De novo generation of short antimicrobial peptides with enhanced stability and cell specificity

Journal of Antimicrobial Chemotherapy

Volumn 69, Issue 1, 2014, Pages 121-132

  Kim, Hyun ^a   Jang, Ju Hye ^a   Kim, Sun Chang ^b   Cho, Ju Hyun ^a  

^a Gyeongsang National University   (South Korea)

^b Korea Advanced Institute of Science and Technology (KAIST)   (South Korea)

Author keywords

AMPs; Antibiotic resistant bacteria; Peptide antibiotics

Indexed keywords

BETA GALACTOSIDASE; CHYMOTRYPSIN; GNU 1; GNU 2; GNU 3; GNU 4; GNU 5; GNU 6; GNU 7; MAGAININ 2; POLYPEPTIDE ANTIBIOTIC AGENT; TRYPSIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANTIBACTERIAL ACTIVITY; ANTIBIOTIC RESISTANCE; ANTIFUNGAL ACTIVITY; ARTICLE; CELL SPECIFICITY; CELL VIABILITY; CIRCULAR DICHROISM; CONTROLLED STUDY; CYTOTOXICITY; DRUG DESIGN; DRUG POTENCY; DRUG STABILITY; DRUG SYNTHESIS; ERYTHROCYTE; FIELD EMISSION SCANNING ELECTRON MICROSCOPY; FUNGUS; GRAM NEGATIVE BACTERIUM; GRAM POSITIVE BACTERIUM; HEMOLYSIS; HUMAN; HUMAN CELL; HYDROPHOBICITY; IN VITRO STUDY; KERATINOCYTE; MEMBRANE PERMEABILITY; METHICILLIN RESISTANT STAPHYLOCOCCUS AUREUS; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; PROTEIN DEGRADATION; PROTEIN SECONDARY STRUCTURE; SCANNING ELECTRON MICROSCOPY; SKIN FIBROBLAST; VANCOMYCIN RESISTANT ENTEROCOCCUS;

AMPS; ANTIBIOTIC-RESISTANT BACTERIA; PEPTIDE ANTIBIOTICS;

ANTIMICROBIAL CATIONIC PEPTIDES; BACTERIA; BACTERIAL PROTEINS; CELL MEMBRANE; CELL MEMBRANE PERMEABILITY; CELL SURVIVAL; CELLS, CULTURED; CHYMOTRYPSIN; ERYTHROCYTES; FIBROBLASTS; FUNGI; HUMANS; KERATINOCYTES; METALLOENDOPEPTIDASES; MICROBIAL SENSITIVITY TESTS; MICROSCOPY, ELECTRON, SCANNING; PROTEIN STABILITY; PROTEOLYSIS; TRYPSIN;

EID: 84890381519     PISSN: 03057453     EISSN: 14602091     Source Type: Journal    
DOI: 10.1093/jac/dkt322     Document Type: Article

References (53)

