De novo generation of antimicrobial LK peptides with a single tryptophan at the critical amphipathic interface

Journal of Peptide Science

Volumn 15, Issue 9, 2009, Pages 583-588

  Kang, Su Jin ^a   Won, Hyung Sik ^b   Choi, Wahn Soo ^b   Lee, Bong Jin ^a  

^a Seoul National University   (South Korea)

^b Konkuk University   (South Korea)

Author keywords

Amphipathic helix; Antimicrobial peptides; Critical amphipathic interface; De novo design; LK peptides; Tryptophan

Indexed keywords

LEUCYLLEUCYLLYSYLLEUCYLLEUCYLLYSYLTRYPTOPHANYLLEUCYLLEUCYLLYSLLEUCYLLEUCYLLYSINAMIDE; LEUCYLLEUCYLLYSYLTRYPTOPHANYLLEUCYLLEUCYLLYSINAMIDE; LEUCYLLEUCYLLYSYLTRYPTOPHANYLLEUCYLLYSYLLYSINAMIDE; LEUCYLLEUCYLLYSYLTRYPTOPHANYLLEUCYLLYSYLLYYLLEUCINAMIDE; LEUCYLLYSYLLEUCYLLEUCYLLYSYLTRYPTOPHANYLLEUCYLLEUCYLLYSLLEUCYLLEUCINAMIDE; LEUCYLLYSYLLYSYLLEUCYLLEUCYLLYSYLTRYPTOPHANYLLEUCYLLEUCYLLYSLLEUCYLLEUCYLLYSINAMIDE; LEUCYLLYSYLLYSYLTRYPTOPHANYLLEUCYLLYSINAMIDE; LEUCYLLYSYLLYSYLTRYPTOPHANYLLEUCYLLYSYLLYSINAMIDE; LYSYLLEUCYLLEUCYLLYSYLTRYPTOPHANYLLEUCYLLEUCYLLYSINAMIDE; LYSYLLEUCYLLEUCYLLYSYLTRYPTOPHANYLLEUCYLLEUCYLLYSLLEUCINAMIDE; LYSYLLYSYLLEUCYLLEUCYLLYSYLTRYPTOPHANYLLEUCYLLEUCYLLYSLLEUCYLLEUCINAMIDE; LYSYLLYSYLLEUCYLLEUCYLLYSYLTRYPTOPHANYLLEUCYLLYSYLLYSLLEUCYLLEUCINAMIDE; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

AMINO ACID COMPOSITION; AMINO ACID SEQUENCE; ANTIMICROBIAL ACTIVITY; BACTERIAL STRAIN; CONCENTRATION RESPONSE; CONFERENCE PAPER; CONTROLLED STUDY; DRUG DESIGN; DRUG STRUCTURE; GRAM NEGATIVE BACTERIUM; GRAM POSITIVE BACTERIUM; HYDROPHOBICITY; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANTIMICROBIAL CATIONIC PEPTIDES; CIRCULAR DICHROISM; GRAM-NEGATIVE BACTERIA; GRAM-POSITIVE BACTERIA; HEMOLYSIS; HUMANS; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; STRUCTURE-ACTIVITY RELATIONSHIP; TRYPTOPHAN;

BACTERIA (MICROORGANISMS); NEGIBACTERIA; POSIBACTERIA;

EID: 70349637842     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1149     Document Type: Conference Paper

References (35)

