Interaction of the antimicrobial peptide melimine with bacterial membranes

International Journal of Antimicrobial Agents

Volumn 35, Issue 6, 2010, Pages 566-572

  Rasul, R ^a   Cole, N ^a,b   Balasubramanian, D ^c   Chen, R ^a   Kumar, N ^a   Willcox, M D P ^a,b  

^a UNIVERSITY OF NEW SOUTH WALES   (Australia)

^b VISION COOPERATIVE RESEARCH CENTRE   (Australia)

^c L V PRASAD EYE INSTITUTE   (India)

Author keywords

Cationic antimicrobial peptide; Pseudomonas aeruginosa; Staphylococcus aureus

Indexed keywords

ANTIMICROBIAL CATIONIC PEPTIDE; DODECYL SULFATE SODIUM; MELIMINE; ORGANIC SOLVENT; SOLVENT; UNCLASSIFIED DRUG;

ANTIMICROBIAL ACTIVITY; ARTICLE; BACTERIAL CELL; BACTERIAL INFECTION; BACTERIAL MEMBRANE; CELL MEMBRANE; CELL VIABILITY; CIRCULAR DICHROISM; CONTROLLED STUDY; DRUG CONFORMATION; FLUORESCENCE MICROSCOPY; FLUORESCENCE SPECTROSCOPY; GRAM NEGATIVE BACTERIUM; GRAM POSITIVE BACTERIUM; MICELLIZATION; NONHUMAN; PRIORITY JOURNAL; PSEUDOMONAS AERUGINOSA; SCANNING ELECTRON MICROSCOPY; SOLUBILIZATION; STAPHYLOCOCCUS AUREUS;

ANTIMICROBIAL CATIONIC PEPTIDES; CELL MEMBRANE; CIRCULAR DICHROISM; FLUORESCENT DYES; MICROBIAL VIABILITY; MICROSCOPY, ELECTRON, SCANNING; MICROSCOPY, FLUORESCENCE; PSEUDOMONAS AERUGINOSA; SPECTROMETRY, FLUORESCENCE; STAPHYLOCOCCUS AUREUS;

EID: 77951768593     PISSN: 09248579     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijantimicag.2010.02.005     Document Type: Article

References (33)

