Spectroscopic Studies on the Interaction of Efonidipine with Bovine Serum Albumin
The binding of efonidipine to bovine serum albumin (BSA) was investigated by fluorescence spectroscopy and circular dichroism (CD) technique. The quenching mechanism of fluorescence BSA by efonidipine showed that efonidipine quenched the fluorescence of tryptophan residue mainly through the collision mode. The thermodynamic parameters AH0 and AS0 were calculated to be 75.95 kJ·mol-1 and 342.32 J·mol-1 K-1, respectively, indicating that the hydrophobic force played a major role. The results of CD spectrum and synchronous fluorescence spectrum showed that the binding of efonidipine to BSA leads to conformational change of BSA. Binding studies in the presence of ANS indicated that efonidipine competed with ANS for hydrophobic sites on BSA. The effects of metal ion on the binding constant of efonidipine-BSA complex were also investigated.
Efonidipine Bovine serum albumin quenching
Nan Wang Shuting Ku Peilin Yu Bingqing Zhao Ling Ye
School of Chemical Biology and Pharmaceutical Sciences Capital Medical University, Beijing 100069 P.R. China
国际会议
上海
英文
261-264
2008-05-16（万方平台首次上网日期，不代表论文的发表时间）