Circular Dichroism studies on the interactions of antimicrobial peptides with bacterial cells

Scientific Reports

Volumn 4, Issue , 2014, Pages

  Avitabile, Concetta ^a   D'Andrea, Luca Domenico ^b   Romanelli, Alessandra ^c  

^a Diagnostica e Farmaceutica Molecolari Scarl   (Italy)

^b CNR   (Italy)

^c UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; ANTIMICROBIAL CATIONIC PEPTIDE; CECROPIN A; LIPOPOLYSACCHARIDE; MAGAININ 2 PEPTIDE, XENOPUS; MAGAININ DERIVATIVE; XENOPUS PROTEIN;

ANIMAL; ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; ESCHERICHIA COLI; METABOLISM; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; TIME; XENOPUS LAEVIS;

ANIMALS; ANTI-BACTERIAL AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; CIRCULAR DICHROISM; ESCHERICHIA COLI; LIPOPOLYSACCHARIDES; MAGAININS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; TIME FACTORS; XENOPUS LAEVIS; XENOPUS PROTEINS;

EID: 84896264352     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep04293     Document Type: Article

References (34)

1. Yount, N. Y. & Yeaman, M. R. Emerging themes and therapeutic prospects for anti-infective peptides. Annu Rev Pharmacol Toxicol 52, 337-360, doi:10.1146/ annurev-pharmtox-010611-134535 (2012).
2. Schuerholz, T., Brandenburg, K. & Marx, G. Antimicrobial peptides and their potential application in inflammation and sepsis. Crit Care 16, 207, doi:10.1186/ cc11220 (2012).
3. Zasloff, M. Antimicrobial peptides of multicellular organisms. Nature 415, 389-395, doi:10.1038/415389a (2002). (Pubitemid 34100944)
4. Yang, L., Harroun, T. A., Weiss, T. M., Ding, L. & Huang, H. W. Barrel-stave model or toroidal model? Acase study on melittin pores. Biophys J 81, 1475-1485, doi:10.1016/S0006-3495(01)75802-X (2001). (Pubitemid 32783588)
5. Pouny, Y., Rapaport, D., Mor, A., Nicolas, P. & Shai, Y. Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes. Biochemistry 31, 12416-12423 (1992). (Pubitemid 23163118)
6. Matsuzaki, K., Murase, O., Fujii, N. & Miyajima, K. An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation. Biochemistry 35, 11361-11368, doi:10.1021/bi960016v (1996). (Pubitemid 26299310)
7. Ding, L. et al. Interaction of antimicrobial peptides with lipopolysaccharides. Biochemistry 42, 12251-12259, doi:10.1021/bi0351301 (2003). (Pubitemid 37296502)
8. Bhunia, A., Saravanan, R., Mohanram, H., Mangoni, M. L. & Bhattacharjya, S. NMR structures and interactions of temporin-1Tl and temporin-1Tb with lipopolysaccharide micelles: mechanistic insights into outer membrane permeabilization and synergistic activity. J Biol Chem 286, 24394-24406, doi:10.1074/jbc.M110.189662 (2011).
9. Gesell, J., Zasloff, M. & Opella, S. J. Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution. J Biomol NMR 9, 127-135 (1997). (Pubitemid 127715704)
10. Holak, T. A. et al. The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study. Biochemistry 27, 7620-7629 (1988).
11. Bozzi, A., Mangoni, M. L., Rinaldi, A. C., Mignogna, G. & Aschi, M. Folding propensity and biological activity of peptides: the effect of a single stereochemical isomerization on the conformational properties of bombinins in aqueous solution. Biopolymers 89, 769-778, doi:10.1002/bip.21006 (2008).
12. Avitabile, C. et al. Design, structural and functional characterization of a Temporin-1b analog active against Gram-negative bacteria. Biochim Biophys Acta 1830, 3767-3775, doi:10.1016/j.bbagen.2013.01.026 (2013).
13. Ramamoorthy, A. Beyond NMR spectra of antimicrobial peptides: dynamical images at atomic resolution and functional insights. Solid State Nucl Magn Reson 35, 201-207, doi:10.1016/j.ssnmr.2009.03.003 (2009).
14. Henzler Wildman, K. A., Lee, D. K. & Ramamoorthy, A. Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37. Biochemistry 42, 6545-6558, doi:10.1021/bi0273563 (2003). (Pubitemid 36665830)
