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首页> 外文期刊>Bulletin of the Korean Chemical Society >Interaction of Bilobalide and Ginkgolides B with Bovine Serum Albumin: A Fluorescence Quenching Study
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Interaction of Bilobalide and Ginkgolides B with Bovine Serum Albumin: A Fluorescence Quenching Study

机译:Bilobalide和银杏内酯B与牛血清白蛋白的相互作用:荧光猝灭研究

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The interaction of bilobalide (BB) and ginkgolides B (GB) with bovine serum albumin (BSA) was investigated by fluorescent technique and UV/vis absorption spectroscopy. The results showed that BB and GB could intensively quench the fluorescence of BSA through a static quenching procedure. The binding constants (Ka) and the average binding distance between the donor (BSA) and the acceptor (ginkgolides) were obtained (rBB = 5.33 nm and rGB = 4.20 nm) by the theory of non-radiation energy transfer, and then the thermodynamic parameters such as ΔS0 (0.17-0.32 kJ/mol), ΔG0 (-20.76 ~ -17.79 kJ/mol) and ΔH0 (32.47-76.52 kJ/mol) could be calculated, respectively. All these results revealed that the interaction of BB and GB with BSA were driven mainly by hydrophobie force. The synchronous fluorescence spectroscopy was applied to examine the effect of two ginkgolides on the configuration of BSA. The configuration alteration of BSA could be induced by the hydrophobicitv environment of tyrosine with the increase of the drug concentration.
机译:通过荧光技术和紫外/可见吸收光谱法研究了银杏内酯(BB)和银杏内酯B(GB)与牛血清白蛋白(BSA)的相互作用。结果表明,BB和GB可以通过静态猝灭程序来强烈猝灭BSA的荧光。通过无辐射能量转移理论,然后通过热力学原理,获得了结合常数(Ka)和供体(BSA)与受体(银杏内酯)之间的平均结合距离(rBB = 5.33 nm,rGB = 4.20 nm)。可以分别计算出ΔS0(0.17-0.32 kJ / mol),ΔG0(-20.76〜-17.79 kJ / mol)和ΔH0(32.47-76.52 kJ / mol)等参数。所有这些结果表明,BB和GB与BSA的相互作用主要是由疏水力驱动的。采用同步荧光光谱法研究了两种银杏内酯对BSA构型的影响。随着药物浓度的增加,酪氨酸的疏水环境可能引起BSA的构型改变。

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