Next Article in Journal
In Vivo Anti-Tumor Activity and Toxicological Evaluations of Perillaldehyde 8,9-Epoxide, a Derivative of Perillyl Alcohol
Previous Article in Journal
Ruthenium(III) Complexes of Heterocyclic Tridentate (ONN) Schiff Base: Synthesis, Characterization and its Biological Properties as an Antiradical and Antiproliferative Agent
Article Menu
Issue 1 (January) cover image

Export Article

Open AccessArticle
Int. J. Mol. Sci. 2016, 17(1), 59; doi:10.3390/ijms17010059

Binding of Sulpiride to Seric Albumins

1
Laboratory of Innovations in Therapies, Education and Bioproducts, Oswaldo Cruz Institute/FIOCRUZ, Av. Brasil 4365, Rio de Janeiro 21045-900, Brazil
2
Postgraduation in Medical Sciences, Rio de Janeiro State University, Av. Manoel de Abreu, 444, Rio de Janeiro 20550-171, Brazil
3
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)
View Full-Text   |   Download PDF [1076 KB, uploaded 4 January 2016]   |  

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. View Full-Text
Keywords: sulpiride; interaction; albumins; fluorescence quenching sulpiride; interaction; albumins; fluorescence quenching
Figures

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

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.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top