1. Zaiou M. Multifunctional antimicrobial peptides: therapeutic targets in several human diseases. J. Mol. Med. 2007; 85: 317-329.
2. Koczulla AR, Bals R. Antimicrobial peptides: current status and therapeutic potential. Drugs 2003; 63: 389-406.
3. Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002; 415: 389-395.
4. Hancock REW, Scott MG. The role of antimicrobial peptides in animal defenses. Proc. Natl. Acad. Sci. 2000; 97: 8856-8861.
5. Jenssen H, Hamill P, Hancock REW. Peptide antimicrobial agents. Clin. Microbiol. Rev. 2006; 19: 491-511.
6. Yeaman MR, Yount NY. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 2003; 55: 27-55.
7. Won HS, Jung SJ, Kim HE, Seo MD, Lee BJ. Systematic peptide engineering and structural characterization to search for the shortest antimicrobial peptide analogue of gaegurin 5. J. Biol. Chem. 2004; 279: 14784-14791.
8. Zelezetsky I, Tossi A. Alpha-helical antimicrobial peptides-using a sequence template to guide structure-activity relationships studies. Biochim. Biophys. Acta 2006; 1758: 1436-1449.
9. Tossi A, Sandri L, Giangaspero A. Amphipathic, a-helical antimicrobial peptides. Biopolymers 2000; 55: 4-30.
10. Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by a-helical antimicrobial and cell non-selectivemembrane-lytic peptides. Biochim. Biophys. Acta 1999; 1462: 55-70.
11. Oren Z, Shai Y. Mode of action of linear amphipathic a-helical antimicrobial peptides. Biopolymers 1998; 47: 451-463.
12. Chou PY, Fasman GD. Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins. Biochemistry 1974; 13: 211-222.
13. Blondelle SE, Houghten RA. Design of model amphipathic peptides having potent antimicrobial activities. Biochemistry 1992; 31: 12688-12694.
14. Béven L, Castano S, Dufourcq J, Wieslander Å, Wróblewski H. The antibiotic activity of cationic linear amphipathic peptides: lessons from the action of leucine/lysine copolymers on bacteria of the class Mollicutes. Eur. J. Biochem. 2003; 270: 2207-2217.
15. Won HS, Park SH, Kim HE, Hyun B, Kim M, Lee BJ, Lee BJ. Effects of a tryptophanyl substitution on the structure and antimicrobial activity of C-terminally truncated gaegurin 4. Eur. J. Biochem. 2002; 269: 4367-4374.
16. Won HS, Seo MD, Jung SJ, Lee SJ, Kang SJ, Son WS, Kim HJ, Park TK, Park SJ, Lee BJ. Structural determinants for the membrane interaction of novel bioactive undecapeptides derived from gaegurin 5. J. Med. Chem. 2006; 49: 4886-4895.
17. Oh D, Shin SY, Lee S, Kang JH, Kim SD, Ryu PD, Hahm KS, Kim Y. Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-Magainin 2(1-12) and its analogues, on their antibiotic activities and structures. Biochemistry 2000; 39: 11855-11964.
18. Park K, Oh D, Shin SY, Hahm KS, Kim Y. Structural studies of porcine myeloid antibacterial peptide PMAP-23 and its analogues in DPC micelles by NMR spectroscopy. Biochem. Biophys. Res. Commun. 2002; 290: 204-212.
19. Ridder ANJA, Morein S, Stam JG, Kuhn A, de Kruijff B, Killian JA. Analysis of the role of interfacial tryptophan residues in controlling the topology of membrane proteins. Biochemistry 2000; 39: 6521-6528.
20. Hu W, Lee KC, Cross TA. Tryptophans in membrane proteins: indole ring orientations and functional implications in the gramicidin channel. Biochemistry 1993; 32: 7035-7047.
21. Epand RM, Vogel HJ. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1999; 1462: 11-28.
22. Sitaram N. Antimicrobial peptides with unusual amino acid compositions and unusual structures. Curr. Med. Chem. 2006; 13: 679-696.
23. Won HS, Kang SJ, Lee BJ. Action mechanism and structural requirements of the antimicrobial peptides, gaegurins. Biochim. Biophys. Acta 2008; (in press). DOI: 10.1016/j.bbamem.2008.10.021.
24. Park SH, Kim HE, Kim CM, Yun HJ, Choi EC, Lee BJ. Role of proline, cysteine and a disulphide bridge in the structure and activity of the anti-microbial peptide gaegurin 5. Biochem. J. 2002; 368: 171-182.
25. Avrahami D, Oren Z, Shai Y. Effect of multiple aliphatic amino acids substitutions on the structure, function, and mode of action of diastereomeric membrane active peptides. Biochemistry 2001; 40: 12591-12603.
26. Shin SY, HahmKS. A short a-helical antimicrobial peptide with antibacterial selectivity. Biotechnol. Lett. 2004; 26: 735-739.
27. Oren Z, Ramesh J, Avrahami D, Suryaprakash N, Shai Y, Jelinek R. Structures and mode of membrane interaction of a short a helical lytic peptide and its diastereomer determined by NMR, FTIR, and fluorescence spectroscopy. Eur. J. Biochem. 2002; 269: 3869-3880.
28. Deslouches B, Phadke SM, Lazarevic V, Cascio M, Islam K, Montelaro RC, Mietzner TA. De novo generation of cationic antimicrobial peptides: influence of length and tryptophan substitution on antimicrobial activity. Antimicrob. Agents Chemother. 2005; 49: 316-322.
29. Jin Y, Hammer J, Pate M, Zhang Y, Zhu F, Zmuda E, Blazyk J. Antimicrobial activities and structures of two linear cationic peptide families with various amphipathic β-sheet and a-helical potentials. Antimicrob. Agents Chemother. 2005; 49: 4957-4964.
30. Jin Y, Mozsolits H, Hammer J, Zmuda E, Zhu F, Zhang Y, Aguilar MI, Blazyk J. Influence of tryptophan on lipid binding of lenear amphipathic cationic antimicrobial peptides. Biochemistry 2003; 42: 9395-9405.
31. Dathe M, Wieprecht T, Nikolenko H, Handel L, Maloy WL, MacDonald DL, Beyermann M, Bienert M. Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides. FEBS Lett. 1997; 403: 208-212.
32. Mee RP, Auton TR, Morgan PJ. Design of active analogues of a 15-residue peptide using D-optimal design, QSAR and a combinatorial search algorithm. J. Pept. Res. 1997; 49: 89-102.
33. Bessalle R, Gorea A, Shalit I, Metzger JW, Dass C, Desiderio DM, Fridkin M. Structure-function studies of amphiphilic antibacterial peptides. J. Med. Chem. 1993; 36: 1203-1209.
34. Chia CSB, Torres J, Cooper MA, Arkin IT, Bowie JH. The orientation of the antibiotic peptide maculatin 1.1 in DMPG and DMPC lipid bilayers. Support for a pore-forming mechanism. FEBS Lett. 2002; 512: 47-51.
35. Shai Y, Oren Z. From "carpet" mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides. Peptides 2001; 22: 1629-1641.