1. Boman HG. Peptide antibiotics and their role in innate immunity. Annu Rev Immunol 1995; 13: 61-92.
2. ZasloffM. Antimicrobial peptides of multicellular organisms. Nature 2002; 415: 389-95.
3. Fjell CD, Hiss JA, Hancock RE et al. Designing antimicrobial peptides: form follows function. Nat Rev Drug Discov 2011; 11: 37-51.
4. Hancock RE, Sahl HG. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat Biotechnol 2006; 24: 1551-7.
5. Mookherjee N, Hancock RE. Cationic host defence peptides: innate immune regulatory peptides as a novel approach for treating infections. Cell Mol Life Sci 2007; 64: 922-33.
6. Navon-Venezia S, Feder R, Gaidukov L et al. Antibacterial properties of dermaseptin S4 derivatives with in vivo activity. Antimicrob Agents Chemother 2002; 46: 689-94.
7. Pereira HA. Novel therapies based on cationic antimicrobial peptides. Curr Pharm Biotechnol 2006; 7: 229-34.
8. Shai Y, Makovitzky A, Avrahami D. Host defense peptides and lipopeptides: modes of action and potential candidates for the treatment of bacterial and fungal infections. Curr Protein Pept Sci 2006; 7: 479-86.
9. Mangoni ML. Host-defense peptides: from biology to therapeutic strategies. Cell Mol Life Sci 2011; 68: 2157-9.
10. GoldmanMJ, AndersonGM, StolzenbergEDet al. Humanb-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. Cell 1997; 88: 553-60.
11. Maisetta G, Di Luca M, Esin S et al. Evaluation of the inhibitory effects of humanserum components on bactericidal activity of humanbeta defensin 3. Peptides 2008; 29: 1-6.
12. Oyston PC, Fox MA, Richards SJ et al. Novel peptide therapeutics for treatment of infections. J Med Microbiol 2009; 58: 977-87.
13. Vlieghe P, Lisowski V, Martinez J et al. Synthetic therapeutic peptides: science and market. Drug Discov Today 2010; 15: 40-56.
14. Sieprawska-Lupa M, Mydel P, Krawczyk K et al. Degradation of human antimicrobial peptide LL-37 by Staphylococcus aureus-derived proteinases. Antimicrob Agents Chemother 2004; 48: 4673-9.
15. Koprivnjak T, Peschel A. Bacterial resistance mechanisms against host defense peptides. Cell Mol Life Sci 2011; 68: 2243-54.
16. Podorieszach AP, Huttunen-Hennelly HE. The effects of tryptophan and hydrophobicity on the structure and bioactivity of novel indolicidin derivatives with promising pharmaceutical potential. Org Biomol Chem 2010; 8: 1679-87.
17. Hawrani A, Howe RA, Walsh TR et al. Origin of low mammalian cell toxicity in a class of highly active antimicrobial amphipathic helical peptides. J Biol Chem 2008; 283: 18636-45.
18. Ciornei CD, Sigurdardottir T, Schmidtchen A et al. Antimicrobial and chemoattractant activity, lipopolysaccharide neutralization, cytotoxicity, and inhibition by serum of analogs of human cathelicidin LL-37. Antimicrob Agents Chemother 2005; 49: 2845-50.
19. Stromstedt AA, Pasupuleti M, Schmidtchen A et al. Evaluation of strategies for improving proteolytic resistance of antimicrobial peptides by using variants of EFK17, an internal segment of LL-37. Antimicrob Agents Chemother 2009; 53: 593-602.
20. John H, Maronde E, ForssmannWGet al. N-terminal acetylation protects glucagon-like peptide GLP-1-(7-34)-amide from DPP-IV-mediated degradation retaining cAMP- and insulin-releasing capacity. Eur J Med Res 2008; 13: 73-8.
21. Giuliani A, Rinaldi AC. Beyond natural antimicrobial peptides: multimeric peptides and other peptidomimetic approaches. Cell Mol Life Sci 2011; 68: 2255-66.
22. Matsuzaki K. Magainins as paradigm for the mode of action of pore forming polypeptides. Biochim Biophys Acta 1998; 1376: 391-400.
23. Jang SA, Kim H, Lee JY et al. Mechanism of action and specificity of antimicrobial peptides designed based on buforin IIb. Peptides 2012; 34: 283-9.
24. Cho JH, Sung BH, Kim SC. Buforins: histone H2A-derived antimicrobial peptides from toad stomach. Biochim Biophys Acta 2009; 1788: 1564-9.
25. Park IY, Cho JH, Kim KS et al. Helix stability confers salt resistance upon helical antimicrobial peptides. J Biol Chem 2004; 279: 13896-901.
