Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5402846 | Journal of Luminescence | 2009 | 6 Pages |
Abstract
In this paper, the interaction between barbital and bovine serum albumin (BSA) was investigated by the method of fluorescence spectroscopy under simulative physiological conditions. Fluorescence data revealed that the fluorescence quenching of BSA by barbital was the result of the formation of BSA-barbital complex, and the effective quenching constants (Ka) were 1.468Ã104, 1.445Ã104 and 1.403Ã104Â Mâ1 at 297, 303 and 310Â K, respectively. The thermodynamic parameters enthalpy change (ÎH) and entropy change (ÎS) for the reaction were calculated to be â2.679Â kJÂ molâ1 and 70.76Â JÂ molâ1Â Kâ1, respectively, according to the van't Hoff equation. The results indicated that hydrophobic and electrostatic interactions were the dominant intermolecular force in stabilizing the complex. The results of synchronous fluorescence spectra showed that binding of barbital with BSA can induce conformational changes in BSA. In addition, the effects of Cu2+ and Zn2+ on the constants of BSA-barbital complex were also discussed.
Related Topics
Physical Sciences and Engineering
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Physical and Theoretical Chemistry
Authors
Fei Ding, Hong Pan, Zhi-Yuan Li, Feng Liu, Ying Sun,