KR20150072144A - Development of long acting and cell permeable beta-defensin 3 and -3H by conjugating lauric acid and cell permeable peptide respectively and Cosmetic compostion comprising the Same - Google Patents
Development of long acting and cell permeable beta-defensin 3 and -3H by conjugating lauric acid and cell permeable peptide respectively and Cosmetic compostion comprising the Same Download PDFInfo
- Publication number
- KR20150072144A KR20150072144A KR1020130159482A KR20130159482A KR20150072144A KR 20150072144 A KR20150072144 A KR 20150072144A KR 1020130159482 A KR1020130159482 A KR 1020130159482A KR 20130159482 A KR20130159482 A KR 20130159482A KR 20150072144 A KR20150072144 A KR 20150072144A
- Authority
- KR
- South Korea
- Prior art keywords
- beta
- defensin
- lauroyl
- peptide
- present
- Prior art date
Links
- 239000002537 cosmetic Substances 0.000 title claims abstract description 51
- 102100026887 Beta-defensin 103 Human genes 0.000 title claims abstract description 47
- 101710125296 Beta-defensin 3 Proteins 0.000 title claims abstract description 44
- 108090000765 processed proteins & peptides Proteins 0.000 title claims description 67
- 238000011161 development Methods 0.000 title abstract description 7
- POULHZVOKOAJMA-UHFFFAOYSA-N dodecanoic acid Chemical compound CCCCCCCCCCCC(O)=O POULHZVOKOAJMA-UHFFFAOYSA-N 0.000 title description 43
- 239000005639 Lauric acid Substances 0.000 title description 21
- 230000001268 conjugating effect Effects 0.000 title description 3
- 239000000203 mixture Substances 0.000 claims abstract description 59
- 208000002874 Acne Vulgaris Diseases 0.000 claims abstract description 24
- 206010000496 acne Diseases 0.000 claims abstract description 24
- 125000000400 lauroyl group Chemical group O=C([*])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 claims description 61
- 206010012438 Dermatitis atopic Diseases 0.000 claims description 23
- 201000008937 atopic dermatitis Diseases 0.000 claims description 23
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 13
- 230000003115 biocidal effect Effects 0.000 claims description 3
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 2
- 230000006872 improvement Effects 0.000 abstract description 15
- 230000000845 anti-microbial effect Effects 0.000 abstract description 13
- 239000002253 acid Substances 0.000 abstract description 6
- 230000004927 fusion Effects 0.000 abstract description 6
- 206010003645 Atopy Diseases 0.000 abstract description 4
- 239000003814 drug Substances 0.000 abstract description 2
- 229940079593 drug Drugs 0.000 abstract description 2
- 201000004624 Dermatitis Diseases 0.000 abstract 1
- 210000004027 cell Anatomy 0.000 description 41
- 102000012265 beta-defensin Human genes 0.000 description 31
- 108050002883 beta-defensin Proteins 0.000 description 31
- 210000003491 skin Anatomy 0.000 description 28
- 230000000694 effects Effects 0.000 description 27
- 102000044503 Antimicrobial Peptides Human genes 0.000 description 25
- 108700042778 Antimicrobial Peptides Proteins 0.000 description 25
- 238000006243 chemical reaction Methods 0.000 description 17
- 230000000844 anti-bacterial effect Effects 0.000 description 16
- 108090000623 proteins and genes Proteins 0.000 description 14
- 210000002510 keratinocyte Anatomy 0.000 description 13
- 102000004196 processed proteins & peptides Human genes 0.000 description 13
- 238000004519 manufacturing process Methods 0.000 description 12
- 102000004169 proteins and genes Human genes 0.000 description 12
- 238000002474 experimental method Methods 0.000 description 10
- 210000002950 fibroblast Anatomy 0.000 description 10
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 9
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 9
- PSHKMPUSSFXUIA-UHFFFAOYSA-N n,n-dimethylpyridin-2-amine Chemical compound CN(C)C1=CC=CC=N1 PSHKMPUSSFXUIA-UHFFFAOYSA-N 0.000 description 9
- 231100000135 cytotoxicity Toxicity 0.000 description 8
- 230000003013 cytotoxicity Effects 0.000 description 8
- 235000018102 proteins Nutrition 0.000 description 8
- 210000004927 skin cell Anatomy 0.000 description 8
- 241000588724 Escherichia coli Species 0.000 description 7
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 7
- 238000000034 method Methods 0.000 description 7
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 6
- ZMANZCXQSJIPKH-UHFFFAOYSA-N Triethylamine Chemical compound CCN(CC)CC ZMANZCXQSJIPKH-UHFFFAOYSA-N 0.000 description 6
- 238000009472 formulation Methods 0.000 description 6
- 239000000463 material Substances 0.000 description 6
- 239000002609 medium Substances 0.000 description 6
- 244000005700 microbiome Species 0.000 description 6
- 239000003921 oil Substances 0.000 description 6
- 239000003910 polypeptide antibiotic agent Substances 0.000 description 6
- 108091008146 restriction endonucleases Proteins 0.000 description 6
- 241000894006 Bacteria Species 0.000 description 5
- 101001033280 Homo sapiens Cytokine receptor common subunit beta Proteins 0.000 description 5
- 235000001014 amino acid Nutrition 0.000 description 5
- 150000001413 amino acids Chemical class 0.000 description 5
- 239000003242 anti bacterial agent Substances 0.000 description 5
- 229940088710 antibiotic agent Drugs 0.000 description 5
- 210000000170 cell membrane Anatomy 0.000 description 5
- 230000021615 conjugation Effects 0.000 description 5
- 230000002500 effect on skin Effects 0.000 description 5
- 238000004128 high performance liquid chromatography Methods 0.000 description 5
- 102000055647 human CSF2RB Human genes 0.000 description 5
- 229930027917 kanamycin Natural products 0.000 description 5
- 229960000318 kanamycin Drugs 0.000 description 5
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 5
- 229930182823 kanamycin A Natural products 0.000 description 5
- 239000000126 substance Substances 0.000 description 5
- 230000001988 toxicity Effects 0.000 description 5
- 231100000419 toxicity Toxicity 0.000 description 5
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 4
- 241000555676 Malassezia Species 0.000 description 4
- 238000010367 cloning Methods 0.000 description 4
- 239000013604 expression vector Substances 0.000 description 4
- 230000001976 improved effect Effects 0.000 description 4
- 239000006210 lotion Substances 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- 238000003786 synthesis reaction Methods 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- 239000013598 vector Substances 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- 208000020154 Acnes Diseases 0.000 description 3
- 201000004384 Alopecia Diseases 0.000 description 3
- 241000222122 Candida albicans Species 0.000 description 3
- 208000001840 Dandruff Diseases 0.000 description 3
- 206010021531 Impetigo Diseases 0.000 description 3
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 3
- 241000194017 Streptococcus Species 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 3
- 230000000692 anti-sense effect Effects 0.000 description 3
- 230000002421 anti-septic effect Effects 0.000 description 3
- 239000004599 antimicrobial Substances 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 229940095731 candida albicans Drugs 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- 238000003776 cleavage reaction Methods 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 239000006071 cream Substances 0.000 description 3
- 235000018417 cysteine Nutrition 0.000 description 3
- 230000003247 decreasing effect Effects 0.000 description 3
- 201000010099 disease Diseases 0.000 description 3
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 3
- 239000003995 emulsifying agent Substances 0.000 description 3
- 238000011156 evaluation Methods 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- 235000011187 glycerol Nutrition 0.000 description 3
- 208000024963 hair loss Diseases 0.000 description 3
- 230000003676 hair loss Effects 0.000 description 3
- 208000015181 infectious disease Diseases 0.000 description 3
- 239000004615 ingredient Substances 0.000 description 3
- 230000002401 inhibitory effect Effects 0.000 description 3
