Interaction of tetrandrine with human serum albumin: a fluorescence quenching study.
The interaction of tetrandrine with human serum albumin (HSA) was studied by measuring fluorescence quenching spectra, synchronous fluorescence spectra and ultra-violet spectra. The fluorescence quenching spectra of HSA in the presence of tetrandrine showed that tetrandrine quenched the fluorescence of HSA. The quenching constants of tetrandrine on HSA were determined using the Stern-Volmer equation. Static quenching and non-radiation energy transfer were the two main reasons leading to the fluorescence quenching of HSA by tetrandrine. According to the Förster theory of non-radiation energy transfer, the binding distances (r) and the binding constants (K(A)) were obtained. The thermodynamic parameters obtained in this study revealed that the interaction between tetrandrine and HSA was mainly driven by a hydrophobic force. The conformational changes of HSA were investigated by synchronous spectrum studies.
Wang
Chun
C
College of Science, Agricultural University of Hebei, Hebei, China.
Wu
Qiu-Hua
QH
Li
Cai-Rui
CR
Wang
Zhi
Z
Ma
Jing-Jun
JJ
Zang
Xiao-Huan
XH
Qin
Na-Xin
NX
D000470:Alkaloids / Q000097:blood / Q000737:chemistry*; D044182:Benzylisoquinolines / Q000097:blood / Q000737:chemistry*; D006801:Humans; D007166:Immunosuppressive Agents / Q000737:chemistry*; D012709:Serum Albumin / Q000737:chemistry*; D013050:Spectrometry, Fluorescence
D000470:Alkaloids; D044182:Benzylisoquinolines; D007166:Immunosuppressive Agents; D012709:Serum Albumin; C009438:tetrandrine