Fret Studies of Conformational Changes in Heparin-Binding Peptides

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dc.contributor.authorSouza, Eduardo Sergio de
dc.contributor.authorKatagiri, Alberto H.
dc.contributor.authorJuliano, Luiz [UNIFESP]
dc.contributor.authorJuliano, Maria Aparecida [UNIFESP]
dc.contributor.authorPimenta, Daniel Carvalho
dc.contributor.authorIto, Amando Siuiti
dc.contributor.institutionUniversidade Federal de Goiás (UFG)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionInst Butantan
dc.date.accessioned2016-01-24T14:37:14Z
dc.date.available2016-01-24T14:37:14Z
dc.date.issued2014-05-01
dc.description.abstractFRET (Forster Resonance Energy Transfer) was applied to study structural properties of heparin-binding peptides containing the sequence XBBBXXBX where 'X' represents hydropathic or uncharged and 'B' represents basic amino acids. Internally quenched fluorogenic peptides were synthesized containing the fluorescent donor oaminobenzoic acid (o-Abz) and the acceptor dinitrophenyl ethylenediamine (Eddnp) group. Using the CONTIN computational package, distance distributions were recovered from time resolved fluorescence data, associated to end-to-end distances of the peptides. the peptides containing three or four repeat units have random structure in aqueous medium, and the interaction with low molecular weight heparin stabilized short end-to end distances. Experiments in water/trifluoroethanol (TFE) mixtures showed changes in distance distributions compatible with compact conformations stabilized above 40 % volume content of TFE in the mixture. Similar changes in distance distributions were also observed for the peptides in interaction with SDS micelles in aqueous suspensions and circular dichroism data revealed alpha-helix formation in the peptides in interaction with heparin, SDS micelles or the co-solvent TFE. the process is dependent on electrostatic and hydrogen bond interactions and the end-to-end distances obtained are smaller than expected for the peptides in linear alpha-helix conformation, indicating the occurrence of structural arrangements leading to additional decrease in the distances.en
dc.description.affiliationUniv Fed Goias, Dept Fis, BR-75704020 Catalao, Go, Brazil
dc.description.affiliationUniv São Paulo, Inst Fis, BR-05508090 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biofis, Escola Paulista Med, BR-04044020 São Paulo, Brazil
dc.description.affiliationInst Butantan, Lab Bioquim & Biofis, BR-05503900 São Paulo, Brazil
dc.description.affiliationUniv São Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, BR-14040901 Ribeirao Preto, SP, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biofis, Escola Paulista Med, 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.sponsorshipINCT-FCx, Brazil
dc.description.sponsorshipIDFAPESP: 12/50191-4
dc.format.extent885-894
dc.identifierhttp://dx.doi.org/10.1007/s10895-014-1366-3
dc.identifier.citationJournal of Fluorescence. New York: Springer/plenum Publishers, v. 24, n. 3, p. 885-894, 2014.
dc.identifier.doi10.1007/s10895-014-1366-3
dc.identifier.issn1053-0509
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/37716
dc.identifier.wosWOS:000336733100029
dc.language.isoeng
dc.publisherSpringer
dc.relation.ispartofJournal of Fluorescence
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dc.subjectGlycosaminoglicanen
dc.subjectCardinmotif peptidesen
dc.subjectTime resolved fluorescenceen
dc.subjectForster resonant energy transferen
dc.subjectIntramolecular distanceen
dc.subjectInternally quenched fluorogenic peptidesen
dc.subjectHeparinen
dc.titleFret Studies of Conformational Changes in Heparin-Binding Peptidesen
dc.typeinfo:eu-repo/semantics/article
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