| 光谱学与光谱分析 |
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| Study on the Interaction between Fangchinoline and Bovine Serum Albumin |
| WU Qiu-hua,WANG Chun,WANG Zhi*,MA Jing-jun,ZANG Xiao-huan,QIN Na-xin |
| College of Science, Agricultural University of Hebei, Baoding 071001, China |
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Abstract The binding reaction of fangchinoline with bovine serum albumin was studied at different temperatures by fluorescence quenching spectra, synchronous fluorescence spectra and ultra-violet spectra. It was shown that fangchinoline has a strong ability of quenching the fluorescence of BSA. The Stern-Volmer curve of the fluorescence quenching of BSA by fangchinoline indicated that the quenching mechanism of fangchinoline to BSA was a static quenching. According to the Frster theory of non-radiation energy transfer, the binding distances (r) at different temperature were 2.51 nm (27 ℃), 2.72 nm (37 ℃) and 2.89 nm (47 ℃), respectively, while the binding constants (KA) were 1.05×105 L·mol-1 (27 ℃), 3.31×105 L·mol-1 (37 ℃), and 7.24×105 L·mol-1 (47 ℃), respectively. The thermodynamic parameters showed that the interaction of fangchinoline and BSA was mainly driven by hydrophobic force. Synchronous spectrum was used to investigate the conformational changes of BSA.
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Received: 2006-07-30
Accepted: 2006-11-02
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Corresponding Authors:
WANG Zhi
E-mail: wangzhi@hebau.edu.cn
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| Cite this article: |
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WU Qiu-hua,WANG Chun,WANG Zhi, et al. Study on the Interaction between Fangchinoline and Bovine Serum Albumin[J]. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2007, 27(12): 2498-2501.
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| URL: |
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https://www.gpxygpfx.com/EN/Y2007/V27/I12/2498 |
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