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dc.contributor.authorPertinhezsini, T. A.
dc.contributor.authorNakaie, Clovis Ryuichi [UNIFESP]
dc.contributor.authorCarvalho, Regina Siqueira Haddad [UNIFESP]
dc.contributor.authorPaiva, Antonio Cechelli de Mattos [UNIFESP]
dc.contributor.authorTabak, M.
dc.contributor.authorToma, F.
dc.contributor.authorSchreier, Shirley [UNIFESP]
dc.date.accessioned2018-06-15T14:28:07Z
dc.date.available2018-06-15T14:28:07Z
dc.date.issued1994-02-01
dc.identifier.citationBrazilian Journal Of Medical And Biological Research. Sao Paulo: Assoc Bras Divulg Cientifica, v. 27, n. 2, p. 535-540, 1994.
dc.identifier.issn0100-879X
dc.identifier.urihttp://repositorio.unifesp.br/11600/43056
dc.description.abstractMembrane proteins influence the organizational and motional properties of lipids,while the conformation and function of these proteins (receptors, channels, enzymes, pumps) are affected by the lipid environment. Model systems consisting of peptides and lipids can provide information at a molecular level about the interactions between proteins and lipids in biological membranes. We have synthesized peptides (residues 253-266 (EYWSTFGNLHHISL) from the seven-helix receptor expressed by the mas oncogene),having free or blocked N- and C-terminals. An analog was obtained by linking a spin-labeled amino acid to the N-terminal via a peptide bond. Several spectroscopic techniques were employed to study the interaction between the peptides and lipophilic systems (zwitterionic and negatively charged phospholipid bilayers,and negatively charged,positively charged, zwitterionic and nonionic micelles). Peptide conformational changes were monitored by circular dichroism (CD). The peptides acquired an increased secondary structure upon binding to the lipid systems. Additional evidence for peptide incorporation into micelles came from fluorescence measurements which indicated a blue shift of the tryptophan's emission wavelength,and from ESR spectra of the spin-labeled analog. While narrow lines were obtained in the aqueous phase, line broadening indicative of slower motion was observed in the presence of the lipophilic aggregates. The slow exchange between the two media allowed the evaluation of partition coefficients. The spectra in aqueous solution were also sensitive to conformational changesen
dc.format.extent535-540
dc.language.isoeng
dc.publisherAssoc Bras Divulg Cientifica
dc.relation.ispartofBrazilian Journal Of Medical And Biological Research
dc.rightsAcesso restrito
dc.subjectPEPTIDE-BILAYER INTERACTIONen
dc.subjectMAS ONCOGENE PROTEINen
dc.subjectLIPID BILAYERen
dc.subjectMICELLEen
dc.subjectELECTRON SPIN RESONANCEen
dc.subjectFLUORESCENCEen
dc.subjectCIRCULAR DICHROISMen
dc.titleBINDING OF PEPTIDE-FRAGMENTS FROM A 7 HELIX MEMBRANE-RECEPTOR TO LIPID BILAYERS AND TO MICELLESen
dc.typeArtigo
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionCEA
dc.description.affiliationUNIV SAO PAULO,INST QUIM,DEPT BIOQUIM,BR-05508900 SAO PAULO,BRAZIL
dc.description.affiliationESCOLA PAULISTA MED,DEPT BIOFIS,BR-04023062 SAO PAULO,SP,BRAZIL
dc.description.affiliationUNIV SAO PAULO,INST FIS & QUIM SAO CARLOS,BR-13560970 SAO CARLOS,SP,BRAZIL
dc.description.affiliationCEA,DEPT INGN & ETUD PROT,SACLAY,FRANCE
dc.description.affiliationUnifespESCOLA PAULISTA MED,DEPT BIOFIS,BR-04023062 SAO PAULO,SP,BRAZIL
dc.description.sourceWeb of Science
dc.identifier.wosWOS:A1994MX60900066


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