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Int. J. Mol. Sci. 2016, 17(1), 59;

Binding of Sulpiride to Seric Albumins

Laboratory of Innovations in Therapies, Education and Bioproducts, Oswaldo Cruz Institute/FIOCRUZ, Av. Brasil 4365, Rio de Janeiro 21045-900, Brazil
Postgraduation in Medical Sciences, Rio de Janeiro State University, Av. Manoel de Abreu, 444, Rio de Janeiro 20550-171, Brazil
Applied Mathematics, Rio de Janeiro State University, Rua São Francisco Xavier, 524, Rio de Janeiro 20559-900, Brazil
These authors contributed equally to this work.
Author to whom correspondence should be addressed.
Academic Editor: Jesus Vicente De Julián Ortiz
Received: 14 September 2015 / Revised: 23 November 2015 / Accepted: 30 November 2015 / Published: 4 January 2016
(This article belongs to the Section Physical Chemistry, Theoretical and Computational Chemistry)
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The aim of this work was to study the interaction of sulpiride with human serum albumin (HSA) and bovine serum albumin (BSA) through the fluorescence quenching technique. As sulpiride molecules emit fluorescence, we have developed a simple mathematical model to discriminate the quencher fluorescence from the albumin fluorescence in the solution where they interact. Sulpiride is an antipsychotic used in the treatment of several psychiatric disorders. We selectively excited the fluorescence of tryptophan residues with 290 nm wavelength and observed the quenching by titrating HSA and BSA solutions with sulpiride. Stern-Volmer graphs were plotted and quenching constants were estimated. Results showed that sulpiride form complexes with both albumins. Estimated association constants for the interaction sulpiride–HSA were 2.20 (±0.08) × 104 M−1, at 37 °C, and 5.46 (±0.20) × 104 M−1, at 25 °C. Those for the interaction sulpiride-BSA are 0.44 (±0.01) × 104 M−1, at 37 °C and 2.17 (±0.04) × 104 M−1, at 25 °C. The quenching intensity of BSA, which contains two tryptophan residues in the peptide chain, was found to be higher than that of HSA, what suggests that the primary binding site for sulpiride in albumin should be located next to the sub domain IB of the protein structure. View Full-Text
Keywords: sulpiride; interaction; albumins; fluorescence quenching sulpiride; interaction; albumins; fluorescence quenching

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da Silva Fragoso, V.M.; de Morais Coura, C.P.; Hoppe, L.Y.; Soares, M.A.G.; Silva, D.; Cortez, C.M. Binding of Sulpiride to Seric Albumins. Int. J. Mol. Sci. 2016, 17, 59.

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