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

K. R. Grigoryan | Zendy; Hasmik A. Shilajyan | Zendy

Open Access

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

Author(s) -

K. R. Grigoryan,

Hasmik A. Shilajyan

Publication year - 2012

Publication title -

dataset papers in chemistry

Language(s) - English

Resource type - Journals

ISSN - 2314-5315

DOI - 10.7167/2013/534328

Subject(s) - bovine serum albumin , chemistry , iodide , fluorescence , quenching (fluorescence) , aqueous solution , enthalpy , ion , iodine , hydrophobic effect , binding constant , analytical chemistry (journal) , absorption (acoustics) , inorganic chemistry , chromatography , binding site , thermodynamics , organic chemistry , materials science , biochemistry , physics , quantum mechanics , composite material

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 : 2H 2 O 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.

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