Peptydy przeciwdrobnoustrojowe (Antimicrobial peptides)
Nazwa/Name | Sekwencja/Sequence | M.W. | Cena/Price |
Aurein 1.11 | GLFDIIKKIAESI-NH2 Gly-Leu-Phe-Asp-Ile-Ile-Lys-Lys-Ile-Ala-Glu-Ser-Ile-NH2 |
1445.72 | |
Bactenecin 2A (Bac2A)2 | RLARIVVIRVAR-NH2 Arg-Leu-Ala-Arg-Ile-Val-Val-Ile-Arg-Val-Ala-Arg-NH2 |
1420.78 | |
Beta amyloid peptide (1-42)3 | DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val-Ile-Ala |
4514.02 | |
Buforin II4 | TRSSRAGLQFPVGRVHRLLRK Thr-Arg-Ser-Ser-Arg-Ala-Gly-Leu-Gln-Phe-Pro-Val-Gly-Arg-Val-His-Arg-Leu-Leu-Arg-Lys |
2434.83 | |
CAMEL5 | KWKLFKKIGAVLKVL-NH2 Lys-Trp-Lys-Leu-Phe-Lys-Lys-Ile-Gly-Ala-Val-Leu-Lys-Val-Leu-NH2 |
1770.28 | |
Cecropin A6 | KWKLFKKIEKVGQNIRDGIIKAGPAVAVVGQATQIAK-NH2 Lys-Trp-Lys-Leu-Phe-Lys-Lys-Ile-Glu-Lys-Val-Gly-Gln-Asn-Ile-Arg-Asp-Gly-Ile-Ile-Lys-Ala-Gly-Pro-Ala-Val-Ala-Val-Val-Gly-Gln-Ala-Thr-Gln-Ile-Ala-Lys-NH2 |
4003.76 | |
Citropin 1.17 | GLFDVIKKVASVIGGL-NH2 Gly-Leu-Phe-Asp-Val-Ile-Lys-Lys-Val-Ala-Ser-Val-Ile-Gly-Gly-Leu-NH2 |
1614.95 | |
Dermaseptin8 | ALWKTMLKKLGTMALHAGKAALGAAADTISQGTQ-NH2 Ala-Leu-Trp-Lys-Thr-Met-Leu-Lys-Lys-Leu-Gly-Thr-Met-Ala-Leu-His-Ala-Gly-Lys-Ala-Ala-Leu-Gly-Ala-Ala-Ala-Asp-Thr-Ile-Ser-Gln-Gly-Thr-Gln-NH2 |
3454.05 | |
Drosocin9 | GKPRPYSPRPTSHPRPIRV Gly-Lys-Pro-Arg-Pro-Tyr-Ser-Pro-Arg-Pro-Thr-Ser-His-Pro-Arg-Pro-Ile-Arg-Val |
2198.51 | |
Histatin 510 | DSHAKRHHGYKRKFHEKHHSHRGY Asp-Ser-His-Ala-Lys-Arg-His-His-Gly-Tyr-Lys-Arg-Lys-Phe-His-Glu-Lys-His-His-Ser-His-Arg-Gly-Tyr |
3036.27 | |
Histatin 811 | KFHEKHHSHRGY Lys-Phe-His-Glu-Lys-His-His-Ser-His-Arg-Gly-Tyr |
1562.67 | |
IB-36712 | RGGLCYCRGRFCVCVGR-NH2 Arg-Gly-Gly-Leu-Cys-Tyr-Cys-Arg-Gly-Arg-Phe-Cys-Val-Cys-Val-Gly-Arg-NH2 |
1905.30 | |
Indolicidin13 | ILPWKWPWWPWRR-NH2 Ile-Leu-Pro-Trp-Lys-Trp-Pro-Trp-Trp-Pro-Trp-Arg-Arg-NH2 |
1906.26 | |
Lactoferricin B14 | FKCRRWQWRMKKLGAPSITCVRRAF (S-S BOND) Phe-Lys-Cys-Arg-Arg-Trp-Gln-Trp-Arg-Met-Lys-Lys-Leu-Gly-Ala-Pro-Ser-Ile-Thr-Cys-Val-Arg-Arg-Ala-Phe (S - S BOND) |
3123.80 | |
LL-3715,16 | LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser |
4493.33 | |
Melittin17 | GIGAVLKVLTTGLPALISWIKRKRQQ-NH2 Gly-Ile-Gly-Ala-Val-Leu-Lys-Val-Leu-Thr-Thr-Gly-Leu-Pro-Ala-Leu-Ile-Ser-Trp-Ile-Lys-Arg-Lys-Arg-Gln-Gln-NH2 |
2846.48 | |