26. Bucki R, Sostarecz AG, Byfield FJ et al. Resistance of the antibacterial agent ceragenin CSA-13 to inactivation by DNA or F-actin and its activity in cystic fibrosis sputum. J Antimicrob Chemother 2007; 60: 535-45.
27. Jang JH, Kim MY, Lee JW et al. Enhancement of the cancer targeting specificity of buforin IIb by fusion with an anionic peptide via a matrix metalloproteinases-cleavable linker. Peptides 2011; 32: 895-9.
28. Schoop VM, Mirancea N, Fusenig NE. Epidermal organization and differentiation of HaCaT keratinocytes in organotypic coculture with human dermal fibroblasts. J Invest Dermatol 1999; 112: 343-53.
29. Greenfield N, Fasman GD. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 1969; 8: 4108-16.
30. Lehrer RI, Barton A, Daher KA et al. Interaction of human defensins with Escherichia coli. Mechanism of bactericidal activity. J Clin Invest 1989; 84: 553-61.
31. Zelezetsky I, Tossi A. Alpha-helical antimicrobial peptides-using a sequence template to guide structure-activity relationship studies. Biochim Biophys Acta 2006; 1758: 1436-49.
32. Walsh KA. Trypsinogens and trypsins of various species. In: Gertrude E, Perlmann LL, eds. Methods in Enzymology, Vol. 19. Academic Press, New York, 1970; 41-63.
33. Craik CS, Largman C, Fletcher T et al. Redesigning trypsin: alteration of substrate specificity. Science 1985; 228: 291-7.
34. Harris JL, Backes BJ, Leonetti F et al. Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries. Proc Natl Acad Sci USA 2000; 97: 7754-9.
35. Hedstrom L. Serine protease mechanism and specificity. Chem Rev 2002; 102: 4501-24.
36. Matsuzaki K, Sugishita K, HaradaMet al. Interactions ofanantimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria. Biochim Biophys Acta 1997; 1327: 119-30.
37. Epand RM, Vogel HJ. Diversity of antimicrobial peptides and their mechanisms of action. Biochim Biophys Acta 1999; 1462: 11-28.
38. HamamotoK, Kida Y, Zhang Yet al. Antimicrobial activityand stability to proteolysis of small linear cationic peptides with D-amino acid substitutions. Microbiol Immunol 2002; 46: 741-9.
39. Rozek A, Powers JP, Friedrich CL et al. Structure-based design of an indolicidin peptide analogue with increased protease stability. Biochemistry 2003; 42: 14130-8.
40. Unger T, Oren Z, Shai Y. The effect of cyclization of magainin 2 and melittin analogues on structure, function, and model membrane interactions: implication to their mode of action. Biochemistry 2001; 40: 6388-97.
41. Freidinger RM. Design and synthesis of novel bioactive peptides and peptidomimetics. J Med Chem 2003; 46: 5553-66.
42. Shin YP, Park HJ, Shin SH et al. Antimicrobial activity of a halocidinderived peptide resistant to attacks by proteases. Antimicrob Agents Chemother 2010; 54: 2855-66.
43. Li Y. Carrier proteins for fusion expression of antimicrobial peptides in Escherichia coli. Biotechnol Appl Biochem 2009; 54: 1-9.
44. Yeung AT, Gellatly SL, Hancock REW. Multifunctional cationic host defense peptides and their clinical applications. Cell Mol Life Sci 2011; 68: 2161-76.
45. Li Y. Recombinant production of antimicrobial peptides in Escherichia coli: a review. Protein Expr Purif 2011; 80: 260-7.
46. Dathe M, Wieprecht T, Nikolenko H et al. Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides. FEBS Lett 1997; 403: 208-12.
47. Wieprecht T, Dathe M, Beyermann M et al. Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes. Biochemistry 1997; 36: 6124-32.
48. Yeaman MR, Yount NY. Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev 2003; 55: 27-55.
49. Chen Y, Mant CT, Farmer SW et al. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. J Biol Chem 2005; 280: 12316-29.
50. White SH, Wimley WC. Hydrophobic interactions of peptides with membrane interfaces. Biochim Biophys Acta 1998; 1376: 339-52.
51. Juretic D, Chen HC, Brown JH et al. Magainin 2 amide and analogues. Antimicrobial activity, membrane depolarization and susceptibility to proteolysis. FEBS Lett 1989; 249: 219-23.
52. Schmidtchen A, Frick IM, Andersson E et al. Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37. Mol Microbiol 2002; 46: 157-68.
53. Dubin G. Extracellular proteases of Staphylococcus spp. BiolChem2002; 383: 1075-86.