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Molecules 2010, 15(6), 3905-3919; doi:10.3390/molecules15063905

Bovine and Human Serum Albumin Interactions with 3-Carboxyphenoxathiin Studied by Fluorescence and Circular Dichroism Spectroscopy

Department of Physical Chemistry, University of Bucharest, Bd. Regina Elisabeta, 4-12, Bucharest, Romania
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Received: 5 May 2010 / Accepted: 26 May 2010 / Published: 1 June 2010
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Abstract

The interactions of 3-carboxyphenoxathiin with Bovine Serum Albumin (BSA) and Human Serum Albumin (HSA) have been studied by fluorescence and circular dichroism spectroscopy. The binding of 3-carboxyphenoxathiin quenches the BSA and HSA fluorescence, revealing a 1:1 interaction with a binding constant of about 105 M-1. In addition, according to the synchronous fluorescence spectra of BSA and HSA in presence of 3-carboxyphenoxathiin, the tryptophan residues of the proteins are most perturbed by the binding process. Finally, the distance between the acceptor, 3-carboxyphenoxathiin, and the donor, BSA or HSA, was estimated on the basis of the Förster resonance energy transfer (FRET). The fluorescence results are correlated with those obtained from the circular dichroism spectra, which reveal the change of the albumin conformation during the interaction process.
Keywords: steady state fluorescence; synchronous fluorescence; circular dichroism; 3-carboxyphenoxathiin; serum albumin steady state fluorescence; synchronous fluorescence; circular dichroism; 3-carboxyphenoxathiin; serum albumin
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MDPI and ACS Style

Varlan, A.; Hillebrand, M. Bovine and Human Serum Albumin Interactions with 3-Carboxyphenoxathiin Studied by Fluorescence and Circular Dichroism Spectroscopy. Molecules 2010, 15, 3905-3919.

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