MSI-78 (pexiganan)18 | GIGKFLKKAKKFGKAFVKILKK-NH2 Gly-Ile-Gly-Lys-Phe-Leu-Lys-Lys-Ala-Lys-Lys-Phe-Gly-Lys-Ala-Phe-Val-Lys-Ile-Leu-Lys-Lys-NH2 |
2477.19 | |
Nisin A | ITSISLCTPGCKTGALMGCNMKTATCHCSIHVSK-NH2 Ile-Thr-Ser-Ile-Ser-Leu-Cys-Thr-Pro-Gly-Cys-Lys-Thr-Gly-Ala-Leu-Met-Gly-Cys-Asn-Met-Lys-Thr-Ala-Thr-Cys-His-Cys-Ser-Ile-His-Val-Ser-Lys-NH2 |
3497.22 | |
MBI-226 (Omiganan) | ILRWPWWPWRRK-NH2 Ile-Leu-Arg-Trp-Pro-Trp-Trp-Pro-Trp-Arg-Arg-Lys-NH2 |
1779.17 | |
Protegrin 120 | RGGRLCYCRRRFCVCVGR-NH2 (disulfide bridge:6-15 and 8-13) Arg-Gly-Gly-Arg-Leu-Cys-Tyr-Cys-Arg-Arg-Arg-Phe-Cys-Val-Cys-Val-Gly-Arg-NH2 (disulfide bridge:6 - 15 and 8 - 13) |
2155.64 | |
Tachyplesin III21 | KWCFRVCYRGICYRKCR-NH2 Lys-Trp-Cys-Phe-Arg-Val-Cys-Tyr-Arg-Gly-Ile-Cys-Tyr-Arg-Lys-Cys-Arg-NH2 |
2239.76 | |
Temporin A22 | FLPLIGRVLSGIL-NH2 Phe-Leu-Pro-Leu-Ile-Gly-Arg-Val-Leu-Ser-Gly-Ile-Leu-NH2 |
1396.76 | |
Thymosin beta-423 | SDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser |
4921.47 | |
Palm-GHK24,25 | Pal-Gly-His-Lys | ||
Palm-KTTKS26 | Pal-Lys-Thr-Thr-Lys-Ser | ||
Palm-GQPR27 | Pal-Gly-Gln-Pro-Arg | ||
Palm-VGVAPG28 | Pal-Val-Gly-Val-Ala-Pro-Gly | ||
Ac-EEMQRR-NH229 | Ac-Glu-Glu-Met-Gln-Arg-Arg-NH2 | ||
Octa-arginine (Arg)(8) |
RRRRRRRR Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg |
Długie peptydy (Long (>40AA) peptides)
Nazwa/Name | Sekwencja/Sequence | M.W. | Nazwa/Price |
Beta Amyloid 1-42 | DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val-Ile-Ala |
4514.02 | |
LL-37 | LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser |
4493.33 | |
LL-37 reverse | SETRPVLNRLFDKIRQVIRKFEKGIKEKSKRFFDGLL Ser-Glu-Thr-Arg-Pro-Val-Leu-Asn-Arg-Leu-Phe-Asp-Lys-Ile-Arg-Gln-Val-Ile-Arg-Lys-Phe-Glu-Lys-Gly-Ile-Lys-Glu-Lys-Ser-Lys-Arg-Phe-Phe-Asp-Gly-Leu-Leu |
4493.33 | |
Thymosin | SDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES Ser-Asp-Lys-Pro-Asp-Met-Ala-Glu-Ile-Glu-Lys-Phe-Asp-Lys-Ser-Lys-Leu-Lys-Lys-Thr-Glu-Thr-Gln-Glu-Lys-Asn-Pro-Leu-Pro-Ser-Lys-Glu-Thr-Ile-Glu-Gln-Glu-Lys-Gln-Ala-Gly-Glu-Ser |
4921.47 |
Inne peptydy syntetyczne i lipopeptydy (Other synthetic peptides and lipopeptides)
Peptydy kosmetyczne (Cosmetic peptides)
Nazwa/Name | Sekwencja/Sequence | M.W. | Cena/Price |
Palm-GHK | Palm-GHK Palm-Gly-His-Lys |
578.78 | |
