The Fluorescence Spectroscopic Studies on the Interaction of Diltiazem Hydrochloride with Bovine Serum Albumin
Chengman Bao
Jiangsu Key Laboratory for Bioresources of Saline Solis, College of Ocean and Biological Engineering, Yancheng Teachers University, Yancheng, 224051, China
Jialian Wang
Jiangsu Key Laboratory for Bioresources of Saline Solis, College of Ocean and Biological Engineering, Yancheng Teachers University, Yancheng, 224051, China
Xuehong Tong
Jiangsu Key Laboratory for Bioresources of Saline Solis, College of Ocean and Biological Engineering, Yancheng Teachers University, Yancheng, 224051, China
Xinhui Tang *
Jiangsu Key Laboratory for Bioresources of Saline Solis, College of Ocean and Biological Engineering, Yancheng Teachers University, Yancheng, 224051, China
Qingming Wang
School of Pharmacy, Yancheng Teachers University, Yancheng, 224051, China
*Author to whom correspondence should be addressed.
Abstract
Aim: To explore the interaction of the diltiazem hydrochloride (DTZ) with bovine serum albumin (BSA).
Methodology: Fluorescence and UV-Vis spectroscopic techniques were used to study the interaction between diltiazem hydrochloride (DTZ) and BSA. DTZ is a nondihydropyridine calcium channel blocker used in the treatment of many kinds of diseases. The Stern-Volmer quenching constant (Ksv), the quenching rate constant of the bimolecular reaction (Kq), the binding constant (Ka), and a number of binding sites (n) of DTZ with BSA were evaluated.
Results: The results revealed that DTZ quenches the fluorescence intensity of BSA through a static quenching process. The values of ΔS and ΔH indicated that hydrophobic bond interactions played major roles in the binding process and contributed to the stability of the DTZ-BSA complex. Based on the Förster’s theory of non-radiation energy transfer, the distance between donor (BSA) and acceptor (DTZ) was less than 7 nm, which indicated that energy transfer from BSA to DTZ occurs with high probability.
Keywords: Spectroscopy, diltiazem hydrochloride, bovine serum albumin, thermodynamic parameters