[Study on the interaction of genistein and human serum albumin by spectroscopic method].
The interaction of genistein and human serum albumin (HSA) was investigated by fluorescence quenching spectra, synchronous fluorescence spectra and ultra-violet absorption spectra. The results showed that the quenching mechanism of the intrinsic fluorescence of HSA by genistein is due to the formation of genistein-HSA complex, resulting in a static quenching procedure. The binding constants (KA) were 1.00 x 10(6) (27 degrees C), 1.66 x 10(6) (37 degrees C) and 5.25 x 10(6) (47 degrees C), respectively. According to the Förster theory of non-radiation energy transfer, the binding distances (r) were 2.59 nm (27 degrees C), 2.65 nm (37 degrees C) and 2.90 nm (47 degrees C), respectively. The thermodynamic parameters showed that the binding power between genistein and HSA is mainly the electrostatic interaction Synchronous spectrum was used to investigate the conformational change of HSA.
Wu
Qiu-Hua
QH
Key Laboratory of Bioinorganic Chemistry, College of Science, Agricultural University of Hebei, Baoding 071001, China.
Wang
Chun
C
Zhang
Zhi-Heng
ZH
Zhang
Mei-Yue
MY
Song
Shuang-Ju
SJ
Wang
Zhi
Z
D019833:Genistein / Q000737:chemistry*; D006801:Humans; D007700:Kinetics; D048789:Phytoestrogens / Q000737:chemistry*; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry*; D013050:Spectrometry, Fluorescence / Q000379:methods*
D048789:Phytoestrogens; D012709:Serum Albumin; D019833:Genistein