| 光谱学与光谱分析 |
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| Study on the Interaction of Genistein and Human Serum Albumin by Spectroscopic Method |
| WU Qiu-hua, WANG Chun, ZHANG Zhi-heng, ZHANG Mei-yue, SONG Shuang-ju, WANG Zhi* |
| Key Laboratory of Bioinorganic Chemistry, College of Science, Agricultural University of Hebei, Baoding 071001, China |
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Abstract 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 1.00×106 (27 ℃), 1.66×106 (37 ℃) and 5.25×106 (47 ℃), respectively. According to the Frster theory of non-radiation energy transfer, the binding distances (r) were 2.59 nm (27 ℃), 2.65 nm (37 ℃) and 2.90 nm (47 ℃), 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.
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Received: 2007-11-06
Accepted: 2008-02-12
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Corresponding Authors:
WANG Zhi
E-mail: wangzhi@hebau.edu.cn
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