Study on the interaction between clozapine and bovine serum albumin
作者： Jing-Ci Li , Ning Li , Qiu-Hua Wu , Zhi Wang , Jing-Jun Ma
DOI: 10.1016/J.MOLSTRUC.2006.09.019
关键词: Binding site 、 Analytical chemistry 、 Hydrogen bond 、 van der Waals force 、 Tryptophan 、 Quenching (fluorescence) 、 Bovine serum albumin 、 Chemistry 、 Ultraviolet visible spectroscopy 、 Fluorescence spectroscopy 、 Physical chemistry
摘要: Abstract The interaction between bovine serum albumin (BSA) and clozapine (CZP) was investigated using fluorescence spectroscopy (FS) ultraviolet (UV). experimental data showed that the CZP could insert into BSA quench its intrinsic by forming CZP–BSA complex. It found both static quenching non-radiation energy transfer were main reasons leading to quenching. apparent binding constants ( K ) determined be 1.26 × 10 5 (300 K) 1.67 × 10 4 (310 K). sites n 1.1 ± 0.1. According Forster theory of transfer, distances r tryptophan residue 2.99 nm 2.74 nm (310 K), respectively. thermodynamic parameters driven mainly hydrogen bonding interactions Van der Waals force.
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