Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/17838
Title: Binding of Sulpiride to Seric Albumins
Authors: Fragoso, Viviane Muniz da Silva
Coura, Carla Patrícia de Morais
Hoppe, Luanda Yanaan
Soares, Marília Amável Gomes
Silva, Dilson
Cortez, Celia Martins
Affilliation: Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Inovações em Terapias, Ensino e Bioprodutos. Rio de Janeiro, RJ. Brasil.
Universidade do Estado do Rio de Janeiro. Pós-Graduação em Ciências Médicas. Rio de Janeiro, RJ, Brasil.
Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Inovações em Terapias, Ensino e Bioprodutos. Rio de Janeiro, RJ. Brasil.
Universidade do Estado do Rio de Janeiro. Matemática Aplicada. Rio de Janeiro, RJ, Brasil.
Universidade do Estado do Rio de Janeiro. Pós-Graduação em Ciências Médicas. Rio de Janeiro, RJ, Brasil / Universidade do Estado do Rio de Janeiro. Matemática Aplicada. Ri de Janeiro, RJ, Brasil. .
Universidade do Estado do Rio de Janeiro. Pós-Graduação em Ciências Médicas. Rio de Janeiro, RJ, Brasil / Universidade do Estado do Rio de Janeiro. Matemática Aplicada. Rio de Janeiro, RJ, Brasil. .
Abstract: 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.
Keywords: albumins
fluorescence quenching
interaction
sulpiride
keywords: Albuminas
Extinção de fluorescência
Interação
Sulpirida
Issue Date: 2016
Publisher: MDPI
Citation: FRAGOSO, Viviane Muniz da Silva; et al. Binding of Sulpiride to Seric Albumins. Int. J. Mol. Sci., v.17, n.1, 10p, 2016.
DOI: 10.3390/ijms17010059
ISSN: 1661-6596
Copyright: open access
Appears in Collections:IOC - Artigos de Periódicos

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