- 231100001083 no cytotoxicity Toxicity 0.000 description 3
- 230000035699 permeability Effects 0.000 description 3
- 230000002265 prevention Effects 0.000 description 3
- 239000002994 raw material Substances 0.000 description 3
- 230000007017 scission Effects 0.000 description 3
- 208000017520 skin disease Diseases 0.000 description 3
- 231100000245 skin permeability Toxicity 0.000 description 3
- 241000894007 species Species 0.000 description 3
- 239000003381 stabilizer Substances 0.000 description 3
- 208000024891 symptom Diseases 0.000 description 3
- 210000001519 tissue Anatomy 0.000 description 3
- PUPZLCDOIYMWBV-UHFFFAOYSA-N (+/-)-1,3-Butanediol Chemical compound CC(O)CCO PUPZLCDOIYMWBV-UHFFFAOYSA-N 0.000 description 2
- DQNLFLGFZAUIOW-FXQIFTODSA-N Arg-Cys-Ala Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](C)C(O)=O DQNLFLGFZAUIOW-FXQIFTODSA-N 0.000 description 2
- HQIZDMIGUJOSNI-IUCAKERBSA-N Arg-Gly-Arg Chemical compound N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(O)=O HQIZDMIGUJOSNI-IUCAKERBSA-N 0.000 description 2
- JBDLMLZNDRLDIX-HJGDQZAQSA-N Asn-Thr-Leu Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(C)C)C(O)=O JBDLMLZNDRLDIX-HJGDQZAQSA-N 0.000 description 2
- 244000063299 Bacillus subtilis Species 0.000 description 2
- 235000014469 Bacillus subtilis Nutrition 0.000 description 2
- 108020004705 Codon Proteins 0.000 description 2
- HBHMVBGGHDMPBF-GARJFASQSA-N Cys-Leu-Pro Chemical compound CC(C)C[C@@H](C(=O)N1CCC[C@@H]1C(=O)O)NC(=O)[C@H](CS)N HBHMVBGGHDMPBF-GARJFASQSA-N 0.000 description 2
- DQGIAOGALAQBGK-BWBBJGPYSA-N Cys-Ser-Thr Chemical compound C[C@H]([C@@H](C(=O)O)NC(=O)[C@H](CO)NC(=O)[C@H](CS)N)O DQGIAOGALAQBGK-BWBBJGPYSA-N 0.000 description 2
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 2
- 206010016936 Folliculitis Diseases 0.000 description 2
- 241000233866 Fungi Species 0.000 description 2
- DQLVHRFFBQOWFL-JYJNAYRXSA-N Gln-Lys-Tyr Chemical compound C1=CC(=CC=C1C[C@@H](C(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(=O)N)N)O DQLVHRFFBQOWFL-JYJNAYRXSA-N 0.000 description 2
- AAHSHTLISQUZJL-QSFUFRPTSA-N Gly-Ile-Ile Chemical compound [H]NCC(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)CC)C(O)=O AAHSHTLISQUZJL-QSFUFRPTSA-N 0.000 description 2
- 101000912247 Homo sapiens Beta-defensin 103 Proteins 0.000 description 2
- 206010061218 Inflammation Diseases 0.000 description 2
- CFVQPNSCQMKDPB-CIUDSAMLSA-N Lys-Cys-Cys Chemical compound C(CCN)C[C@@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CS)C(=O)O)N CFVQPNSCQMKDPB-CIUDSAMLSA-N 0.000 description 2
- 108060003100 Magainin Proteins 0.000 description 2
- 241000699666 Mus <mouse, genus> Species 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 241000589517 Pseudomonas aeruginosa Species 0.000 description 2
- 241000293869 Salmonella enterica subsp. enterica serovar Typhimurium Species 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 241000191967 Staphylococcus aureus Species 0.000 description 2
- BTWMICVCQLKKNR-DCAQKATOSA-N Val-Leu-Ser Chemical compound CC(C)[C@H]([NH3+])C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C([O-])=O BTWMICVCQLKKNR-DCAQKATOSA-N 0.000 description 2
- 239000013543 active substance Substances 0.000 description 2
- 239000002671 adjuvant Substances 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- 239000003963 antioxidant agent Substances 0.000 description 2
- 108010062796 arginyllysine Proteins 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 239000013592 cell lysate Substances 0.000 description 2
- 239000011248 coating agent Substances 0.000 description 2
- 238000000576 coating method Methods 0.000 description 2
- 239000003086 colorant Substances 0.000 description 2
- 230000000052 comparative effect Effects 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- 210000004207 dermis Anatomy 0.000 description 2
- 235000014113 dietary fatty acids Nutrition 0.000 description 2
- 238000009826 distribution Methods 0.000 description 2
- 239000000975 dye Substances 0.000 description 2
- 210000000959 ear middle Anatomy 0.000 description 2
- 239000000839 emulsion Substances 0.000 description 2
- 239000002158 endotoxin Substances 0.000 description 2
- 239000000686 essence Substances 0.000 description 2
- 239000000194 fatty acid Substances 0.000 description 2
- 229930195729 fatty acid Natural products 0.000 description 2
- 150000004665 fatty acids Chemical class 0.000 description 2
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 2
- XKUKSGPZAADMRA-UHFFFAOYSA-N glycyl-glycyl-glycine Chemical compound NCC(=O)NCC(=O)NCC(O)=O XKUKSGPZAADMRA-UHFFFAOYSA-N 0.000 description 2
- 102000055779 human DEFB103A Human genes 0.000 description 2
- 239000003906 humectant Substances 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 230000004054 inflammatory process Effects 0.000 description 2
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 2
- 210000003734 kidney Anatomy 0.000 description 2
- 229920006008 lipopolysaccharide Polymers 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 230000005923 long-lasting effect Effects 0.000 description 2
- 239000007937 lozenge Substances 0.000 description 2
- 230000014759 maintenance of location Effects 0.000 description 2
- 239000003607 modifier Substances 0.000 description 2
- 239000003960 organic solvent Substances 0.000 description 2
- 239000002304 perfume Substances 0.000 description 2
- 239000012071 phase Substances 0.000 description 2
- 239000013612 plasmid Substances 0.000 description 2
- -1 polyoxyethylene Polymers 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 239000008213 purified water Substances 0.000 description 2
- 210000004761 scalp Anatomy 0.000 description 2
- 230000035945 sensitivity Effects 0.000 description 2
- 229920002545 silicone oil Polymers 0.000 description 2
- 210000001626 skin fibroblast Anatomy 0.000 description 2
- 210000002784 stomach Anatomy 0.000 description 2
- 208000003265 stomatitis Diseases 0.000 description 2
- 239000004094 surface-active agent Substances 0.000 description 2
- 230000004083 survival effect Effects 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 231100000331 toxic Toxicity 0.000 description 2
- 230000002588 toxic effect Effects 0.000 description 2
- 108010003137 tyrosyltyrosine Proteins 0.000 description 2
- 239000006097 ultraviolet radiation absorber Substances 0.000 description 2
- 239000000080 wetting agent Substances 0.000 description 2
- NBDTZVVEDLDLSG-UHFFFAOYSA-N 4,6,6-trimethylheptan-2-yl acetate Chemical compound CC(C)(C)CC(C)CC(C)OC(C)=O NBDTZVVEDLDLSG-UHFFFAOYSA-N 0.000 description 1
- BTBUEVAGZCKULD-XPUUQOCRSA-N Ala-Gly-His Chemical compound C[C@H](N)C(=O)NCC(=O)N[C@H](C(O)=O)CC1=CN=CN1 BTBUEVAGZCKULD-XPUUQOCRSA-N 0.000 description 1
- 102400000237 Alpha-neoendorphin Human genes 0.000 description 1
- 101800001617 Alpha-neoendorphin Proteins 0.000 description 1
- HJVGMOYJDDXLMI-AVGNSLFASA-N Arg-Arg-Lys Chemical compound NCCCC[C@@H](C(O)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@@H](N)CCCNC(N)=N HJVGMOYJDDXLMI-AVGNSLFASA-N 0.000 description 1
- BTJVOUQWFXABOI-IHRRRGAJSA-N Arg-Lys-Lys Chemical compound NCCCC[C@@H](C(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CCCNC(N)=N BTJVOUQWFXABOI-IHRRRGAJSA-N 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 241000222120 Candida <Saccharomycetales> Species 0.000 description 1
- 108050004290 Cecropin Proteins 0.000 description 1
- 229920000742 Cotton Polymers 0.000 description 1
- XGIAHEUULGOZHH-GUBZILKMSA-N Cys-Arg-Val Chemical compound CC(C)[C@@H](C(=O)O)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CS)N XGIAHEUULGOZHH-GUBZILKMSA-N 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 101710178508 Defensin 3 Proteins 0.000 description 1
- 102000000541 Defensins Human genes 0.000 description 1
- 108010002069 Defensins Proteins 0.000 description 1
- 241000723298 Dicentrarchus labrax Species 0.000 description 1
- 108010067770 Endopeptidase K Proteins 0.000 description 1
- 238000012413 Fluorescence activated cell sorting analysis Methods 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- YRWWJCDWLVXTHN-LAEOZQHASA-N Gln-Ile-Gly Chemical compound CC[C@H](C)[C@@H](C(=O)NCC(=O)O)NC(=O)[C@H](CCC(=O)N)N YRWWJCDWLVXTHN-LAEOZQHASA-N 0.000 description 1
