| 光谱学与光谱分析 |
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| Spectroscopic Study on the Interaction between Resveratrol and Human Serum Albumin |
| WU Qiu-hua, ZHOU Xin, ZANG Xiao-huan, WANG Chun, ZHANG Zhi-heng, WANG Zhi* |
| Key Laboratory of Bioinorganic Chemistry, College of Science, Agricultural University of Hebei, Baoding 071001, China |
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Abstract The interaction between resveratrol and human serum albumin (HSA) was studied by using fluorescence quenching spectra, synchronous fluorescence spectra and ultra-violet spectra. The Stern-Volmer curve of the fluorescence quenching of HSA by resveratrol indicated that the quenching mechanism between resveratrol and HSA was mainly static quenching, with nonradiation energy transfer occurring within single molecule. The binding constants (KA) were 2.39×105 (25 ℃)，1.25×105 (35 ℃) and 1.10×105 (45 ℃), respectively. According to the Frster theory of nonradiation energy transfer, the binding distances (r) were 3.02 nm (25 ℃), 3.46 nm (35 ℃) and 3.79 nm (45 ℃), respectively. The thermodynamic parameters showed that the interaction between resveratrol and HSA was mainly driven by hydrophobic force. Synchronous spectrum was used to investigate the conformational change of HSA.
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Received: 2007-10-06
Accepted: 2008-01-08
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Corresponding Authors:
WANG Zhi
E-mail: wangzhi@hebau.edu.cn
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