Interaction between Xanthoxylin and Bovine Serum Albumin

Interaction between Xanthoxylin and Bovine Serum Albumin
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黄木精和牛血清白蛋白之间的相互作用

DOI:
10.1002/cjoc.200990049
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发表时间:
2009-02
期刊:
中国化学(英文版)
影响因子:
--
通讯作者:
Huang Yonglin
Huang Yonglin
中科院分区:
其他
文献类型:
--
作者:
Liang Hong;Wen Maogui;Chen Zhengfeng;Tian Jianniao;Bian Hedong;Huang Yonglin

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利用荧光光谱、圆二色光谱和傅里叶变换红外光谱等多种光谱技术,对模拟生理条件下xanthoxylin (XT)与牛血清白蛋白(BSA)的相互作用进行了详细分析。荧光猝灭数据表明,在286、298和310 K时,猝灭常数(K)分别为3.31×105、2.03×105和0.94×105 L·mol−1。根据荧光结果,发现XT与BSA相互作用的荧光猝灭机制为静态猝灭与动态猝灭相结合。热力学参数ΔH0、ΔS0和ΔG0表明疏水力在XT与BSA结合中起主要作用。通过FT-IR光谱分析XT对牛血清白蛋白构象的影响,并通过CD光谱定量计算α-螺旋含量降低约3.9%。此外,还讨论了普通离子对结合常数的影响。
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 dichroism (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 ΔH0, ΔS0 and ΔG0 suggested that the hydrophobic force played a main role in binding of XT to BSA. The effect of XT on the conformation of BSA was analyzed by FT-IR spectroscopy and quantitatively calculated from CD spectroscopy with reduction of α-helical content by about 3.9%. In addition, the effect of common ions on the binding constant was also discussed.
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