Structure-activity relationships of cecropin-like peptides and their interactions with phospholipid membrane
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Cecropin A and papiliocin are novel 37-residue cecropin-like antimicrobial peptides isolated from insect. We have confirmed that papiliocin possess high bacterial cell selectivity and has an α-helical structure from Lys3 to Lys21 and from Ala25 to Val35,linked by a hinge region. In this study, we demonstrated that both peptides showed high antimicrobial activities against multi-drug resistant Gram negative bacteria as well as fungi. Interactions between these cecropin-like peptides and phospholipid membrane were studied using CD, dye leakage experiments, and NMR experiments, showing that both peptides have strong permeabilizing activities against bacterial cell membranes and fungal membranes as well as Trp2 and Phe5 at the N-terminal helix play an important role in attracting cecropin-like peptides to the negatively charged bacterial cell membrane. Cecropin-like peptides can be potent peptide antibiotics against multi-drug resistant Gram negative bacteria and fungi.
Abstract
Cecropin A and papiliocin are novel 37-residue cecropin-like antimicrobial peptides isolated from insect. We have confirmed that papiliocin possess high bacterial cell selectivity and has an α-helical structure from Lys3 to Lys21 and from Ala25 to Val35,linked by a hinge region. In this study, we demonstrated that both peptides showed high antimicrobial activities against multi-drug resistant Gram negative bacteria as well as fungi. Interactions between these cecropin-like peptides and phospholipid membrane were studied using CD, dye leakage experiments, and NMR experiments, showing that both peptides have strong permeabilizing activities against bacterial cell membranes and fungal membranes as well as Trp2 and Phe5 at the N-terminal helix play an important role in attracting cecropin-like peptides to the negatively charged bacterial cell membrane. Cecropin-like peptides can be potent peptide antibiotics against multi-drug resistant Gram negative bacteria and fungi.
참고문헌 (22)
- Hancock, R. E., "Cationic peptides: a new source of antibiotics", Trends Biotechnol, 16, pp.82~88 (1998)
- Otvos, L. Jr., "Antibacterial peptides isolated from insects", J. Pept. Sci, 6, pp.497~511 (2000)
- Dimarcq, J. L., "Cysteine-rich antimicrobial peptides in invertebrates", Biopolymers, 47, pp.465~477 (1998)
- Yeaman, M. R, "Mechanisms of antimicrobial peptide action and resistance", Pharmacol. Rev, 55, pp.27~55 (2003)
- Broqden, K. A., "Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?", Nat. Rev. Microbiol, 3, pp.238~250 (2005)
- Bulet, P., "Antimicrobial peptides in insects: structure and function", Dev. Comp. Immunol, 23, pp.329~344 (1999)
- Boman, H. G., "Cell-free immunity in insects. Cell-free immunity in insects", Annu. Rev. Microbiol, 41, pp.103~126 (1987)
- Morishima, I., "Isolation and structure of cecropins, inducible antibacterial peptides, from the silkworm, Bombyx mori", Comp. Biochem. Physiol, 95, pp.551~554 (1990)
- Kylsten, P., "The cecropin locus in Drosophila; a compact gene cluster involved in the response to infection", EMBO J, 9, pp.217~224 (1990)
- Liang, Y., "Molecular cloning and characterization of cecropin from the housefly (Musca domestica) and its expression in Escherichia coli", Dev. Comp. Immunol, 30, pp.249~257 (2006)
- Saito, A., "Purification and cDNA cloning of a cecropin from the longicorn beetle, Acalolepta luxuriosa", Comp. Biochem. Physiol. B. Biochem. Mol. Biol, 142, pp.317~323 (2005)
- Li, W., "Characterization and expression of a cecropin-like gene from Helicoverpa armigera", Comp. Biochem. Physiol. B. Biochem. Mol. Biol, 148, pp.417~425 (2007)
- Seong Ryul Kim, "Characterization and cDNA Cloning of a Cecropin-Like Antimicrobial Peptide, Papiliocin, from the Swallowtail Butterfly, Papilio xuthus", Molecules and Cells, 29(4), pp.419~423 (2010), 한국분자세포생물학회
- Kim, J. K., "Structure and function of papiliocin with antimicrobial and anti-inflammatory activities isolated from the Swallowtail Butterfly, Papilio xuthus", J. Biol. Chem, 285, pp.3883~3895 (2011)
- Boman, H. G., "On the primary structures of lysozyme, cecropins and attacins from Hyalophora cecropia", Dev. Comp. Immunol, 9, pp.551~558 (1985)
- Pliška, V., "Partition coefficients of amino acids and hydrophobic parameters π of their side-chains as measured by thin-layer chromatography", J. Chromatography A, 216, pp.79~92 (1981)
- Holak, T. A., "The solution conformation of the antibacterial peptide cecropin A: a nuclear magnetic resonance and dynamical simulated annealing study", Biochemistry, 27, pp.7620~7629 (1998)
- Kauffman, C. A., "Fungal infections", Proc. Am. Thorac. Soc, 3, pp.35~40 (2006)
- Ashbee, R. H., "Malassezia. In Pathogenic Yeasts", pp.209~230 (2010), Springer Verlag Heidelberg
- Cole, A. M., "Characterization of a fish antimicrobial peptide: Gene expression, subcellular localization and spectrum of activity", Antimicrob. Agents Chemother, 44, pp.2039~2045 (2000)
- Gennis, R. B., "In Biomembranes: Molecular Structure and Function", pp.155~156 (1989), Springer-Verlag New York Inc
- Scudiero, D. A., "Evaluation of a soluble tetrazolium", formazan assay for cell growth and drug sensitivity in culture using human and other tumor cell lines, 1988, pp.48, 4827~4833