15. Porcelli, F. et al. Structure and orientation of pardaxin determined by NMR experiments in model membranes. J Biol Chem 279, 45815-45823, doi:10.1074/ jbc.M405454200 (2004). (Pubitemid 39491574)
16. Hallock, K. J., Lee, D. K. & Ramamoorthy, A. MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain. Biophys J 84, 3052-3060, doi:10.1016/S0006-3495(03) 70031-9 (2003). (Pubitemid 36531755)
17. Silhavy, T. J., Kahne, D. & Walker, S. The bacterial cell envelope. Cold Spring Harb Perspect Biol 2, a000414, doi:10.1101/cshperspect.a000414 (2010).
18. Duong, F., Eichler, J., Price, A., Leonard, M. R. & Wickner, W. Biogenesis of the gram-negative bacterial envelope. Cell 91, 567-573 (1997). (Pubitemid 27513648)
19. Santos, N. C., Silva, A. C., Castanho, M. A., Martins-Silva, J. & Saldanha, C. Evaluation of lipopolysaccharide aggregation by light scattering spectroscopy. Chembiochem 4, 96-100, doi:10.1002/cbic.200390020 (2003). (Pubitemid 36114216)
20. Hancock, R. E.&Chapple, D. S. Peptide antibiotics. Antimicrob Agents Chemother 43, 1317-1323 (1999). (Pubitemid 29259318)
21. Brogden, K. A. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 3, 238-250, doi:10.1038/nrmicro1098 (2005). (Pubitemid 40298223)
22. Gee, M. L. et al. Imaging the action of antimicrobial peptides on living bacterial cells. Sci Rep 3, 1557, doi:10.1038/srep01557 (2013).
23. Silvestro, L. & Axelsen, P. H. Membrane-induced folding of cecropin A. Biophys J 79, 1465-1477, doi:10.1016/S0006-3495(00)76398-3 (2000).
24. Silvestro, L., Weiser, J. N. & Axelsen, P. H. Antibacterial and antimembrane activities of cecropin A in Escherichia coli. Antimicrob Agents Chemother 44, 602-607 (2000). (Pubitemid 30117948)
25. Bechinger, B., Zasloff, M. & Opella, S. J. Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy. Protein Sci 2, 2077-2084, doi:10.1002/pro.5560021208 (1993). (Pubitemid 23354711)
26. Bland, J. M., De Lucca, A. J., Jacks, T. J. & Vigo, C. B. All-D-cecropin B: synthesis, conformation, lipopolysaccharide binding, and antibacterial activity. Mol Cell Biochem 218, 105-111 (2001). (Pubitemid 32294141)
27. Tietze, L. F., Krewer, B.,Major, F. & Schuberth, I. CD-spectroscopy as a powerful tool for investigating the mode of action of unmodified drugs in live cells. J Am Chem Soc 131, 13031-13036, doi:10.1021/ja902767f (2009).
28. Steiner, H., Hultmark, D., Engstrom, A., Bennich, H. & Boman, H. G. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292, 246-248 (1981). (Pubitemid 11001840)
29. Zasloff, M. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc Natl Acad Sci U S A 84, 5449-5453 (1987). (Pubitemid 17129018)
30. Imura, Y., Choda, N. & Matsuzaki, K. Magainin 2 in action: distinct modes of membrane permeabilization in living bacterial andmammalian cells. Biophys J 95, 5757-5765, doi:10.1529/biophysj.108.133488 (2008).
31. Kim, C., Spano, J., Park, E. K. & Wi, S. Evidence of pores and thinned lipid bilayers induced in oriented lipid membranes interacting with the antimicrobial peptides, magainin-2 and aurein-3.3. Biochim Biophys Acta 1788, 1482-1496, doi:10.1016/ j.bbamem.2009.04.017 (2009).
32. Matsuzaki, K., Sugishita, K., Harada, M., Fujii, N. & Miyajima, K. Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gramnegative bacteria. Biochim Biophys Acta 1327, 119-130 (1997). (Pubitemid 27283405)
33. Christensen, B., Fink, J., Merrifield, R. B. & Mauzerall, D. Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. Proc Natl Acad Sci U S A 85, 5072-5076, (1988).
34. Hong, R. W., Shchepetov, M., Weiser, J. N. & Axelsen, P. H. Transcriptional profile of the Escherichia coli response to the antimicrobial insect peptide cecropin A. Antimicrob Agents Chemother 47, 1-6 (2003). (Pubitemid 36070334)