English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/102839
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Exportar a otros formatos:

Title

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
PublisherElsevier
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.
URIhttp://hdl.handle.net/10261/102839
DOIhttp://dx.doi.org/10.1016/j.bbamem.2013.05.036
Identifiersdoi: 10.1016/j.bbamem.2013.05.036
issn: 0005-2736
Appears in Collections:(CFMAC-IEM) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.