Interaction of biologically-relevant peptides with membrane model systems

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dc.contributor.authorBasso, Luis G. Mansor
dc.contributor.authorVicente, Eduardo F.[UNESP]
dc.contributor.authorCilli, Eduardo Maffud [UNESP]
dc.contributor.authorCosta-filho, Antonio José
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2015-05-15T13:30:15Z
dc.date.available2015-05-15T13:30:15Z
dc.date.issued2011
dc.description.abstractIn 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 inserteden
dc.description.affiliationUniversidade Estadual Paulista Júlio de Mesquita Filho, Departamento de Bioquímica e Tecnologia Química, Instituto de Química de Araraquara, Araraquara, Rua Professor Francisco Degni, 55, Jardim Quitandinha, CEP 14800060, SP, Brasil
dc.description.affiliationUnespUniversidade Estadual Paulista Júlio de Mesquita Filho, Departamento de Bioquímica e Tecnologia Química, Instituto de Química de Araraquara, Araraquara, Rua Professor Francisco Degni, 55, Jardim Quitandinha, CEP 14800060, SP, Brasil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.format.extent495a-495a
dc.identifierhttp://www.sciencedirect.com/science/article/pii/S0006349510044061#
dc.identifier.citationBiophysical Journal, v. 100, n. 3, p. 495a, 2011.
dc.identifier.doi10.1016/j.bpj.2010.12.2903
dc.identifier.issn0006-3495
dc.identifier.lattes9424346762460416
dc.identifier.orcid0000-0002-4767-0904
dc.identifier.urihttp://hdl.handle.net/11449/123462
dc.language.isoeng
dc.relation.ispartofBiophysical Journal
dc.relation.ispartofjcr3.495
dc.relation.ispartofsjr1,949
dc.rights.accessRightsAcesso restrito
dc.sourceCurrículo Lattes
dc.titleInteraction of biologically-relevant peptides with membrane model systemsen
dc.typeResumo
unesp.author.lattes9424346762460416
unesp.author.lattes6380599830437803[2]
unesp.author.orcid0000-0002-9154-3574[2]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Química, Araraquarapt
unesp.departmentBioquímica e Tecnologia Químicapt

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