 02 primers, 12.3 ⁇ l sterile water per clone) using the same program as described above.
  • Sequencing using 1 ⁇ l of PCR product and 11 ⁇ l of g96 primer was completed at Sequetech (Mountain View, Calif.); Biotech Core, Inc (Mountain View, Calif.) or internally using an ABI Applied Biosystem 373XL.
  • M13KE vector New England Biolabs (NEB), Beverly, Mass.
  • NEB Newcastle Equivalent Research
  • 10 ⁇ g of M13KE vector was digested overnight (16 h) at 37° C. and according to NEB recommended conditions, digestion was performed in 400 ⁇ l total volume as follows: M13KE, 10 ⁇ l; Eag 1, 10 ⁇ l; Acc65 I, 10 ⁇ l; 10 ⁇ NEB buffer 3, 40 ⁇ l; 100 ⁇ BSA 4 ⁇ l; and dH 2 O, 326 ⁇ l.
  • the digested vector was purified using Qiagen PCR Purification Kit (Qiagen) using 30 ⁇ l of elution buffer (EB). The purified digest was stored at ⁇ 20° C.
  • PCR product from the first round of selection was purified using the Qiagen Purification Kit and eluted in 30 ⁇ l of EB buffer. 15 ⁇ l of the purified material was digested overnight in 100 ⁇ l total volume as follows: PCR product, 15 ⁇ l; Eag1, 1 ⁇ l; Acc651, 1 ⁇ l; 10 ⁇ NEB buffer 3, 10 ⁇ l; 100 ⁇ BSA, 1 ⁇ l; and dH 2 O, 64 ⁇ l. The digestion was followed by a heat shock treatment at 60° C. for 20 min and the product was stored at ⁇ 20° C. until further use.
  • the ligation was performed as described below using the Takara kit at 16° C. for 30 min, then placed on ice.
  • Vector preparation 1 ⁇ l
  • Insert preparation 1 ⁇ l
  • EB buffer 3 ⁇ l
  • Solution 5 ⁇ l from Takara Biolnc., (Shiga, Japan).
  • the phage peptide libraries were amplified and titered according to standard techniques. Subsequent rounds of deselection and selection may also be performed according to the methods described above.
  • FIGS. 2 and 3 illustrate the stability of the phage populations in shampoo ( FIG. 2 ) and shower gel ( FIG. 3 ).
  • the phage display libraries were more stable in the bath gel solution than in the shampoo solution.
  • the pfu/mL of the phage libraries decreased by less than one log unit in the bath gel solution, but they decreased by up to two log units in the shampoo.

