Utilize este identificador para referenciar este registo: http://hdl.handle.net/10451/20182
Título: Fluorescence spectroscopy evaluation of fibrinogen–β-estradiol binding
Autor: Gonçalves, Sónia
Santos, Nuno C.
Martins-Silva, J.
Saldanha, Carlota
Palavras-chave: Fibrinogen
β-estradiol
Fluorescence
Binding constant
Quenching
Data: 2006
Editora: Elsevier
Citação: Journal of Photochemistry and Photobiology B: Biology 86 (2007) 170–176
Resumo: Fluorescence spectroscopy experiments were performed in order to study conformational changes induced by the binding of b-estradiol to fibrinogen at different ligand concentrations. The association constant (Ka) obtained for the fibrinogen-β -estradiol binding was 6.47 x 106 M-1, indicating a high affinity interaction. Fluorescence quenching experiments showed that approximately 30% of the tryptophan residues in the protein quaternary structure are accessible to ionic quenchers. The extent of quenching in the absence and presence of β estradiol was maximum for cesium ions and minimum for iodide, suggesting the presence of negatively charged residues in the vicinity of the tryptophan residues. The quenching parameters obtained at different β-estradiol concentrations show alterations that confirm a conformational change, possibly due to a discrete reorganization of tryptophan residues during fibrinogen-b-estradiol binding. This binding may be responsible for the effects of b-estradiol on the decrease of erythrocyte aggregation and on cardiovascular risk reduction.
Descrição: © 2006 Elsevier B.V. All rights reserved.
Peer review: yes
URI: http://hdl.handle.net/10451/20182
DOI: http://dx.doi.org/10.1016/j.jphotobiol.2006.09.001
ISSN: 1011-1344
Versão do Editor: http://www.sciencedirect.com/science/journal/10111344
Aparece nas colecções:IMM - Artigos em Revistas Internacionais
FM-IB-Artigos em Revistas Internacionais

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