应用紫外吸收光谱、荧光光谱和同步荧光光谱法研究了矢车菊-3 -O-葡萄糖苷与牛血清白蛋白(BSA)的相互作用,结果表明:矢车菊-3 -O -葡萄糖苷能使BSA发生内源荧光猝灭,属静态猝灭机理.25℃和30℃下,矢车菊-3 -O -葡萄糖苷与BSA的静态猝灭速率常数分别为3.7×104 L·mol-1,4.1×104 L·mol -1,结合常数为1.1×105 L·mol-1,1.5×105 L·mol-1,结合位点数为1.根据Fòrster非辐射能量转移机理,矢车菊-3 -O-葡萄糖苷与BSA之间的作用距离约为5.6nm,能量转移效率为0.085.热力学分析表明矢车菊-3 -O -葡萄糖苷与BSA存在疏水相互作用,矢车菊-3 -O -葡萄糖苷对BSA构象影响较小.%The interaction of Cyanidin - 3 - 0 - glucoside chloride with bovine serum albumin ( BSA) was studied by UV absorption spectroscopy fluorescence spectroscopy and synchronous fluorescence spectroscopy in the work. The results showed that Cy -3 -0 -Glu could induce an endogenous fluorescence quenching of BSA under a mechanism of static quenching. The quenching rate constants at 25℃ and 30℃ were determined to be 3. 7 × 104 L · mol -1 ,4. 1 × 104 L · mol-1, respectively; the binding constants 1. 1 × 105 L · mol-1, 1. 5 × 105 L · mol-1, respectively. The number of binding site of the static quenching was calculated. According to the theory of Fdrster nonradiative energy transfer the interacting distance of Cy - 3 - 0 - Glu and BSA was estimated to be 5. 62nm nm with an efficiency of 0. 0851. By analysis of thermodynamic parameters, the binding of Cy - 3 - 0 - Glu with BSA was mainly attributed to the hydrophobic interaction. The Cy - 3 - 0 - Glu had only a slight influence on the BSA conformation by the fluorescence spectra.
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