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US20080227716A1 (en) * 2003-11-28 2008-09-18 Helga Rothe Use of Peptides for Protecting Skin from Hair-Treatment Agents
US20080280810A1 (en) * 2006-10-30 2008-11-13 O'brien John P Peptides having affinity for body surfaces
US20100158847A1 (en) * 2008-12-18 2010-06-24 E. I. Du Pont De Nemours And Company Hair-binding peptides
US20100158846A1 (en) * 2008-12-18 2010-06-24 E. I. Du Pont De Nemours And Company Hair-binding peptides
US20100158822A1 (en) * 2008-12-18 2010-06-24 E .I. Du Pont De Nemours And Company Peptides that bind to silica-coated particles
US20100158823A1 (en) * 2008-12-18 2010-06-24 E. I. Du Pont De Nemours And Company Peptide linkers for effective multivalent peptide binding
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US20080227716A1 (en) * 2003-11-28 2008-09-18 Helga Rothe Use of Peptides for Protecting Skin from Hair-Treatment Agents
US20080280810A1 (en) * 2006-10-30 2008-11-13 O'brien John P Peptides having affinity for body surfaces
US20080175798A1 (en) * 2006-12-11 2008-07-24 Beck William A Peptide-based hair protectants
US8697654B2 (en) 2008-12-18 2014-04-15 E I Du Pont De Nemours And Company Peptide linkers for effective multivalent peptide binding
US20100158847A1 (en) * 2008-12-18 2010-06-24 E. I. Du Pont De Nemours And Company Hair-binding peptides
US20100158846A1 (en) * 2008-12-18 2010-06-24 E. I. Du Pont De Nemours And Company Hair-binding peptides
US20100158822A1 (en) * 2008-12-18 2010-06-24 E .I. Du Pont De Nemours And Company Peptides that bind to silica-coated particles
US20100158823A1 (en) * 2008-12-18 2010-06-24 E. I. Du Pont De Nemours And Company Peptide linkers for effective multivalent peptide binding
US9278138B2 (en) 2008-12-18 2016-03-08 E. I. Du Pont De Nemours And Company Peptide linkers for effective multivalent peptide binding
US8287845B2 (en) 2008-12-18 2012-10-16 E I Du Pont De Nemours And Company Hair-binding peptides
US20100227361A1 (en) * 2009-03-05 2010-09-09 E. I. Du Pont De Nemours And Company Host cell modifications that improve peptide production and downstream processing
US7915011B2 (en) 2009-03-05 2011-03-29 E.I. Du Pont De Nemours And Company Host cell modifications that improve peptide production and downstream processing
US20100298240A1 (en) * 2009-05-20 2010-11-25 E. I. Du Pont De Nemours And Company Pmma binding peptides
US20100298531A1 (en) * 2009-05-20 2010-11-25 E.I. Du Pont De Nemours And Company Pmma binding peptides
US20100298533A1 (en) * 2009-05-20 2010-11-25 E.I. Du Pont De Nemours And Company Pmma binding peptides
US20100298231A1 (en) * 2009-05-20 2010-11-25 E. I. Du Pont De Nemours And Company Pmma binding peptides
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US8389675B2 (en) 2009-05-20 2013-03-05 E I Du Pont De Nemours And Company PMMA binding peptides
US8404214B2 (en) 2009-05-20 2013-03-26 E I Du Pont De Nemours And Company PMMA binding peptides
US8455614B2 (en) 2009-05-20 2013-06-04 E.I. Du Pont De Nemours And Company PMMA binding peptides
US20100298241A1 (en) * 2009-05-20 2010-11-25 E.I. Du Pont De Nemours And Company Pmma binding peptides
US20100310495A1 (en) * 2009-06-08 2010-12-09 E. I. Du Pont De Nemours And Company Peptides having affinity for poly (benzyl methacrylate-co-methacrylic acid) potassium salt copolymers and methods of use
US20120052034A1 (en) * 2010-09-01 2012-03-01 Zotos International, Inc. Hair treatment composition with naturally - derived peptide identical to human hair
US9505820B2 (en) * 2010-09-01 2016-11-29 Zotos International, Inc. Hair treatment composition with naturally - derived peptide identical to human hair
US8609621B2 (en) 2010-11-15 2013-12-17 E I Du Pont De Nemours And Company Acid-cleavable linkers exhibiting altered rates of acid hydrolysis
US8663616B2 (en) 2010-12-20 2014-03-04 E I Du Pont De Nemours And Company Enzymatic peracid generation for use in oral care products
US8652455B2 (en) 2010-12-20 2014-02-18 E I Du Pont De Nemours And Company Targeted perhydrolases
US8815550B2 (en) 2010-12-20 2014-08-26 E I Du Pont De Nemours And Company Targeted perhydrolases
US9273336B2 (en) 2011-02-21 2016-03-01 E. I. Du Pont De Nemours And Company Recombinant host cells having an increase in buoyant density

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US20100168383A1 (en) 2010-07-01
CN1774232A (zh) 2006-05-17
US8546528B2 (en) 2013-10-01
WO2004048399A2 (fr) 2004-06-10
US8816048B2 (en) 2014-08-26
EP1572723B1 (fr) 2013-02-27
AU2003294266A1 (en) 2004-06-18
EP1572723A2 (fr) 2005-09-14
CN102584951A (zh) 2012-07-18
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JP2006514932A (ja) 2006-05-18
US20140080996A1 (en) 2014-03-20
US20140364584A1 (en) 2014-12-11
EP2581383A1 (fr) 2013-04-17
WO2004048399A3 (fr) 2005-12-22
CN1774232B (zh) 2012-05-09

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