- HNVFSTLPVJWIDV-CIUDSAMLSA-N Glu-Glu-Gln Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(N)=O)C(O)=O HNVFSTLPVJWIDV-CIUDSAMLSA-N 0.000 description 1
- ADZGCWWDPFDHCY-ZETCQYMHSA-N Gly-His-Gly Chemical compound OC(=O)CNC(=O)[C@@H](NC(=O)CN)CC1=CN=CN1 ADZGCWWDPFDHCY-ZETCQYMHSA-N 0.000 description 1
- DAKSMIWQZPHRIB-BZSNNMDCSA-N His-Tyr-Leu Chemical compound [H]N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC(C)C)C(O)=O DAKSMIWQZPHRIB-BZSNNMDCSA-N 0.000 description 1
- PDTMWFVVNZYWTR-NHCYSSNCSA-N Ile-Gly-Lys Chemical compound CC[C@H](C)[C@H](N)C(=O)NCC(=O)N[C@@H](CCCCN)C(O)=O PDTMWFVVNZYWTR-NHCYSSNCSA-N 0.000 description 1
- 206010061217 Infestation Diseases 0.000 description 1
- 102000004310 Ion Channels Human genes 0.000 description 1
- HBJZFCIVFIBNSV-DCAQKATOSA-N Leu-Arg-Asn Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CC(N)=O)C(O)=O HBJZFCIVFIBNSV-DCAQKATOSA-N 0.000 description 1
- UBZGNBKMIJHOHL-BZSNNMDCSA-N Leu-Leu-Phe Chemical compound CC(C)C[C@H]([NH3+])C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C([O-])=O)CC1=CC=CC=C1 UBZGNBKMIJHOHL-BZSNNMDCSA-N 0.000 description 1
- ZDBMWELMUCLUPL-QEJZJMRPSA-N Leu-Phe-Ala Chemical compound CC(C)C[C@H](N)C(=O)N[C@H](C(=O)N[C@@H](C)C(O)=O)CC1=CC=CC=C1 ZDBMWELMUCLUPL-QEJZJMRPSA-N 0.000 description 1
- DRWMRVFCKKXHCH-BZSNNMDCSA-N Leu-Phe-Leu Chemical compound CC(C)C[C@H]([NH3+])C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C([O-])=O)CC1=CC=CC=C1 DRWMRVFCKKXHCH-BZSNNMDCSA-N 0.000 description 1
- FBNPMTNBFFAMMH-AVGNSLFASA-N Leu-Val-Arg Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](C(C)C)C(=O)N[C@H](C(O)=O)CCCN=C(N)N FBNPMTNBFFAMMH-AVGNSLFASA-N 0.000 description 1
- FBNPMTNBFFAMMH-UHFFFAOYSA-N Leu-Val-Arg Natural products CC(C)CC(N)C(=O)NC(C(C)C)C(=O)NC(C(O)=O)CCCN=C(N)N FBNPMTNBFFAMMH-UHFFFAOYSA-N 0.000 description 1
- 239000006142 Luria-Bertani Agar Substances 0.000 description 1
- PBIPLDMFHAICIP-DCAQKATOSA-N Lys-Glu-Glu Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O PBIPLDMFHAICIP-DCAQKATOSA-N 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- ZEDVFJPQNNBMST-CYDGBPFRSA-N Met-Arg-Ile Chemical compound [H]N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)CC)C(O)=O ZEDVFJPQNNBMST-CYDGBPFRSA-N 0.000 description 1
- SOAYQFDWEIWPPR-IHRRRGAJSA-N Met-Ser-Tyr Chemical compound [H]N[C@@H](CCSC)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O SOAYQFDWEIWPPR-IHRRRGAJSA-N 0.000 description 1
- 239000004909 Moisturizer Substances 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- XZFYRXDAULDNFX-UHFFFAOYSA-N N-L-cysteinyl-L-phenylalanine Natural products SCC(N)C(=O)NC(C(O)=O)CC1=CC=CC=C1 XZFYRXDAULDNFX-UHFFFAOYSA-N 0.000 description 1
- 206010030113 Oedema Diseases 0.000 description 1
- 238000012408 PCR amplification Methods 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- LRBSWBVUCLLRLU-BZSNNMDCSA-N Phe-Leu-Lys Chemical compound CC(C)C[C@H](NC(=O)[C@@H](N)Cc1ccccc1)C(=O)N[C@@H](CCCCN)C(O)=O LRBSWBVUCLLRLU-BZSNNMDCSA-N 0.000 description 1
- BQMFWUKNOCJDNV-HJWJTTGWSA-N Phe-Val-Ile Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(O)=O BQMFWUKNOCJDNV-HJWJTTGWSA-N 0.000 description 1
- 229920003171 Poly (ethylene oxide) Polymers 0.000 description 1
- LGMBKOAPPTYKLC-JYJNAYRXSA-N Pro-Phe-Arg Chemical compound C([C@@H](C(=O)N[C@@H](CCCNC(=N)N)C(O)=O)NC(=O)[C@H]1NCCC1)C1=CC=CC=C1 LGMBKOAPPTYKLC-JYJNAYRXSA-N 0.000 description 1
- ZMLRZBWCXPQADC-TUAOUCFPSA-N Pro-Val-Pro Chemical compound CC(C)[C@@H](C(=O)N1CCC[C@@H]1C(=O)O)NC(=O)[C@@H]2CCCN2 ZMLRZBWCXPQADC-TUAOUCFPSA-N 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 208000003251 Pruritus Diseases 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 241000607142 Salmonella Species 0.000 description 1
- SNXUIBACCONSOH-BWBBJGPYSA-N Ser-Thr-Ser Chemical compound OC[C@H](N)C(=O)N[C@@H]([C@H](O)C)C(=O)N[C@@H](CO)C(O)=O SNXUIBACCONSOH-BWBBJGPYSA-N 0.000 description 1
- 239000004902 Softening Agent Substances 0.000 description 1
- 241000191940 Staphylococcus Species 0.000 description 1
- 108010070741 Tachypleus tridentatus tachyplesin peptide Proteins 0.000 description 1
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 description 1
- KLGFILUOTCBNLJ-IHRRRGAJSA-N Tyr-Cys-Arg Chemical compound C1=CC(=CC=C1C[C@@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCN=C(N)N)C(=O)O)N)O KLGFILUOTCBNLJ-IHRRRGAJSA-N 0.000 description 1
- ICFRWCLVYFKHJV-FXQIFTODSA-N Val-Cys-Cys Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CS)C(=O)O)N ICFRWCLVYFKHJV-FXQIFTODSA-N 0.000 description 1
- AEFJNECXZCODJM-UWVGGRQHSA-N Val-Val-Gly Chemical compound CC(C)[C@H]([NH3+])C(=O)N[C@@H](C(C)C)C(=O)NCC([O-])=O AEFJNECXZCODJM-UWVGGRQHSA-N 0.000 description 1
- AOILQMZPNLUXCM-AVGNSLFASA-N Val-Val-Lys Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](C(C)C)C(=O)N[C@H](C(O)=O)CCCCN AOILQMZPNLUXCM-AVGNSLFASA-N 0.000 description 1
- 230000001133 acceleration Effects 0.000 description 1
- 230000010933 acylation Effects 0.000 description 1
- 238000005917 acylation reaction Methods 0.000 description 1
- 239000000443 aerosol Substances 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 238000000246 agarose gel electrophoresis Methods 0.000 description 1
- OFHCOWSQAMBJIW-AVJTYSNKSA-N alfacalcidol Chemical compound C1(/[C@@H]2CC[C@@H]([C@]2(CCC1)C)[C@H](C)CCCC(C)C)=C\C=C1\C[C@@H](O)C[C@H](O)C1=C OFHCOWSQAMBJIW-AVJTYSNKSA-N 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 230000003255 anti-acne Effects 0.000 description 1
- 230000000843 anti-fungal effect Effects 0.000 description 1
- 239000002543 antimycotic Substances 0.000 description 1
- 239000002246 antineoplastic agent Substances 0.000 description 1
- 229940041181 antineoplastic drug Drugs 0.000 description 1
- 230000003078 antioxidant effect Effects 0.000 description 1
- 239000003443 antiviral agent Substances 0.000 description 1
- 239000008346 aqueous phase Substances 0.000 description 1
- 108010036533 arginylvaline Proteins 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 239000012754 barrier agent Substances 0.000 description 1
- 108010066270 beta-lactorphin Proteins 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 238000005251 capillar electrophoresis Methods 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 239000004359 castor oil Substances 0.000 description 1
- 235000019438 castor oil Nutrition 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 239000002738 chelating agent Substances 0.000 description 1
- 239000007809 chemical reaction catalyst Substances 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 238000011278 co-treatment Methods 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 125000000151 cysteine group Chemical class N[C@@H](CS)C(=O)* 0.000 description 1
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 230000001472 cytotoxic effect Effects 0.000 description 1
- 231100000263 cytotoxicity test Toxicity 0.000 description 1
- 230000007123 defense Effects 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- 239000002270 dispersing agent Substances 0.000 description 1
- 125000003438 dodecyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])* 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 210000002919 epithelial cell Anatomy 0.000 description 1
- 210000004996 female reproductive system Anatomy 0.000 description 1
- 239000000945 filler Substances 0.000 description 1
- 239000006260 foam Substances 0.000 description 1
- 239000004088 foaming agent Substances 0.000 description 1
- 230000003325 follicular Effects 0.000 description 1
- 235000013373 food additive Nutrition 0.000 description 1
- 239000002778 food additive Substances 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 239000003349 gelling agent Substances 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- ZEMPKEQAKRGZGQ-XOQCFJPHSA-N glycerol triricinoleate Natural products CCCCCC[C@@H](O)CC=CCCCCCCCC(=O)OC[C@@H](COC(=O)CCCCCCCC=CC[C@@H](O)CCCCCC)OC(=O)CCCCCCCC=CC[C@H](O)CCCCCC ZEMPKEQAKRGZGQ-XOQCFJPHSA-N 0.000 description 1
- 108010067216 glycyl-glycyl-glycine Proteins 0.000 description 1
