INV SUPERIOR JUBILADO
CASCONE Osvaldo
artículos
Título:
Structural glance into a novel anti-staphylococcal peptide
Autor/es:
IANNUCCI, NANCY BEATRIZ; CURTO, LUCRECIA M; ALBERICIO, FERNANDO; CASCONE, OSVALDO; DELFINO, JOSÉ MARÍA
Revista:
Biopolymers: Peptide Science
Editorial:
WILEY-V C H VERLAG GMBH
Referencias:
Año: 2013 vol. 102 p. 49 - 57
ISSN:
1097-0282
Resumen:
Novel antimicrobial peptides are valuable molecules for developing anti-infective drugs to counteract the microbial resistance spread. We have previously reported a novel peptide derived from the 107-115 human lysozyme fragment which displays 20-fold increased anti-staphylococcal activity. This peptide interacts distinctively with synthetic membranes composed by staphylococcal-isolated lipids and saturated phosphatidylcholines and posphatidylethanolamines. The conformational analysis of the peptide - assayed by circular dicroism - shows a notorious correlation between induced α-helicity and anti-staphylococcal activity. This result highlights the role of the peptide?s secondary structure in the interaction with the bacterial plasma membrane to trigger its lethal effect. This knowledge may contribute to the rational design of a new generation of AMPs with increased effectiveness
