| 光谱学与光谱分析 |
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| Studies on the Interaction of Rhein with Bovine Serum Albumin by Spectroscopic and Voltammetric Methods |
| LIANG Hui, ZHAO Fang*, LI Bing-qi |
| College of Chemistry and Chemical Engineering, Shihezi University, Shihezi 832000，China |
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Abstract The interaction between rhein and bovine serum albumin(BSA) was studied by UV-Visible，fluorescence spectroscopy and circular dichroism in conjunction with electrochemical method. The results indicated that rhein has a powerful ability to quench the albumin’s fluorescence in a static mode. The binding constants(KA) and binding site numbers (n) obtained at different temperatures were 3.67×105, 0.99 (298 K) and 2.60×104, 0.83 (309 K) respectively. According to the thermodynamic parameters the main sorts of binding force of rhein-BSA was fixed as electrostatic. The distance between donor and acceptor in rhein-BSA was 3.28 nm based on the Frster energy transfer theory. Results of the circular dichroism and synchronous fluorescence show that the binding can cause conformation change of BSA.
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Received: 2010-11-30
Accepted: 2011-04-01
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Corresponding Authors:
ZHAO Fang
E-mail: nnllzzff@163.com
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