End-to-end distance distribution in bradykinin observed by Forster resonance energy transfer

End-to-end distance distribution in bradykinin observed by Forster resonance energy transfer

Autor Souza, E. S. de Google Scholar
Hirata, I. Y. Google Scholar
Juliano, L. Google Scholar
Ito, A. S. Google Scholar
Instituição Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
Resumo Forster resonance energy transfer (FRET) was used to study the conformational dynamics of bradykinin related peptides. the fluorescent probe aminobenzoic acid (Abz) bound to the amino terminal of bradykinin maintained its fluorescence characteristics, like high quantum yield and excited state decay dominated by a lifetime of 8.3 ns. the binding of the acceptor group N-[2,4-dinitrophenyl]-ethylenediamine (EDDnp) to the carboxy terminal of Abz labeled bradykinin resulted in a drastic decrease of the fluorescence intensity and in a fastening of the excited state decay. the change of the decay kinetics to an heterogeneous process, precludes the use of energy transfer models based on a single fixed distance between donor and acceptor. the computational package CONTIN was employed to the analysis of time-resolved fluorescence data, allowing the recovery of a distance distribution between donor and acceptor corresponding to the end-to-end distance of the labeled peptide. the distance distribution reflects the occurrence of distinct conformations for the peptide, that coexist in equilibrium during the fluorescence lifetime. We observed three distance populations for bradykinin in water, that merged to two populations when the solvent was trifluoroethanol (TFE). the results were consistent with those obtained from circular dichroism spectroscopy, that showed structural flexibility in water and the presence of more defined secondary structure in TFE. We also studied several peptides related to bradykinin, and the results emphasized the formation of turns involving the proline residues and the decrease of conformational flexibility induced by using TFE as the solvent. (C) 2000 Elsevier Science B.V. All rights reserved.
Assunto ortho-aminobenzoyl-peptide
Forster resonance energy transfer
distance distribution
conformational dynamical
protease fluorescent substrate
Idioma Inglês
Data 2000-04-06
Publicado em Biochimica Et Biophysica Acta-general Subjects. Amsterdam: Elsevier B.V., v. 1474, n. 2, p. 251-261, 2000.
ISSN 0304-4165 (Sherpa/Romeo, fator de impacto)
Editor Elsevier B.V.
Extensão 251-261
Fonte http://dx.doi.org/10.1016/S0304-4165(00)00004-0
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000086303100017
URI http://repositorio.unifesp.br/handle/11600/26292

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