Headgroup specificity for the interaction of the antimicrobial peptide tritrpticin with phospholipid Langmuir monolayers

Página do item simplificado
dc.contributor.authorSalay, Luiz C.
dc.contributor.authorFerreira, Marystela
dc.contributor.authorOliveira, Osvaldo N.
dc.contributor.authorNakaie, Clovis R. [UNIFESP]
dc.contributor.authorSchreier, Shirley
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de São Carlos (UFSCar)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T14:28:05Z
dc.date.available2016-01-24T14:28:05Z
dc.date.issued2012-12-01
dc.description.abstractWe examined the interaction of the cationic antimicrobial peptide (AMP) tritrpticin (VRRFPWWWPFLRR, TRP3) with Langmuir monolayers of zwitterionic (dipalmitoyl phosphatidylcholine, DPPC, and dipalmitoyl phosphatidylethanolamine, DPPE) and negatively charged phospholipids (dipalmitoyl phosphatidic acid, DPPA, and dipalmitoyl phosphatidylglycerol, DPPG). Both surface pressure and surface potential isotherms became more expanded upon addition of TRP3 (DPPE similar to DPPC << DPPA < DPPG). the stronger interaction with negatively charged phospholipids agrees with data for vesicles and planar lipid bilayers, and with AMPs greater activity against bacterial membranes versus mammalian cell membranes. Considerable expansion of negatively charged monolayers occurred at 10 and 30 mol% TRP3, especially at low surface pressure. Moreover, a difference was observed between PA and PG, demonstrating that the interaction, besides being modulated by electrostatic interactions, displays specificity with regard to headgroup, being more pronounced in the case of PG, present in large quantities in bacterial membranes. in previous studies, it was proposed that the peptide acts by a toroidal pore-like mechanism [1,2]. Considering the evidence from the literature that PG shows a propensity to form a positive curvature as do toroidal pores, the observation of TRP3's preference for the PG headgroup and the dramatic increase in area promoted by this interaction represent further support for the toroidal pore mechanism of action proposed for TRP3. (C) 2012 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniv São Paulo, Inst Chem, Dept Biochem, BR-05513970 São Paulo, Brazil
dc.description.affiliationUniv Fed Sao Carlos, BR-18052780 Sorocaba, SP, Brazil
dc.description.affiliationUniv São Paulo, Inst Phys, BR-13560970 Sao Carlos, SP, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipRede Biomat (Brazil)
dc.format.extent95-102
dc.identifierhttp://dx.doi.org/10.1016/j.colsurfb.2012.05.002
dc.identifier.citationColloids and Surfaces B-biointerfaces. Amsterdam: Elsevier B.V., v. 100, p. 95-102, 2012.
dc.identifier.doi10.1016/j.colsurfb.2012.05.002
dc.identifier.issn0927-7765
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/35557
dc.identifier.wosWOS:000307683900014
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofColloids and Surfaces B-biointerfaces
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectTritrpticinen
dc.subjectAntimicrobial peptideen
dc.subjectModel membranesen
dc.subjectPhospholipid monolayersen
dc.subjectToroidal poreen
dc.titleHeadgroup specificity for the interaction of the antimicrobial peptide tritrpticin with phospholipid Langmuir monolayersen
dc.typeinfo:eu-repo/semantics/article
Arquivos
Coleções
EPM - Artigos