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Antimicrobial peptides

Name Sequence M.W. Price
Aurein 1.11 GLFDIIKKIAESI-NH2
Gly-Leu-Phe-Asp-Ile-Ile-Lys-Lys-Ile-Ala-Glu-Ser-Ile-NH2
1445.72 e-mail
Bactenecin 2A (Bac2A)2 RLARIVVIRVAR-NH2
Arg-Leu-Ala-Arg-Ile-Val-Val-Ile-Arg-Val-Ala-Arg-NH2
1420.78 e-mail
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 e-mail
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 e-mail
CAMEL5 KWKLFKKIGAVLKVL-NH2
Lys-Trp-Lys-Leu-Phe-Lys-Lys-Ile-Gly-Ala-Val-Leu-Lys-Val-Leu-NH2
1770.28 e-mail
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 e-mail
Citropin 1.17 GLFDVIKKVASVIGGL-NH2
Gly-Leu-Phe-Asp-Val-Ile-Lys-Lys-Val-Ala-Ser-Val-Ile-Gly-Gly-Leu-NH2
1614.95 e-mail
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 e-mail
Drosocin9 GKPRPYSPRPTSHPRPIRV
Gly-Lys-Pro-Arg-Pro-Tyr-Ser-Pro-Arg-Pro-Thr-Ser-His-Pro-Arg-Pro-Ile-Arg-Val
2198.51 e-mail
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 e-mail
Histatin 811 KFHEKHHSHRGY
Lys-Phe-His-Glu-Lys-His-His-Ser-His-Arg-Gly-Tyr
1562.67 e-mail
IB-36712 RGGLCYCRGRFCVCVGR-NH2
Arg-Gly-Gly-Leu-Cys-Tyr-Cys-Arg-Gly-Arg-Phe-Cys-Val-Cys-Val-Gly-Arg-NH2
1905.30 e-mail
Indolicidin13 ILPWKWPWWPWRR-NH2
Ile-Leu-Pro-Trp-Lys-Trp-Pro-Trp-Trp-Pro-Trp-Arg-Arg-NH2
1906.26 e-mail
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 e-mail
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 e-mail
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 e-mail
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 e-mail
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 e-mail
MBI-226 (Omiganan) ILRWPWWPWRRK-NH2
Ile-Leu-Arg-Trp-Pro-Trp-Trp-Pro-Trp-Arg-Arg-Lys-NH2
1779.17 e-mail
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 e-mail
Tachyplesin III21 KWCFRVCYRGICYRKCR-NH2
Lys-Trp-Cys-Phe-Arg-Val-Cys-Tyr-Arg-Gly-Ile-Cys-Tyr-Arg-Lys-Cys-Arg-NH2
2239.76 e-mail
Temporin A22 FLPLIGRVLSGIL-NH2
Phe-Leu-Pro-Leu-Ile-Gly-Arg-Val-Leu-Ser-Gly-Ile-Leu-NH2
1396.76 e-mail
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 e-mail
Palm-GHK24,25  Pal-Gly-His-Lys   e-mail
Palm-KTTKS26  Pal-Lys-Thr-Thr-Lys-Ser   e-mail
Palm-GQPR27  Pal-Gly-Gln-Pro-Arg   e-mail
Palm-VGVAPG28 Pal-Val-Gly-Val-Ala-Pro-Gly   e-mail
Ac-EEMQRR-NH229  Ac-Glu-Glu-Met-Gln-Arg-Arg-NH2   e-mail
Octa-arginine
(Arg)(8)
RRRRRRRR
Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg
  e-mail

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Long (>40AA) peptides

Name Sequence M.W. 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 e-mail
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 e-mail
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 e-mail
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 e-mail


Other synthetic peptides and lipopeptides

Cosmetic peptides

Name Sequence M.W. Price
Palm-GHK Palm-GHK
Palm-Gly-His-Lys
578.78 e-mail
Palmitoyl Pentapeptide Palm-KTTKS
Palm-Lys-Thr-Thr-Lys-Ser
802.05 e-mail
Palmitoyl Tetrapeptide-3 Palm-GQPR
Palm-Gly-Gln-Pro-Arg
694.90 e-mail
Palmitoyl Hexapeptide Palm-VGVAPG
Palm-Val-Gly-Val-Ala-Pro-Gly
736.98 e-mail
Acetyl Hexapeptide-3 Ac-EEMQRR-NH2
Ac-Glu-Glu-Met-Gln-Arg-Arg-NH2
888.98 e-mail

Fmoc-protected dipeptides

Name M.W. Price
Fmoc-β-Ala-Asn(Trt)-OH  667.76 e-mail
Fmoc-Asn(Trt)-Asn(Trt)-OH  953.11 e-mail
Fmoc-Cys(Trt)-Cys(Trt)-OH  931.19 e-mail
Fmoc-β-Ala-Glu(OtBu)-OH  496.56 e-mail
Fmoc-Glu(OtBu)-Glu(OtBu)-OH  610.70 e-mail
Fmoc-β-Ala-Gln(Trt)-OH  681.79 e-mail
Fmoc-Gln(Trt)-Gln(Trt)-OH  981.16 e-mail
Fmoc-β-Ala-Gly-OH  368.39 e-mail
Fmoc-β-Ala-His(Trt)-OH  690.80 e-mail
Fmoc-His(Trt)-His(Trt)-OH  999.18 e-mail
Fmoc-β-Ala-Leu-OH  424.50 e-mail
Fmoc-β-Ala-Pro-OH  408.45 e-mail

Cell Permeable Peptide

Name Sequence M.W. Price
(Arg)9 RRRRRRRRR RRRRRRRRR
Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg
1423.6 e-mail



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).
 


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