Spectrofluorimetric study of the binding of daphnetin to bovine serum albumin.
Spectrofluorimetric study of the binding of daphnetin to bovine serum albumin.
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DOI：
10.1016/j.jpba.2004.02.010
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发表时间：
2004-05
影响因子：
3.4
通讯作者：
Jiaqin Liu;Jianniao Tian;Wenying He;J. Xie;Zhide Hu;Xingguo Chen
中科院分区：
文献类型：
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作者：
Jiaqin Liu;Jianniao Tian;Wenying He;J. Xie;Zhide Hu;Xingguo Chen
达芙妮素（7,8-二羟基香豆素）是一种螯合剂、抗氧化剂和蛋白激酶抑制剂，是从达芙妮草中分离出来的主要生物活性成分之一（作为葡萄糖苷）。在本文中，我们首次报道了在牛血清白蛋白（BSA）浓度为1.5×10−6moll−1，药物浓度为6.7×10−6至2.0×10−5moll−1的生理条件下，瑞香素与牛血清白蛋白（BSA）结合的研究。采用荧光猝灭光谱、傅里叶变换红外（FT-IR）光谱和圆二色（CD）光谱相结合的方法研究了水溶液中瑞香素存在时药物的结合方式、结合常数和蛋白质结构的变化。Scatchard图的曲率表明，瑞香素与BSA上的不止一类位点结合。根据van 't Hoff方程计算得到的热力学参数、焓变（ΔH）和熵变（ΔS）分别为- 24.21 jmol−1和19.30Jmol−1K−1，表明疏水和静电相互作用在瑞香素与牛血清白蛋白的结合中起主要作用。
Daphnetin (7,8-dihydroxycoumarin), one of the major bioactive components isolated from Daphne odora (as glucoside), is a chelator, an antioxidant and a protein kinase inhibitor. In this paper, we report for the first time studies on the binding of daphnetin to bovine serum albumin (BSA) under physiological conditions with BSA concentration of 1.5×10−6moll−1and drug concentration in the range of 6.7×10−6to 2.0×10−5moll−1. Fluorescence quenching spectra in combination with Fourier transform infrared (FT-IR) spectroscopy and circular dichroism (CD) spectroscopy was used to investigate the drug-binding mode, the binding constant and the protein structure changes in the presence of daphnetin in aqueous solution. The curvature of Scatchard plot indicates that daphnetin binds to more than one class of sites on BSA. The thermodynamic parameters, enthalpy change (ΔH) and entropy change (ΔS) were calculated to be −24.21kJmol−1and 19.30Jmol−1K−1according to van’t Hoff equation, which indicated that hydrophobic and electrostatic interaction played main role in the binding of daphnetin to BSA.