- 108010015792 glycyllysine Proteins 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 239000007902 hard capsule Substances 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 108010036413 histidylglycine Proteins 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- WGCNASOHLSPBMP-UHFFFAOYSA-N hydroxyacetaldehyde Natural products OCC=O WGCNASOHLSPBMP-UHFFFAOYSA-N 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000015788 innate immune response Effects 0.000 description 1
- 239000002054 inoculum Substances 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 230000007803 itching Effects 0.000 description 1
- 108010090333 leucyl-lysyl-proline Proteins 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 108010054155 lysyllysine Proteins 0.000 description 1
- 230000002101 lytic effect Effects 0.000 description 1
- 210000000260 male genitalia Anatomy 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 239000004530 micro-emulsion Substances 0.000 description 1
- 239000003094 microcapsule Substances 0.000 description 1
- 238000001000 micrograph Methods 0.000 description 1
- 230000001333 moisturizer Effects 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 230000017095 negative regulation of cell growth Effects 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 239000002674 ointment Substances 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 230000035515 penetration Effects 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 230000003132 peptidolytic effect Effects 0.000 description 1
- 230000002688 persistence Effects 0.000 description 1
- 239000000575 pesticide Substances 0.000 description 1
- 238000000053 physical method Methods 0.000 description 1
- 239000000049 pigment Substances 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 239000001818 polyoxyethylene sorbitan monostearate Substances 0.000 description 1
- 235000010989 polyoxyethylene sorbitan monostearate Nutrition 0.000 description 1
- 238000011533 pre-incubation Methods 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000003658 preventing hair loss Effects 0.000 description 1
- 108010029020 prolylglycine Proteins 0.000 description 1
- 239000003380 propellant Substances 0.000 description 1
- 210000002307 prostate Anatomy 0.000 description 1
- 235000019833 protease Nutrition 0.000 description 1
- 235000019419 proteases Nutrition 0.000 description 1
- 238000012827 research and development Methods 0.000 description 1
- 210000002345 respiratory system Anatomy 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 210000003079 salivary gland Anatomy 0.000 description 1
- 239000003352 sequestering agent Substances 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 239000002453 shampoo Substances 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000007901 soft capsule Substances 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 235000013599 spices Nutrition 0.000 description 1
- 239000007921 spray Substances 0.000 description 1
- 238000013097 stability assessment Methods 0.000 description 1
- 238000013112 stability test Methods 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 239000000375 suspending agent Substances 0.000 description 1
- ZJQFYZCNRTZAIM-PMXBASNASA-N tachyplesin Chemical compound C([C@H]1C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@H](C(N[C@H]2CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC=3C=CC=CC=3)NC(=O)[C@@H](NC(=O)[C@H](CC=3C4=CC=CC=C4NC=3)NC(=O)[C@@H](N)CCCCN)CSSC[C@H](NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC2=O)C(=O)N[C@@H](CCCNC(N)=N)C(N)=O)C(=O)N1)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZJQFYZCNRTZAIM-PMXBASNASA-N 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- 238000005382 thermal cycling Methods 0.000 description 1
- 239000002562 thickening agent Substances 0.000 description 1
- 150000004992 toluidines Chemical class 0.000 description 1
- 239000012137 tryptone Substances 0.000 description 1
- 210000004881 tumor cell Anatomy 0.000 description 1
- 210000000689 upper leg Anatomy 0.000 description 1
- 230000002485 urinary effect Effects 0.000 description 1
- 229940099259 vaseline Drugs 0.000 description 1
- 235000013311 vegetables Nutrition 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
- 229940088594 vitamin Drugs 0.000 description 1
- 229930003231 vitamin Natural products 0.000 description 1
- 239000000341 volatile oil Substances 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
- KZTDMJBCZSGHOG-XJIZABAQSA-N α-neoendorphin Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(O)=O)NC(=O)CNC(=O)CNC(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=CC=C1 KZTDMJBCZSGHOG-XJIZABAQSA-N 0.000 description 1
Images
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—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
- A61Q17/00—Barrier preparations; Preparations brought into direct contact with the skin for affording protection against external influences, e.g. sunlight, X-rays or other harmful rays, corrosive materials, bacteria or insect stings
- A61Q17/005—Antimicrobial preparations
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4723—Cationic antimicrobial peptides, e.g. defensins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K19/00—Hybrid peptides, i.e. peptides covalently bound to nucleic acids, or non-covalently bound protein-protein complexes
-
- 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
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/62—DNA sequences coding for fusion proteins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/20—Fusion polypeptide containing a tag with affinity for a non-protein ligand
- C07K2319/21—Fusion polypeptide containing a tag with affinity for a non-protein ligand containing a His-tag
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Engineering & Computer Science (AREA)
- Biophysics (AREA)
- Zoology (AREA)
- Dermatology (AREA)
- Biomedical Technology (AREA)
- Medicinal Chemistry (AREA)
- Epidemiology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Birds (AREA)
- General Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Biotechnology (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Cosmetics (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Plant Pathology (AREA)
- Microbiology (AREA)
- Physics & Mathematics (AREA)
Abstract
Description
The present invention relates to the development of a skin permeable derivative through the fusion of a cell permeable peptide with a long-lasting derivative through the fusion of lauric acid with the antibacterial peptides beta -
Many types of organisms present in the natural world produce antimicrobial peptides outside the body as part of a biological defense system. These antimicrobial peptides are composed of relatively short amino acid sequences (from about 10 to about 100 amino acid residues) and have a net charge of +2 to +9. However, more than 300 species, including Magainin, Cecropin, Defensin, Buforin, Protegrin, and Tachyplesin, have been discovered by researchers around the world, and a series of antimicrobial peptides produced by almost all living organisms, +), Gram-negative bacteria (Gram-), fungi, and tumor cells. Antimicrobial peptides found in eukaryotic multicellular organisms have alpha-helix, beta-sheet or random coil structures. When these peptides bind to the cell membrane, they form an ion channel in the cell membrane to inhibit the energy production of the microorganism, or to make a large hole in the cell membrane, resulting in death of the cell. Unlike conventional antibiotics, which inhibit the cell wall and the synthesis of intracellular polymers, the microorganisms are very resistant to antimicrobial peptides because they have a mechanism of destroying the cell membrane by a nonspecific and effective physical method in a short time, To date, antimicrobial peptides have been reported not to produce resistance. The expression of these antimicrobial peptides in vivo or in vitro may be continuous, and may be caused by bacterial-derived substances such as inflammation-inducing cytokines, bacteria, and lipopolysaccharides (LPS) that stimulate innate immune responses .