Palmitoyl Pentapeptide | Palm-KTTKS Palm-Lys-Thr-Thr-Lys-Ser |
802.05 | |
Palmitoyl Tetrapeptide-3 | Palm-GQPR Palm-Gly-Gln-Pro-Arg |
694.90 | |
Palmitoyl Hexapeptide | Palm-VGVAPG Palm-Val-Gly-Val-Ala-Pro-Gly |
736.98 | |
Acetyl Hexapeptide-3 | Ac-EEMQRR-NH2 Ac-Glu-Glu-Met-Gln-Arg-Arg-NH2 |
888.98 |
Fmoc-N-dipeptydy (Fmoc-protected dipeptides)
Nazwa/Name | M.W. | Cena/Price |
Fmoc-β-Ala-Asn(Trt)-OH | 667.76 | |
Fmoc-Asn(Trt)-Asn(Trt)-OH | 953.11 | |
Fmoc-Cys(Trt)-Cys(Trt)-OH | 931.19 | |
Fmoc-β-Ala-Glu(OtBu)-OH | 496.56 | |
Fmoc-Glu(OtBu)-Glu(OtBu)-OH | 610.70 | |
Fmoc-β-Ala-Gln(Trt)-OH | 681.79 | |
Fmoc-Gln(Trt)-Gln(Trt)-OH | 981.16 | |
Fmoc-β-Ala-Gly-OH | 368.39 | |
Fmoc-β-Ala-His(Trt)-OH | 690.80 | |
Fmoc-His(Trt)-His(Trt)-OH | 999.18 | |
Fmoc-β-Ala-Leu-OH | 424.50 | |
Fmoc-β-Ala-Pro-OH | 408.45 |
Peptydy penetrujące komórkę (Cell Permeable Peptide)
Nazwa/Name | Sekwencja/Sequence | M.W. | Cena/Price |
(Arg)9 RRRRRRRRR | RRRRRRRRR Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg |
1423.6 |
1. Rozek, T. et al. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2. Eur. J. Biochem. 267, 5330–41 (2000).
2. Hilpert, K. et al. Sequence Requirements and an Optimization Strategy for Short Antimicrobial Peptides. Chem. Biol. 13, 1101–1107 (2006).
3. Soscia, S. J. et al. The Alzheimer’s Disease-Associated Amyloid β-Protein Is an Antimicrobial Peptide. PLoS One 5, e9505 (2010).
4. Park, C. B., Kim, M. S. & Kim, S. C. A Novel Antimicrobial Peptide fromBufo bufo gargarizans. Biochem. Biophys. Res. Commun. 218, 408–413 (1996).
5. Andreu, D. et al. Shortened cecropin A-melittin hybrids. Significant size reduction retains potent antibiotic activity. FEBS Lett. 296, 190–4 (1992).
6. Steiner, H., Hultmark, D., Engström, A., Bennich, H. & Boman, H. G. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292, 246–8 (1981).
7. Wegener, K. L. et al. Host defence peptides from the skin glands of the Australian blue mountains tree-frog Litoria citropa. Solution structure of the antibacterial peptide citropin 1.1. Eur. J. Biochem. 265, 627–37 (1999).
8. Mor, A., Nguyen Van Huong, N. Van, Delfour, A., Migliore-Samour, D. & Nicolas, P. Isolation, amino acid sequence and synthesis of dermaseptin, a novel antimicrobial peptide of amphibian skin. Biochemistry 30, 8824–8830 (1991).
