[Study on the interaction of Nimodipine and bovine serum albumin by fluorescence quenching method].
The interaction of Nimodipine and bovine serum albumin (BSA) was studied using fluorescence spectroscopy (FS) and ultraviolet spectroscopy (UV). The apparent binding constants (KA) between Nimodipine and BSA were 5.01 x 10(4) (26 degrees C) and 4.46 x 10(4) (36 degrees C), and the binding sites (n) were 1.08 +/- 0.01. According to the Förster theory of non-radiation energy transfer, the binding distances (r) were also obtained. The experimental results showed that Nimodipine could quench the inner fluorescence of BSA by forming the Nimodipine-BSA complex. It was found that both static quenching and non-radiation energy transfer led to the fluorescence quenching. The process of binding was a spontaneous molecular interaction in which entropy increased while Gibbs free energy decreased. The thermodynamic parameters indicated that the interaction of Nimodipoine and BSA was driven mainly by static electrical force.
Wu
Qiu-Hua
QH
College of Science, Agricultural University of Hebei, Baoding 071001, China.
Wang
Chun
C
Wang
Zhi
Z
Song
Shuang-Ju
SJ
D000818:Animals; D002417:Cattle; D007700:Kinetics; D009553:Nimodipine / Q000737:chemistry*; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013816:Thermodynamics
D012710:Serum Albumin, Bovine; D009553:Nimodipine