As a kind of antimicrobial peptide, human beta-defensin, which is expressed in various tissues including skin, has three cysteine bonds (SS bonds, disulfide bonds) inside the molecule, and the binding pattern between alpha and beta- And the bonding pattern is also constant in the same group. BETADEPHENES The gins are composed of three cysteine bonds (S-S bonds, disulfide bonds) between 1-5, 2-4 and 3-6, and more than 40 to 50 amino acid residues. Basically three beta sheets and one alpha helix structure are maintained, but the number of amino acids between the cysteines is somewhat variable, and the shape and activity of the tertiary structure are known to be more diverse. Compared to alpha-diphenes, which was published more than 20 years ago in the 1980s, beta-diphenzin has been identified biochemically to date so far since human beta -diphenes-1 (HBD-1) was first isolated in human serum in 1995 . After the completion of the human genome project, Schutte and colleagues examined a program called HMMER (a computational search tool based on hidden Markov models) in parallel with BLAST. As a result, the genome of human β- It was confirmed that 28 human betadipense genes can be additionally present on the chromosome No. 1. In particular, the human betadipenin-25 to -29 (HBD25-29) shows a very tissue-specific expression pattern such as the presence of a gene only in the prostate gland and the like. Human betadiphenes-1 (HBD-1) is expressed in epithelial cells such as kidney, female reproductive system, respiratory system, pancreas, gums, tongue and middle ear It has been reported to be present in skin, lungs, airways, gums, and middle ear after first being found in the wound area of the patient. It is known that it is not present at all in urinary or salivary glands such as kidney, bladder and the like. Human betadiphenes-3 (HBD-3) has been reported almost simultaneously from biochemical identification and genome analysis. It has been reported that human beta -diphenin-4 (HBD-4) After being known, unlike human beta -diphenes-1-3 (HBD1-3), it is expressed in male genitalia and stomach. Recently, the present inventors have reported and registered a patent for a beta -diphenes-3 analogue consisting of 77 amino acids which are similar to human beta -
Antimicrobial peptides are emerging as next-generation antibiotics as an alternative to conventional antibiotics resistance, which is becoming a serious problem because many antimicrobial peptides including beta -diphenes have no report on resistance. In addition, since it is small in size compared to protein, it can easily give various mutations to amino acid sequence by methods such as chemical synthesis, peptide synthesis and synthesis with recombinant protein, so that it is possible to search for peptides having various activities superior to the original peptide , Antibiotics, antibiotics, anti-cancer drugs, anti-viral agents, food additives, pesticides, etc., and has the potential to be developed in various fields such as Magainin Pharmaceutical Inc., Micrologix Biotech Inc., Intrabiotics, Xoma There are many companies that are developing antimicrobial peptides. As part of this development, recent efforts to produce antimicrobial peptides composed of dozens of amino acids as recombinant proteins have continued. Especially Escherichia coli) produce recombinant proteins using has been widely used for being fast growth, high yield expression systems, and well-studied protein produced in E. coli. However, if the target protein is an antimicrobial peptide, 1) the accumulated protein product is likely to be toxic to the production host, 2) to avoid the toxicity of the expression product, the production host is not a soluble protein, And 3) the possibility that the production host has a high possibility of degrading the target protein by hydrolysis activity in order to avoid the toxicity of the expression product. exist. To overcome such limitations, codons that are not generated in E. coli may be replaced with codons commonly found in Escherichia coli, or may be produced in the form of fusion proteins with other proteins capable of enhancing aqueous phase expression, Alternatively, several proteins of interest may be repeatedly expressed (tendem repeat) to increase the expression level.
The present inventors have found that the inventors of the present invention have found that human betadiphene-3, which is mainly expressed in the skin and exhibits a broad antibacterial ability, and the human beta -diphenes-3 homolog having similar structure and activity increase the physical stability of the in vivo binding peptide, Lauroyl beta-
Accordingly, it is an object of the present invention to provide beta-diphenzene-3 or 3H (homolog) peptide derivatives to which lauroyl is conjugated.
Another object of the present invention is to provide a cosmetic composition for prevention or improvement of acne or atopic dermatitis comprising the peptide derivative.
Another object of the present invention is to provide an antimicrobial composition comprising the peptide derivative.
It is still another object of the present invention to provide a cell permeable peptide having an amino acid sequence of IWFGW.
It is still another object of the present invention to provide a peptide derivative in which caffeine-alpha-neo-endorphin is bound to the cell permeable peptide.
In order to achieve the above object, the present invention provides lauroyl-linked beta -diphenes-3 or 3H (homolog) peptide derivatives.
In the present invention, the beta -
The present invention provides a cosmetic composition for prevention or improvement of acne or atopic dermatitis containing the peptide derivative.
The present invention provides an antimicrobial composition comprising the peptide derivative.
The present invention provides a cell permeable peptide having an amino acid sequence of IWFGW.
The present invention provides a peptide derivative in which caffeoyl-alpha-neo-endorphin is bound to the cell permeable peptide.
The lauroyl-conjugated beta -
Fig. 1 shows a cleavage map of an expression vector at the time of cloning of a betadiphene-3 analog according to the present invention.
FIG. 2 is a graph showing HPLC results showing the results of lauroylation of NHS-activated lauric acid and beta-
FIG. 3 is a graph of HPLC analysis of beta-
FIG. 4 is a graph showing the results of HPLC analysis of the effect of the beta-
Figure 5 shows experimental results on the increased physical stability of Lauroyl beta-
Figure 6 shows experimental results on the increased physical stability of Lauroyl beta-
Fig. 7 is a graph showing cell stability of lauroyl beta-
FIG. 8 is a graph showing cell stability of lauroyl beta-
FIG. 9 shows the results of an experiment on the cell stability of lauroyl beta-
FIG. 10 shows the results of experiments on the cell stability of lauroyl beta-
FIG. 11 is a microphotograph showing cell stability (48 hours, 37 degrees) of lauroyl beta-
12 is a graph showing antimicrobial effects of Beta-defensin 3 (black circle), -3H (black square), lauroyl beta-defensin 3 (black triangle) and -3H (black lozenge). ( Upper left) Propioneium Antibacterial effect against acnes , (idol) Pseudomonas Antibacterial effect against aeruginosa , (Stable) Streptococcus Antibacterial effect against pygenes , ( Stomach ) Staphylococcus Antibacterial effect against aureus , (lower left) Malassezia Antimicrobial Effect on Species , (Lower Right) Candida Antibacterial effect on albicanss
13 is a graph showing antimicrobial effects of Beta-defensin 3 (black circle), -3H (black square), lauroyl beta-defensin 3 (black triangle) and -3H (black lozenge). (Top) Bacillus Antimicrobial effect on subtilis, (of) Escherichi Antibacterial effect against E. coli , ( Salmonella Antibacterial effect against typhymurium
14 is a microscopic photograph showing the skin permeability of the cell permeable peptide. (Phase) cell permeability of selected cell permeable peptides, (v) distribution of peptide in mouse skin
Hereinafter, the present invention will be described in detail.