1. Henderson DK, Levy SB, editors. Resistant organisms: global impact on continuum of care. International Congress and Symposium Series #220. New York, NY: Royal Society of Medicine; 1997.
2. Marra A.R., Pereira C.A., Gales A.C., Menezes L.C., Cal R.G., de Souza J.M., et al. Bloodstream infections with metallo-β-lactamase-producing Pseudomonas aeruginosa: epidemiology, microbiology, and clinical outcomes. Antimicrob Agents Chemother 2006, 50:388-390.
3. Panlilio A.L., Culver D.H., Gaynes R.P., Banerjee S., Henderson T.S., Tolson J.S., et al. Methicillin-resistant Staphylococcus aureus in U.S. hospitals, 1975-1991. Infect Control Hosp Epidemiol 1992, 13:582-586.
4. Gordon Y.J., Romanowski E.G., McDermott A.M. A review of antimicrobial peptides and their therapeutic potential as anti-infective drugs. Curr Eye Res 2005, 30:505-515.
5. Wang Z., Wang G. APD: the Antimicrobial Peptide Database. Nucleic Acids Res 2004, 32:D590-D592.
6. Zhang L., Rozek A., Hancock R.E. Interaction of cationic antimicrobial peptides with model membranes. J Biol Chem 2001, 276:35714-35722.
7. Jenssen H., Hamill P., Hancock R.E. Peptide antimicrobial agents. Clin Microbiol Rev 2006, 19:491-511.
8. Willcox M.D., Hume E.B., Aliwarga Y., Kumar N., Cole N. A novel cationic-peptide coating for the prevention of microbial colonization on contact lenses. J Appl Microbiol 2008, 105:1817-1825.
9. Chen R., Cole N., Willcox M.D., Park J., Rasul R., Carter E., et al. Synthesis, characterization and in vitro activity of a surface-attached antimicrobial cationic peptide. Biofouling 2009, 25:517-524.
10. Lam Y.H., Wassall S.R., Morton C.J., Smith R., Separovic F. Solid-state NMR structure determination of melittin in a lipid environment. Biophys J 2001, 81:2752-2761.
11. Matsuzaki K., Sugishita K., Harada M., Fujii N., Miyajima K. Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria. Biochim Biophys Acta 1997, 1327:119-130.
12. Kempf C., Klausner R.D., Weinstein J.N., Van Renswoude J., Pincus M., Blumenthal R. Voltage-dependent trans-bilayer orientation of melittin. J Biol Chem 1982, 257:2469-2476.
13. Mousli M., Bueb J.L., Bronner C., Rouot B., Landry Y. G protein activation: a receptor-independent mode of action for cationic amphiphilic neuropeptides and venom peptides. Trends Pharmacol Sci 1990, 11:358-362.
14. Ebert G., Zolzer U., Nishi N. Solubilization and conformation of protamines in reverse micelles. Prog Colloid Polym Sci 1990, 83:181-187.
15. Aspedon A., Groisman E.A. The antibacterial action of protamine: evidence for disruption of cytoplasmic membrane energization in Salmonella typhimurium. Microbiology 1996, 142:3389-3397.
16. Abrunhosa F., Faria S., Gomes P., Tomaz I., Pessoa J.C., Andreu D., et al. Interaction and lipid-induced conformation of two cecropin-melittin hybrid peptides depend on peptide and membrane composition. J Phys Chem B 2005, 109:17311-17319.
17. Ruhr E., Sahl H.G. Mode of action of the peptide antibiotic nisin and influence on the membrane potential of whole cells and on cytoplasmic and artificial membrane vesicles. Antimicrob Agents Chemother 1985, 27:841-845.
18. Friedrich C.L., Moyles D., Beveridge T.J., Hancock R.E. Antibacterial action of structurally diverse cationic peptides on Gram-positive bacteria. Antimicrob Agents Chemother 2000, 44:2086-2092.
19. Turner J., Cho Y., Dinh N.N., Waring A.J., Lehrer R.I. Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils. Antimicrob Agents Chemother 1998, 42:2206-2214.
20. Bucki R., Pastore J.J., Randhawa P., Vegners R., Weiner D.J., Janmey P.A. Antibacterial activities of rhodamine B-conjugated gelsolin-derived peptides compared to those of the antimicrobial peptides cathelicidin LL37, magainin II, and melittin. Antimicrob Agents Chemother 2004, 48:1526-1533.
21. Friedrich C., Scott M.G., Karunaratne N., Yan H., Hancock R.E. Salt-resistant α-helical cationic antimicrobial peptides. Antimicrob Agents Chemother 1999, 43:1542-1548.
22. Bengoechea J.A., Diaz R., Moriyon I. Outer membrane differences between pathogenic and environmental Yersinia enterocolitica biogroups probed with hydrophobic permeants and polycationic peptides. Infect Immun 1996, 64:4891-4899.
23. Wu M., Maier E., Benz R., Hancock R.E. Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli. Biochemistry 1999, 38:7235-7242.
24. Rifkind J.M. Helix-coil transition of poly-l-arginine: a comparison with other basic polypeptides. Biopolymers 1969, 8:685-688.
25. Vaara M. Agents that increase the permeability of the outer membrane. Microbiol Rev 1992, 56:395-411.
26. Lee K.H., Fitton J.E., Wuthrich K. Nuclear magnetic resonance investigation of the conformation of δ-haemolysin bound to dodecylphosphocholine micelles. Biochim Biophys Acta 1987, 911:144-153.
27. Orlando J.S., Ornelles D.A. An arginine-faced amphipathic α helix is required for adenovirus type 5 E4orf6 protein function. J Virol 1999, 73:4600-4610.
28. Raghuraman H., Chattopadhyay A. Interaction of melittin with membrane cholesterol: a fluorescence approach. Biophys J 2004, 87:2419-2432.
29. Verdon J., Girardin N., Lacombe C., Berjeaud J.M., Hechard Y. δ-Hemolysin, an update on a membrane-interacting peptide. Peptides 2009, 30:817-823.
30. Groisman E.A. Bacterial responses to host-defense peptides. Trends Microbiol 1996, 4:127-128. [discussion 128-9].
31. Zhang L., Dhillon P., Yan H., Farmer S., Hancock R.E. Interactions of bacterial cationic peptide antibiotics with outer and cytoplasmic membranes of Pseudomonas aeruginosa. Antimicrob Agents Chemother 2000, 44:3317-3321.
32. Jia Z. Protein phosphatases: structures and implications. Biochem Cell Biol 1997, 75:17-26.
33. Taubes G. The bacteria fight back. Science 2008, 321:356-361.