Interaction between diethylstilbestrol and bovine serum albumin

Autor: Zhihong Shi, Yujie Wu, Xuyang Liu, Han-Wen Sun, Xianghua Xia
Rok vydání: 2012
Předmět:
Zdroj: Monatshefte für Chemie - Chemical Monthly. 144:739-746
ISSN: 1434-4475
0026-9247
Popis: The interaction between diethylstilbestrol (DES) and bovine serum albumin (BSA) was studied by fluorescence spectroscopy combined with the UV-Vis spectrophotometric technique under simulative physiological conditions. The influence of Cd and/or Se ions on the interaction between DES and BSA was also investigated. The fluorescence quenching rate constants, binding constants, and thermodynamic parameters for the BSA–DES system were determined at different temperatures. The distance between BSA and DES was estimated to be 3.65 nm based on the Forster resonance energy transfer theory. The fluorescence quenching of BSA by addition of DES is due to static quenching and energy transfer. The negative value of enthalpy change and entropy change indicated that both hydrogen bonding and van der Waals forces played major roles in the binding of DES to BSA. The tryptophan residue of BSA molecules mainly participated in the binding reaction to DES. Competitive experiments with warfarin, ibuprofen, and digoxin as specific probes suggested that the primary binding site for DES was located at site III in the sub-domain IIIA of BSA. In addition, the interaction between DES and BSA in the presence of Cd(II) decreased by four orders of magnitude.
Databáze: OpenAIRE
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