Structural biology of membrane-acting peptides: Conformational plasticity of anticoccidial peptide PW2 probed by solution NMR

dc.contributor.authorCruzeiro-Silva, C.
dc.contributor.authorGomes-Neto, F.
dc.contributor.authorTinoco, L. W.
dc.contributor.authorCilli, Eduardo Maffud [UNESP]
dc.contributor.authorBarros, P. V. R. [UNESP]
dc.contributor.authorLapido-Loureiro, P. A. [UNESP]
dc.contributor.authorBisch, P. M. [UNESP]
dc.contributor.authorAlmeida, F. C. L.
dc.contributor.authorValente, A. P.
dc.contributor.institutionUniversidade Federal do Rio de Janeiro (UFRJ)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T15:23:30Z
dc.date.available2014-05-20T15:23:30Z
dc.date.issued2007-12-01
dc.description.abstractThe bottleneck for the complete understanding of the structure-function relationship of flexible membrane-acting peptides is its dynamics. At the same time, not only the structure but also the dynamics are the key points for their mechanism of action. Our model is PW2, a TRP-rich, cationic peptide selected from phage display libraries that shows anticoccidial activity against Eimeria acervulina. In this manuscript we used a combination of several NMR techniques to tackle these difficulties. The structural features of the membrane-acting peptide PW2 was studied in several membrane mimetic environments: we compared the structural features of PW2 in SDS and DPC micelles, that were reported earlier, with the structure properties in different lipid vesicles and the peptide free in water. We were able to unify the structural information obtained in each of these systems. The structural constraints of the peptide free in water were fundamental for the understanding of plasticity necessary for the membrane interaction. Our data suggested that the WWR sequence is the region responsible for anchoring the peptide to the interfaces, and that this same region displays some degree of conformational order in solution. For PW2, we found that affinity is related to the aromatic region, by anchoring the peptide to the membrane, and specificity is related to the N- and C-termini, which are able to accommodate in the membrane due to its plasticity. (C) 2007 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniv Fed Rio de Janeiro, Inst Bioquim Med, Ctr Nacl Ressonancia Magent Nucl Jiri Jonas, Programa Biol Estruct, Rio de Janeiro, Brazil
dc.description.affiliationUniv Fed Rio de Janeiro, Rio de Janeiro, Brazil
dc.description.affiliationUniv Estadual Paulista, UNESP, São Paulo, Brazil
dc.description.affiliationUniv Estadual Paulista, Inst Biofis Carlos Chagas Filho, São Paulo, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, UNESP, São Paulo, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Inst Biofis Carlos Chagas Filho, São Paulo, Brazil
dc.format.extent3182-3192
dc.identifierhttp://dx.doi.org/10.1016/j.bbamem.2007.08.022
dc.identifier.citationBiochimica Et Biophysica Acta-biomembranes. Amsterdam: Elsevier B.V., v. 1768, n. 12, p. 3182-3192, 2007.
dc.identifier.doi10.1016/j.bbamem.2007.08.022
dc.identifier.fileWOS000252488900025.pdf
dc.identifier.issn0005-2736
dc.identifier.lattes9424346762460416
dc.identifier.orcid0000-0002-4767-0904
dc.identifier.urihttp://hdl.handle.net/11449/34289
dc.identifier.wosWOS:000252488900025
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochimica et Biophysica Acta: Biomembranes
dc.relation.ispartofjcr3.438
dc.relation.ispartofsjr1,495
dc.rights.accessRightsAcesso aberto
dc.sourceWeb of Science
dc.titleStructural biology of membrane-acting peptides: Conformational plasticity of anticoccidial peptide PW2 probed by solution NMRen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.lattes9424346762460416
unesp.author.orcid0000-0002-4767-0904[4]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Química, Araraquarapt

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