The present invention relates to lauroyl-linked
In the present invention, "lauroyl" means a lauroyl group in which a -OH group is removed from lauric acid.
In the present invention,
In the present invention, such a peptide derivative has improved biological stability, physical stability, and the like by producing a novel peptide derivative in which a lauroyl group is conjugated to
Specifically, lauroyl-bound beta -
The results of the experimental results demonstrate that the lauroyl-conjugated beta -
The present invention also relates to a cosmetic composition for preventing or ameliorating atopic dermatitis or acne containing the above peptide derivative.
In the present invention, the composition means to contain beta -
The term "atopic dermatitis" or "acne" in the present invention means a state in which the infected area of the skin is changed by atopic dermatitis and acne, and this state includes both a state considered as a skin disease and a state not regarded as a skin disease do.
In the present invention, " improvement " includes partial cure, improvement and alleviation of atopic dermatitis symptoms as a result of application of the cosmetic composition of the present invention to acne or atopic dermatitis.
In the present invention, " prevention " means that the cosmetic composition of the present invention is applied to the skin, particularly acne and atopic dermatitis to prevent or prevent acne and atopic dermatitis symptoms on the skin, thereby preventing acne and atopic dermatitis from occurring in advance it means.
In the present invention, the peptide derivative may be characterized by containing 0.0001 to 1, or 5 to 10% by weight based on the total weight of the composition. When the amount is less than 0.0001% by weight, the effect is insignificant, and when it is more than 10% by weight, there are problems in safety and formulation stability.
In the present invention, the peptide derivative may be modified and processed into a desired form using known techniques in the art to be used as an effective ingredient in a cosmetic composition.
The present invention also relates to an antimicrobial composition comprising the peptide derivative.
In the present invention, in particular, Propioneium acnes (ATCC or KTCC) (acne), Pseudomonas aeruginosa (ATCC or KTCC) (image infection, sea bass piyeom, stomatitis), Streptococcus pygenes (ATCC or KTCC) (skin suppurative diseases, impetigo), Staphylococcus aureus (ATCC or KTCC) (atopic dermatitis, folliculitis, infestation), Malassezia species (ATCC or KTCC) ( Candida albicans (ATCC or KTCC)), Bacillus subtilis (ATCC or KTCC), Escherichia coli (ATCC or KTCC), Salmonella typhimurium (ATCC or KTCC), and antibiotic compositions for improving, preventing, and treating various diseases caused by infection of these bacteria are included in the scope of the present invention.
Furthermore, Malassezia causing dandruff, hair loss There are antibacterial efficacy of the species, improvement dander, dandruff inhibiting, preventing hair loss, a composition for inhibiting hair loss, hair products, as will also be applicable.
The present invention also provides a cell permeable peptide having an amino acid sequence of IWFGW.
The present invention provides a peptide derivative in which caffeoyl-alpha-neo-endorphin is bound to the cell permeable peptide.
In the present invention, the caffeoyl-alpha-neo-endorphin is an alpha neoendorphin (tyrosine-glycine-glycine-phenylalanine-leucine-arginine-lysine-tyrosine-proline-lysine (YGGFLRKYPK)) to which a caffeoyl group is bound. Peptide derivative, and a description thereof is given in Korean Patent Laid-open No. 10-2013-0032099, and the description of the structural formula is included in the scope of the present invention.
The cosmetic composition of the present invention may contain an acceptable carrier in cosmetic preparations. Herein, "an acceptable carrier for a cosmetic preparation" is a known or used compound or composition that can be contained in a cosmetic preparation, or a compound or composition to be developed in the future, which is toxic, instable or irritating It says nothing.
The carrier may be included in the cosmetic composition of the present invention in an amount of about 1% by weight to about 99.99% by weight, preferably about 90% by weight to about 99.99% by weight of the composition, based on the total weight thereof. However, since the ratio varies depending on the formulations described below in which the composition for external application for skin of the present invention is prepared, and its specific application site (face, neck, etc.) or its preferable application amount and the like, And should not be construed as limiting the scope of the invention.
Examples of the carrier include an alcohol, an oil, a surfactant, a fatty acid, a silicone oil, a wetting agent, a moisturizer, a viscous modifier, an emulsifier, a stabilizer, an ultraviolet scattering agent, an ultraviolet absorber, a coloring agent and a perfume. The compounds / compositions which can be used as the above-mentioned alcohol, oil, surfactant, fatty acid, silicone oil, humectant, humectant, viscous modifier, emulsifier, stabilizer, ultraviolet scattering agent, ultraviolet absorber, The person skilled in the art can select and use the appropriate substance / composition.
As an embodiment of the present invention, the cosmetic composition according to the present invention may contain glycerin, butylene glycol, propylene glycol, polyoxyethylene hardened castor oil, ethanol, triethanolamine, Antiseptic, antiseptic, coloring agent, purified water and the like can be contained as needed.
The cosmetic composition according to the present invention can be prepared in various forms such as lotion, essence, gel, emulsion, lotion, cream (water-in-oil type, water-in-water type, multiphase), solution, suspension (Soft capsules, hard capsules) with a coating such as anhydrous products (oil and glycol), gel, mask, pack, powder, or gelatin.
The skin of the present invention includes not only a face but also a scalp and a whole body. The cosmetic composition applicable to such scalp is a shampoo, a rinse, a treatment, a hair removal agent, etc., and a body cleanser And can be manufactured in various forms as an application of the composition.
The method for producing a peptide derivative-containing cosmetic composition according to the present invention is not limited to the above-described preparation method. Any person skilled in the art will recognize that the method Can be produced.
In particular, the above-mentioned cosmetic composition can be produced in the form of a general emulsified formulation and a solubilized formulation, using a conventionally known manufacturing method, in addition to the manufacturing method specifically disclosed in the present invention.
When the cosmetic composition is manufactured from a cosmetic composition, the cosmetic composition of the emulsified formulation includes nutritional lotion, cream, essence and the like. It can also be prepared in the form of adjuvants which can be applied topically or systemically, which are conventionally used in the field of dermatology by containing a dermatologically acceptable medium or base.
In addition, suitable cosmetic formulations include, for example, solutions, gels, solid or kneaded anhydrous products, emulsions obtained by dispersing an oil phase in water, suspensions, microemulsions, microcapsules, microgranules or ionic forms (liposomes) May be provided in the form of a follicular dispersing agent of the type, cream, skin, lotion, powder, ointment, spray or conical stick. It can also be prepared in the form of a foam or an aerosol composition further containing a compressed propellant.
The cosmetic composition of the present invention may further contain at least one selected from the group consisting of fatty substances, organic solvents, solubilizers, thickeners and gelling agents, softening agents, antioxidants, suspending agents, stabilizers, foaming agents, perfumes, Or any other conventionally used in cosmetics such as nonionic emulsifiers, fillers, sequestering and chelating agents, preservatives, vitamins, barrier agents, wetting agents, essential oils, dyes, pigments, hydrophilic or lipophilic active agents, ≪ RTI ID = 0.0 > cosmetics < / RTI > such as botanical ingredients, or adjuvants conventionally used in the field of dermatology. And, the above ingredients can be introduced in amounts commonly used in the field of dermatology.
Such a cosmetic composition according to the present invention includes forms of functional cosmetics including atopic dermatitis, acne improvement, antibacterial and the like.
Hereinafter, the present invention will be described in more detail with reference to Examples. It is to be understood by those skilled in the art that these embodiments are only for illustrating the present invention and that the scope of the present invention is not construed as being limited by these embodiments.
Development of lauroylation synthesis of recombinant proteins beta-
In the present invention, the recombinant protein beta-
1.1 Recombinant protein beta-
Cloning of the human beta-
First, a primer containing BamH I and Nde I restriction enzyme recognition sequences was designed at each end of sense and antisense based on the cDNA sequence of the
sense primer: 5'-AGTTATTTGAGGAATTCCAC (SEQ ID NO: 4),
antisense primer: 5'-TTATTTCTTTCTTCGGCAGCA (SEQ ID NO: 5)
Were used to select colonies showing the correct PCR products. The colonies were grown properly and glycerol was added to produce expression strains. The strain was used as a strain producing this antimicrobial protein. The cleavage map of the expression vector for cloning into the pET-41b (+) vector for protein expression is shown in Fig.
