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Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of Gold(III)
Published on: August 31, 2018
Spectroscopic studies on the interaction between silicotungstic acid and bovine serum albumin
Yan-Qing Wang1, Hong-Mei Zhang, Gen-Cheng Zhang
1Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection, Institute of Applied Chemistry and Environmental Engineering, Yancheng Normal College, Yancheng City, People's Republic of China. wyqing76@126.com
Abstract:
The interaction between silicotungstic acid and bovine serum albumin (BSA) was investigated using fluorescence and UV/vis. The experimental results showed that the fluorescence quenching of BSA by silicotungstic acid is a result of the formation of SiW-BSA complex; static quenching and non-radiative energy transferring were confirmed to result in the fluorescence quenching. The binding site number n, apparent binding constant K(A) and corresponding thermodynamic parameters were measured at different temperatures. The process of binding SiW molecule on BSA was a spontaneous molecular interaction procedure in which entropy increased and Gibbs free energy decreased. Hydrophobic interaction force plays a major role in stabilizing the complex. The effect of silicotungstic acid on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy.
