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Bacteriocin AS-48 binding to model membranes and pore formation as revealed by coarse-grained simulations

AuthorsCruz, Víctor L. ; Ramos, Javier ; Melo, Manuel N.; Martínez-Salazar, Javier
Issue Date2013
CitationBiochimica et Biophysica Acta - Biomembranes 1828: 2524- 2531 (2013)
AbstractBacteriocin AS-48 is a membrane-interacting peptide that acts as a broad-spectrum antimicrobial against Gram-positive and Gram-negative bacteria. Prior Nuclear Magnetic Resonance experiments and the high resolution crystal structure of AS-48 have suggested a mechanism for the molecular activity of AS-48 whereby the peptide undergoes transition from a water-soluble to a membrane-bound state upon membrane binding. To help interpret experimental results, we here simulate the molecular dynamics of this binding mechanism at the coarse-grained level. By simulating the self-assembly of the peptide, we predict induction by the bacteriocin of different pore types consistent with a >leaky slit> model. © 2013 Elsevier B.V.
Identifiersdoi: 10.1016/j.bbamem.2013.05.036
issn: 0005-2736
Appears in Collections:(CFMAC-IEM) Artículos
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