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Fluorescence spectroscopy evaluation of fibrinogen–β-estradiol binding

Paper ID Volume ID Publish Year Pages File Format Full-Text
31168 44560 2007 7 PDF Available
Title
Fluorescence spectroscopy evaluation of fibrinogen–β-estradiol binding
Abstract

Fluorescence spectroscopy experiments were performed in order to study conformational changes induced by the binding of β-estradiol to fibrinogen at different ligand concentrations. The association constant (Ka) obtained for the fibrinogen–β-estradiol binding was 6.47 × 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–β-estradiol binding. This binding may be responsible for the effects of β-estradiol on the decrease of erythrocyte aggregation and on cardiovascular risk reduction.

Keywords
Fibrinogen; β-estradiol; Fluorescence; Binding constant; Quenching
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Fluorescence spectroscopy evaluation of fibrinogen–β-estradiol binding
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 86, Issue 2, 1 February 2007, Pages 170–176
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
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Any Questions? feel free to contact us