BL21 (DE3) having the expression vector containing the human beta-
Human beta-defensin 3 (having the amino acid sequence of SEQ ID NO: 1) was also mass produced in the same manner as described above.
1.2 Production of lauroyl beta-
The laurylation between lysine residues in beta-
After the reaction, reverse-phase HPLC was used to purely separate and purify the desired lauroyl beta-
As a result, as shown in FIG. 2 and FIG. 3, peak values before and after the addition of lauroyl group to beta -
In addition, the reaction molar ratio in the reaction of lauric acid with beta -
(beta-
ratio)
(Compared to (-) DMAP)
Therefore, considering the results of 1: 5, which is about 6.5 times higher than that of 1: 1, the reaction molar ratio of beta -
Experimental Example
One:
Lauroyl
beta
-
1.1 Physical Stability Assessment
The enhanced physical stability of novel lauroyl beta-
As a result, beta-
1.2 Evaluation of biological stability
The safety of lauroyl beta-
In order to confirm the biological stability of peptidolytic enzymes secreted by skin cells, which may occur when applied to skin and induced to skin cells, they were reacted with the skin cell disruption liquid for a certain period of time. That is, in order to evaluate the biological stability, 1 x 10 9 keratinocytes constituting human skin cells and fibroblast cell lysate were incubated at 37 ° C for 4 hours and then the relative content of the remaining antimicrobial peptides was evaluated , Lauryl betadiphenes 3 and 3H were prepared at a concentration of 5 mg / ml, exposed to cell-derived lytic enzymes, and 100 μl after exposure, and measured with a bio-analyzer).
As a result, in the stability test, it was confirmed that the lauroylation enhances the stability of the peptide. lauric acid conjugate protected statistically significant biological stability of antimicrobial peptides from peptidase and protease derived from skin cell lysate (Table 2).
Experimental Example
2:
Lauroyl
beta
-
In order to check the cytotoxicity of the cells in the skin configuration vitro MTT test was performed. For this, HaCat cells, human keratinocyte cell line, and CCD-986sk cells, human fibroblast cell line, were used and cytotoxicity was measured at various antimicrobial peptide concentrations. In general, safety experiments using skin cell cultures are known to be at least 100 times more sensitive than human skin experiments by more than 1000 times, It is possible to easily identify possible cytotoxicity even at very low concentrations since it can affect target cells. Adhesion in a culture flask containing this experiment 37 ℃, 5% CO 2 and wetted with an incubator in DMEM culture solution (30 minutes at 56 ℃ comprises a heat-treated
2.1 Safety of keratinocytes
Lauroyl-
Lauroyl beta-
2.2 Confirmation of safety for fibroblasts
In order to confirm the cytotoxicity of fibroblasts constituting the dermis of the skin constituting cells, 1% (10,000 ppm), 0.1% (1,000 ppm), 0.01% (100 ppm), 0.001% 10 ppm) and 0.0001% (1 ppm), respectively, and it was confirmed to be almost safe without cytotoxicity up to 1% (10,000 ppm) used in the test (FIG. To determine the cytotoxicity of lauroyl beta-
Experimental Example
3:
Lauroyl
beta
-
The antibacterial activity of lauroyl beta-
As a result, the antibacterial activity against various microorganisms was examined in vitro using synthetic purified lauroyl beta-defensins, and it was confirmed that the lauroylation increased antimicrobial activity against almost all the test bacteria and persistence over
Experimental Example 4: Skin permeability Peptides Development
In order to develop a novel cell permeable peptide consisting of 5 amino acids, 20 amino acids were synthesized randomly, and FITC, a fluorescent substance, was labeled and then the peptide having the best cell permeability activity was selected.
For this, HaCaT cells, which are human keratinocytes, were cultured in a 12-well plate at 2 × 10 5 cells / well for 48 hours. After washing with PBS, DMEM medium without FBS was added. 50 uM of the fluorescence labeled FITC-labeled peptide was treated for 1 hour. The peptide bound to the cell membrane was analyzed by using a flow cytometer (FACs analysis) after removing proteinase K (10 ug / ml) at 37 ° C for 10 minutes.
In order to confirm the increase of the skin permeability of the material by the selected peptides, caffeoyl-neo-endorphin was applied to the physiologically active substance known to be effective as a model molecule. The synthesized peptides were synthesized in a form fused to the carboxyl terminal of caffeoyl-neo-endorphin (synthetic procedure was performed as described in Korean Patent Laid-Open No. 10-2013-0032099) HR-1 mice (Central Experimental Animals, Korea), widely used, were identified by treatment with samples. To this end, 50 μl (0.25 mg / ml) of HR-1 mouse thigh skin was anesthetized with a peptide labeled with a hydrophilic fluorescent substance FNR-552 (Bioacts) Cutting Temperature solution. The tissue was placed in a vertical position, cryosectioned to a size of 10 μm, fixed on a slide glass, and the distribution of peptides in the skin was observed through a confocal microscope.
Among the randomly synthesized peptides, the peptide having the amino acid sequence of IWFGW had a cell permeation activity. As a result of examining the ability of the peptides to bind to caffeoyl-neo-endorphin (CANE), it was found that CANE-IWFGW (CANE-IWFGW) fused with cell permeable peptides, ) Showed good penetration of the skin (Fig. 14).
Experimental Example
5:
Lauroyl
beta
-
lauroyl beta-defensin-3H antimicrobial peptide was developed and it was verified that the composition had anti-atopic and anti-acne improving effects.
In order to confirm atopic dermatitis and acne improvement effect in this experiment, nine adult male and female subjects with atopic dermatitis and acne treated with lauroyl beta-defensin-3H antimicrobial peptide as a final concentration of 100ppm (100mg / Kg) The composition of the cosmetic composition (composition shown in Table 3 below) was tested by coating 1 ml of the composition twice daily or 1 g of the composition on the cosmetic cotton and applying it to the affected area. After 14 days of application, the improvement effect was quantified in four steps: very effective, slightly effective, ineffective, and worse.
As a result, cosmetic composition containing 100 ppm of lauroyl beta-
As a result of the test, as shown in Table 4, 2 of the 9 patients having atopic dermatitis had very high effect and 6 of them had slightly improved effect, which accounted for 88% of the total. In general, subjects with atopic dermatitis with severe itching remained significantly calm on the fourth day after application, and many darkness remained on the eighth day, and the degree of improvement felt by the subjects was very high.
In the improvement effect of acne, as shown in Table 5, all of the nine persons having acne had a remarkably improved effect to 4 persons and 3 persons to some effects, which accounted for 77% of the total. In the case of subjects who showed a high degree of improvement, it was found that acne with developed inflammation generally calms down from 6th day of application, and many edema disappears on the 11th day, and the degree of improvement felt by the subject is very high.
While the present invention has been particularly shown and described with reference to specific embodiments thereof, those skilled in the art will appreciate that such specific embodiments are merely preferred embodiments and that the scope of the invention is not limited thereby. It will be obvious. Accordingly, the actual scope of the present invention will be defined by the appended claims and their equivalents.
