Different modes of antibiotic action of homodimeric and monomeric bactenecin, a cathelicidin-derived antibacterial peptide

BMB Reports

Volumn 42, Issue 9, 2009, Pages 586-592

  Lee, Ju Yeon ^a   Yang, Sung Tae ^a,b   Kim, Hyo Jeong ^a   Lee, Seung Kyu ^a   Jung, Hyun Ho ^a   Shin, Song Yub ^c   Kim, Jae Il ^d  

^a Gwangju Institute of Science and Technology (GIST)   (South Korea)

^b EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

^c School of Medicine   (South Korea)

^d AnyGen Corporation   (South Korea)

Author keywords

Antibacterial activity; Homodimeric bactenecin; Model membrane; Monomeric bactenecin; Oligomerization

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; STAPHYLOCOCCUS AUREUS;

ACRYLAMIDE; ANTIINFECTIVE AGENT; BACTENECIN; CYCLOPEPTIDE; LIPOSOME; PEPTIDE FRAGMENT; SODIUM CHLORIDE; TRYPTOPHAN;

ARTICLE; CELL MEMBRANE; CHEMISTRY; DIMERIZATION; DRUG EFFECT; ESCHERICHIA COLI; FLUORESCENCE; GROWTH, DEVELOPMENT AND AGING; KINETICS; LIPID BILAYER; STAPHYLOCOCCUS AUREUS;

ACRYLAMIDE; ANTI-INFECTIVE AGENTS; CELL MEMBRANE; DIMERIZATION; ESCHERICHIA COLI; FLUORESCENCE; KINETICS; LIPID BILAYERS; LIPOSOMES; PEPTIDE FRAGMENTS; PEPTIDES, CYCLIC; SODIUM CHLORIDE; STAPHYLOCOCCUS AUREUS; TRYPTOPHAN;

EID: 70449719332     PISSN: 19766696     EISSN: 1976670X     Source Type: Journal    
DOI: 10.5483/BMBRep.2009.42.9.586     Document Type: Article

References (26)

1. Zasloff, M. (2002) Antimicrobial peptides of multicellular organisms. Nature 415, 389-395.
2. Andreu, D. and Rivas, L. (1998) Animal antimicrobial peptides: an overview. Biopolymers 47, 415-433.
3. Koczulla, A. R. and Bals, R. (2003) Antimicrobial peptides: current status and therapeutic potential. Drugs 63, 389-406.
4. Matsuzaki, K. (2008) Control of cell selectivity of antimicrobial peptides. Biochim. Biophys. Acta (in press).
5. Brogden, K. A. (2005) Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3, 238-250.
6. Yeaman, M. R. and Yount, N. Y. (2003) Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 55, 27-55.
7. Papo, N. and Shai, Y. (2003) Can we predict biological activity of antimicrobial peptides from their interactions with model phospholipid membranes? Peptides 24, 1693-1703.
8. Shai, Y. (2002) Mode of action of membrane active antimicrobial peptides. Biopolymers 66, 236-248.
9. Cudic, M. and Otvos, L. Jr. (2002) Intracellular targets of antibacterial peptides. Curr. Drug Targets 3, 101-106.
10. Yang, S. T., Shin, S. Y., Hahm, K. S. and Kim, J. I. (2006) Different modes in antibiotic action of tritrpticin analogs, cathelicidin-derived Trp-rich and Pro/Arg-rich peptides. Biochim. Biophys. Acta 1758, 1580-1586.
11. Podda, E., Benincasa, M., Pacor, S., Micali, F., Mattiuzzo, M., Gennaro, R. and Scocchi, M. (2006) Dual mode of action of Bac7, a proline-rich antibacterial peptide. Biochim. Biophys. Acta 1760, 1732-1740.
12. Romeo, D., Skerlavaj, B., Bolognesi, M. and Gennaro, R. (1988) Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils. J .Biol. Chem. 263, 9573-9575.
13. Wu, M. and Hancock, R. E. W. (1999) Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane. J. Biol. Chem. 274, 29-35.
14. Gennaro, R., Skerlavaj, B. and Romeo, D. (1989) Purification, composition, and activity of two bactenecins, antibacterial peptides of bovine neutrophils. Infect. Immun. 57, 3142-3146.
15. Wu, M. and Hancock, R. E. W. (1999) Improved derivatives of bactenecin, a cyclic dodecameric antimicrobial cationic peptide. Antimicrob. Agents Chemother. 43, 1274-1276.
16. Storici, P., Tossi, A., Lenarcic, B. and Romeo, D. (1996) Purification and structural characterization of bovine cathelicidins, precursors of antimicrobial peptides. Eur. J. Biochem. 238, 769-776.
17. Lee, J. Y., Yang, S. T., Lee, S. K., Jung, H. H., Shin, S. Y., Hahm, K. S. and Kim, J. I. (2008) Salt-resistant homodimeric bactenecin, a cathelicidin-derived antimicrobial peptide. FEBS J. 275, 3911-3920.
18. Wu, M., Maier, E., Benz, R. and Hancock, R. E. W. (1999) Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli. Biochemistry 38, 7235-7242.
19. Lakoxicz, J. R. (1999) Principles of Fluorescence Spectroscopy, 2nd ed., Kluwer Academic/Plenum, New York, USA.
20. Zelezetsky, I., Pontillo, A., Puzzi, L., Antcheva, N., Segat, L., Pacor, S., Crovella, S. and Tossi, A. (2006) Evolution of the primate cathelicidin. Correlation between structural variations and antimicrobial activity. J. Biol. Chem. 281, 19861-19871.
21. Breukink, E., van Kraaij, C., van Dalen, A., Demel, R. A., Siezen, R. J., de Kruijff, B. and Kuipers, O. P. (1998) The orientation of nisin in membranes. Biochemistry 37, 8153-8162.
22. Zhao, H. and Kinnunen, P. K. (2002) Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence. J. Biol. Chem. 277, 25170-25177.
23. Christiaens, B., Symoens, S., Verheyden, S., Engelborghs, Y., Joliot, A., Prochiantz, A., Vandekerckhove, J., Rosseneu, M. and Vanloo, B. (2002) Tryptophan fluorescence study of the interaction of penetratin peptides with model membranes. Eur. J. Biochem. 269, 2918-2926.
24. Zhu, W. L. and Shin, S. Y. (2009) Effects of dimerization of the cell-penetrating peptide Tat analog on antimicrobial activity and mechanism of bactericidal action. J. Pept. Sci. 15, 345-352.
25. Zhu, W. L. and Shin, S. Y. (2009) Antimicrobial and cytolytic activities and plausible mode of bactericidal action of the cell penetrating peptide penetratin and its lys-linked two-stranded peptide. Chem. Biol. Drug Des. 73, 209-215.
26. Szoka, F. Jr. and Papahadjopoulos, D. (1978) Procedure for preparation of liposomes with large internal aqueous space and high capture by reverse-phase evaporation. Proc. Natl. Acad. Sci. U.S.A. 75, 4194-4198.