9. Bulet, P. et al. A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution. J. Biol. Chem. 268, 14893–7 (1993).
10. Oppenheim, F. G. et al. Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans. J. Biol. Chem. 263, 7472–7 (1988).
11. Yin, A. et al. Physical parameters of hydroxyapatite adsorption and effect on candidacidal activity of histatins. Arch. Oral Biol. 48, 361–8 (2003).
12. Mosca, D. A. et al. IB-367, a protegrin peptide with in vitro and in vivo activities against the microflora associated with oral mucositis. Antimicrob. Agents Chemother. 44, 1803–8 (2000).
13. Selsted, M. E. et al. Indolicidin, a novel bactericidal tridecapeptide amide from neutrophils. J. Biol. Chem. 267, 4292–5 (1992).
14. Bellamy, W., Takase, M., Wakabayashi, H., Kawase, K. & Tomita, M. Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin. J. Appl. Bacteriol. 73, 472–9 (1992).
15. Agerberth, B. et al. FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis. Proc. Natl. Acad. Sci. U. S. A. 92, 195–9 (1995).
16. Bandurska, K., Berdowska, A., Barczyńska-Felusiak, R. & Krupa, P. Unique features of human cathelicidin LL-37. BioFactors 41, 289–300 (2015).
17. Fennell, J. F., Shipman, W. H. & Cole, L. J. Antibacterial action of a bee venom fraction (melittin) against a penicillin-resistant staphylococcus and other microorganisms. USNRDL-TR-67-101. Res. Dev. Tech. Rep. 1–13 (1967).
18. Maloy, W. L. & Kari, U. P. Structure-activity studies on magainins and other host defense peptides. Biopolymers 37, 105–122 (1995).
19. Fraser, J. R., West, M. H. P., Krieger, T. J., Taylor, R. & Erfle, D. Compositions and methods for treating infections using analogues of indolicidin. (1998).
20. Tamamura, H. et al. Synthesis of protegrin-related peptides and their antibacterial and anti-human immunodeficiency virus activity. Chem. Pharm. Bull. (Tokyo). 43, 853–8 (1995).
21. Muta, T., Fujimoto, T., Nakajima, H. & Iwanaga, S. Tachyplesins isolated from hemocytes of Southeast Asian horseshoe crabs (Carcinoscorpius rotundicauda and Tachypleus gigas): identification of a new tachyplesin, tachyplesin III, and a processing intermediate of its precursor. J. Biochem. 108, 261–6 (1990).
22. Simmaco, M. et al. Temporins, antimicrobial peptides from the European red frog Rana temporaria. Eur. J. Biochem. 242, 788–92 (1996).
23. Low, T. L. K., Wang, S. S. & Goldstein, A. L. Solid-phase synthesis of thymosin .beta.4: chemical and biological characterization of the synthetic peptide. Biochemistry 22, 733–740 (1983).
24. Maquart, F. X. et al. Stimulation of collagen synthesis in fibroblast cultures by the tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+. FEBS Lett. 238, 343–6 (1988).
25. Lintner, K. & Peschard, O. Biologically active peptides: from a laboratory bench curiosity to a functional skin care product. Int. J. Cosmet. Sci. 22, 207–218 (2000).
26. Robinson, L. R. et al. Topical palmitoyl pentapeptide provides improvement in photoaged human facial skin1. Int. J. Cosmet. Sci. 27, 155–160 (2005).
27. Lourith, N. & Kanlayavattanakul, M. Biopolymeric agents for skin wrinkle treatment. J. Cosmet. Laser Ther. 18, 301–310 (2016).
28. Kamoun, A. et al. Growth Stimulation of Human Skin Fibroblasts by Elastin-Derived Peptides. Cell Adhes. Commun. 3, 273–281 (1995).
29. Kraeling, M. E. K., Zhou, W., Wang, P. & Ogunsola, O. A. In vitro skin penetration of acetyl hexapeptide-8 from a cosmetic formulation. Cutan. Ocul. Toxicol. 34, 46–52 (2015).
30. Futaki, S. Oligoarginine vectors for intracellular delivery: Design and cellular-uptake mechanisms. Biopolymers 84, 241–249 (2006).