Table of Contents
Dataset Papers in Chemistry
Volume 2013 (2013), Article ID 534328, 5 pages
http://dx.doi.org/10.7167/2013/534328
Dataset Paper

Physicochemical Peculiarities of Iodine-Dimethylsulfoxide-H2O Solutions and Effect on Ion Binding to Bovine Serum Albumin

Department of Chemistry, Yerevan State University, 1 Alex Manoogian Street, 0025 Yerevan, Armenia

Received 27 April 2012; Accepted 6 June 2012

Academic Editors: V. Komanicky, R. Valiullin, and X.-B. Wang

Copyright © 2013 K. Grigoryan and H. Shilajyan. 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.

Abstract

The interaction of iodine with bovine serum albumin (BSA) in dimethylsulfoxide (DMSO) aqueous solutions was studied by means of fluorescence and UV/Vis absorption spectroscopy methods. Physicochemical peculiarities of these solutions were revealed. The results showed that the tri-iodide ion formed in the 1DMSO : 2H2O solution caused the fluorescence quenching of BSA. The modified Stern-Volmer quenching constant and corresponding thermodynamic parameters, the free energy change ( ), enthalpy change ( ), and entropy change ( ), at different temperatures (293, 298, and 303 K) were calculated, which indicated that the hydrophobic and electrostatic interactions were the predominant operating forces. The binding locality distance r between BSA and tri-iodide ion at different temperatures was determined based on Förster nonradiation fluorescence energy transfer theory.