Interaction between Xanthoxylin and Bovine Serum Albumin

The interaction between xanthoxylin (XT) and bovine serum albumin (BSA) under simulative physiological conditions has been analyzed in detail by various spectroscopic techniques including fluorescence, circular dichro- ism (CD), and Fourier transform infrared (FT-IR) spectroscopy. Fluorescence quenching data revealed that the quenching constants (K) were 3.31×105, 2.03×105 and 0.94×105 L·mol-1 at 286, 298 and 310 K, respectively. Based on the fluorescence results, the fluorescence quenching mechanism of the interaction between XT and BSA has been found to be combined static and dynamic quenching. Thermodynamic parameters △H0, △S0 and △G0 sug- gested that the hydrophobic force played a main role in binding of XT to BSA. The effect of XT on the conforma- tion of BSA was analyzed by FT-IR spectroscopy and quantitatively calculated from CD spectroscopy with reduc- tion of α-helical content by about 3.9%. In addition, the effect of common ions on the binding constant was also dis- cussed.

作 者： WEN Maogui TIAN Jianniao HUANG Yonglin BIAN Hedong CHEN Zhengfeng LIANG Hong   作者單位： WEN Maogui,TIAN Jianniao,CHEN Zhengfeng,LIANG Hong(Key Laboratory for Chemistry and Molecular Engineering of Medicinal Resources (Guangxi Normal University),Ministry of Education of China, Guilin, Guangxi 54904, China)

HUANG Yonglin(Guangxi Institute of Botany,Guangxi Zhuangzu Autonomous Region and the Chinese Academy of Sciences,Guilin,Guangxi 541004,China)

BIAN Hedong(Chemistry and Chemical Engineering,Guangxi Normal University,Guilin,Guangxi 541004,China) 

刊 名： 中國(guó)化學(xué)（英文版）  SCI 英文刊名： CHINESE JOURNAL OF CHEMISTRY  年，卷(期)： 2009 27(2)  分類號(hào)： O6  關(guān)鍵詞： bovine serum albumin   xanthoxylin   Fourier transform infrared spectra (FT-IR)   fluorescence quench-ing  

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