<110> BIO FD & C <120> Development of long acting and cell permeable beta-defensin 3 and -3H by conjugating lauric acid and cell permeable peptide respectively and cosmetic compostion comprising the same <130> 2013-12 <160> 5 <170> Kopatentin 2.0 <210> 1 <211> 67 <212> PRT <213> beta defension 3 <400> 1 Met Arg Ile His Tyr Leu Leu Phe Ala Leu Leu Phe Leu Phe Leu Val 1 5 10 15 Pro Val Pro Gly His Gly Gly Ile Ile Asn Thr Leu Gln Lys Tyr Tyr 20 25 30 Cys Arg Val Gly Gly Gly Arg Cys Ala Val Leu Ser Cys Leu Pro Lys 35 40 45 Glu Glu Gln Ile Gly Lys Cys Ser Thr Arg Gly Arg Lys Cys Cys Arg 50 55 60 Arg Lys Lys 65 <210> 2 <211> 77 <212> PRT <213> beta defensin 3 derivative <400> 2 Met Ser Tyr Leu Arg Asn Ser Thr Ser Leu Val Arg Val Val Lys Ala 1 5 10 15 Phe Leu Lys Pro Phe Arg Val Cys Cys Phe Val Ile Ala Gly His Gly 20 25 30 Gly Ile Ile Asn Thr Leu Gln Lys Tyr Tyr Cys Arg Val Val Gly Gly 35 40 45 Arg Cys Ala Val Leu Ser Cys Leu Pro Lys Glu Glu Gln Ile Gly Lys 50 55 60 Cys Ser Thr Arg Gly Arg Lys Cys Cys Arg Arg Lys Lys 65 70 75 <210> 3 <211> 231 <212> DNA <213> beta defensin 3 derivative <400> 3 agttatttga ggaattccac aagccttgta cgtgtaccaa aagccttcct aaaacctttc 60 cgtgtgtgct gttttgtcat tgcaggtcat ggaggaatca taaacacatt acagaaatat 120 tattgcagag tcagaggcgg ccggtgtgct gtgctcagct gccttccaaa ggaggaacag 180 atcggcaagt gctcgacgcg tggccgaaaa tgctgccgaa gaaagaaata a 231 <210> 4 <211> 20 <212> DNA <213> Artificial Sequence <220> <223> sense primer <400> 4 agttatttga ggaattccac 20 <210> 5 <211> 21 <212> DNA <213> Artificial Sequence <220> <223> antisense primer <400> 5 ttatttcttt cttcggcagc a 21
Claims (8)
Priority Applications (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| PCT/KR2013/011904 WO2015093661A1 (en) | 2013-12-19 | 2013-12-19 | Long-lasting derivative through lauric acid fusion of antibacterial peptide beta-defensin 3 and 3h, development of skin permeable derivative through cell transmissive peptide fusion, and cosmetic composition containing same |
| KR1020130159482A KR101620148B1 (en) | 2013-12-19 | 2013-12-19 | Development of long acting and cell permeable beta-defensin 3 and -3H by conjugating lauric acid and cell permeable peptide respectively and Cosmetic compostion comprising the Same |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| KR1020130159482A KR101620148B1 (en) | 2013-12-19 | 2013-12-19 | Development of long acting and cell permeable beta-defensin 3 and -3H by conjugating lauric acid and cell permeable peptide respectively and Cosmetic compostion comprising the Same |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| KR20150072144A true KR20150072144A (en) | 2015-06-29 |
| KR101620148B1 KR101620148B1 (en) | 2016-05-12 |
Family
ID=53402993
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| KR1020130159482A KR101620148B1 (en) | 2013-12-19 | 2013-12-19 | Development of long acting and cell permeable beta-defensin 3 and -3H by conjugating lauric acid and cell permeable peptide respectively and Cosmetic compostion comprising the Same |
Country Status (2)
| Country | Link |
|---|---|
| KR (1) | KR101620148B1 (en) |
| WO (1) | WO2015093661A1 (en) |
Families Citing this family (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR101873827B1 (en) | 2016-10-25 | 2018-07-03 | 주식회사 라파스 | Micro-needle patch for pimple treatment and manufacturing method for the same |
| KR102068521B1 (en) | 2018-10-29 | 2020-01-21 | 대한민국(농촌진흥청장) | Cosmetic composition comprising teleogryllusine 2 peptide for preventing or improving acne or atopic dermatitis |
Family Cites Families (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR2843125B1 (en) * | 2002-08-02 | 2012-11-16 | Coletica | ACTIVE PRINCIPLES STIMULATING HUMAN BETA-DEFENSIVE TYPE 2 AND / OR TYPE 3, AND COSMETIC OR PHARMACEUTICAL COMPOSITIONS COMPRISING SUCH ACTIVE INGREDIENTS |
| KR100998081B1 (en) * | 2008-04-23 | 2010-12-03 | 한국생명공학연구원 | Antiviral effect of raulic acid and thereof |
| KR100991293B1 (en) * | 2008-08-11 | 2010-11-01 | (주)바이오에프디엔씨 | Novel human beta defensin homolog and its usage as anti-atopic dermatitis agent |
| US9907812B2 (en) * | 2011-06-22 | 2018-03-06 | Vyome Biosciences Pvt. Ltd. | Conjugate-based antifungal and antibacterial prodrugs |
| WO2013042811A1 (en) * | 2011-09-22 | 2013-03-28 | (주)바이오에프디엔씨 | Caffeoyl alpha neoendorphin peptide derivative and use thereof as an anti-itch and anti-atopic material |
-
2013
- 2013-12-19 WO PCT/KR2013/011904 patent/WO2015093661A1/en active Application Filing
- 2013-12-19 KR KR1020130159482A patent/KR101620148B1/en active IP Right Grant
Also Published As
| Publication number | Publication date |
|---|---|
| WO2015093661A1 (en) | 2015-06-25 |
| KR101620148B1 (en) | 2016-05-12 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| KR101899552B1 (en) | Antimicrobial Peptide Analogues Derived From The Abalone, Haliotis Discus, And Antimicrobial Pharmaceutical Composition Containing The Same | |
| CN104379177B (en) | Short antimicrobial lipopeptid | |
| KR101944388B1 (en) | Skin penetrating peptide and method of use thereof | |
| KR101734064B1 (en) | Novel antimicrobial peptide derived from myxinidin peptide and uses thereof | |
| KR20130032788A (en) | Peptides for promotion of hair growth and the use thereof | |
| CN111518163B (en) | Application of lipopeptide compounds in resisting novel coronavirus | |
| KR101620148B1 (en) | Development of long acting and cell permeable beta-defensin 3 and -3H by conjugating lauric acid and cell permeable peptide respectively and Cosmetic compostion comprising the Same | |
| KR100991293B1 (en) | Novel human beta defensin homolog and its usage as anti-atopic dermatitis agent | |
| KR101430084B1 (en) | Novel antibiotic peptide against Propionibacterium acnes and use therof | |
| KR101977800B1 (en) | Pseudomonas specific antimicrobial peptide and antimicrobial composition comprising the same | |
| KR102215798B1 (en) | Preservative composition including peptide having antibacterial activity and cosmetic composition having the same | |
| KR102541856B1 (en) | Cosmetic composition for antibacterial comprising the fk-13 peptide as an active ingredient | |
| DE60125809T2 (en) | DIASTEREOME PEPTIDES AND THESE COMPREHENSIVE MEDICAMENTS | |
| KR102243335B1 (en) | Antimicrobial peptide, Protaetiamycine 3 derived from protaetia brevitarsis seulensis and uses thereof | |
| KR102114842B1 (en) | Topical Formulation Composed of Cell Permeable basic Fibroblast Growth Factor (LMWP-bFGF) fusion protein with Skin Physiological Activity | |
| EP3336098B1 (en) | Skin permeable peptide and method for using same | |
| KR101326164B1 (en) | External Composition for Skin Having Antibacterial Activities | |
| KR102206808B1 (en) | Novel cell-penetrating peptiedes and composition for skin improvement including the same | |
| KR102540598B1 (en) | Antibacterial peptide derived from Crassostrea gigas and its use | |
| KR102093209B1 (en) | Conjugate of isotretinoin and peptide | |
| KR102554966B1 (en) | Cosmetic composition for antibacterial comprising the indolicidin analog as an active ingredient | |
| CN117466974B (en) | Antimicrobial peptide and application thereof | |
| KR102358469B1 (en) | Antimicrobial peptide derived from Impatiens balsamina and antimicrobial composition comprising the same | |
| KR20230094681A (en) | Antimicrobial composition comprising polyamidoamine dendrimer derivatives as effective component | |
| KR101791286B1 (en) | Composition for Preventing or Treating of Atopic Dermatitis Comprising Chitinase |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A201 | Request for examination | ||
| E902 | Notification of reason for refusal | ||
| E90F | Notification of reason for final refusal | ||
| E701 | Decision to grant or registration of patent right | ||
| GRNT | Written decision to grant | ||
| FPAY | Annual fee payment |
Payment date: 20190415 Year of fee payment: 4 |