Interaction of biologically-relevant peptides with membrane model systems

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorBasso, Luis G. Mansor
dc.creatorVicente, Eduardo F.
dc.creatorCilli, Eduardo Maffud
dc.creatorCosta-filho, Antonio José
dc.date2015-05-15T13:30:15Z
dc.date2016-10-25T20:48:30Z
dc.date2015-05-15T13:30:15Z
dc.date2016-10-25T20:48:30Z
dc.date2011
dc.date.accessioned2017-04-06T08:16:20Z
dc.date.available2017-04-06T08:16:20Z
dc.identifierBiophysical Journal, v. 100, n. 3, p. 495a, 2011.
dc.identifier0006-3495
dc.identifierhttp://hdl.handle.net/11449/123462
dc.identifierhttp://acervodigital.unesp.br/handle/11449/123462
dc.identifierhttp://dx.doi.org/10.1016/j.bpj.2010.12.2903
dc.identifier0000-0002-4767-0904
dc.identifier9424346762460416
dc.identifierhttp://www.sciencedirect.com/science/article/pii/S0006349510044061#
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/934075
dc.descriptionIn this work, we monitor the alterations caused in membrane model systems upon the addition of biologically-relevant peptides. Our first study reports on the interaction with model membranes of an internal fusion peptide (SARSIFP) from the S2 subunit of the SARS coronavirus spike glycoprotein. It is believed that SARSIFP might be fundamental for the later steps of the fusion between the viral and host cellular membranes. Non-linear least-squares fits of stearic acid spin labels ESR spectra showed that the rotational dynamics of the HPS headgroup region and of the whole carbon chain of SDS surfactants was perturbed by the peptide. Additionally, Tyr fluorescence quenching promoted by spin labels locates this residue in the aqueous interface of HPS and in the hydrophobic core of SDS micelles. The second investigation deals with the conformational changes induced by interactions with model membranes of three TOAC-labeled peptide analogues derived from a new antimicrobial peptide extracted from the skin secretion of the frog Hypsiboas albopunctatus. Our results shed light on how the peptides labeled at positions 0, 2, and 13 interact with DPPC/DPPA/X (X = DPPE, SM, and CL) liposomes and LPC micelles. The findings allowed the description of the peptide topology into the membrane, where the N-terminal region is solvent-exposed, position 2 is at the interface, and position 13 is fully inserted
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.languageeng
dc.relationBiophysical Journal
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.titleInteraction of biologically-relevant peptides with membrane model systems
dc.typeOtro


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