富勒醇与血清白蛋白相互作用的光谱学研究

发布时间：2018-04-27 20:51

本文选题：富勒醇 + 人血清白蛋白　；参考：《光谱学与光谱分析》2017年11期

【摘要】：采用荧光光谱法和紫外-可见吸收光谱法研究了不同温度下富勒醇与血清白蛋白的相互作用机理,研究结果表明,富勒醇对人和牛血清白蛋白的内源荧光有明显的猝灭作用,猝灭过程均为静态猝灭,并测定和计算得到不同温度下富勒醇与血清白蛋白反应的结合常数(K_(HSA)=273K1.546×10~4,K_(HSA)=293K1.513×10~4;K_(BSA)=273K13.920×10~4,K_(BSA)=293K939.500×104~)、结合位点数(n_(HSA)=293K0.952 2;n_(BSA)=293K1.376 2)。通过结合反应的热力学数据分析,推测出富勒醇与血清白蛋白之间主要靠疏水作用结合;富勒醇与BSA结合强度明显大于富勒醇与HSA的结合强度,BSA的结合常数受温度影响更大;人和牛血清白蛋白在273和293K的结合位点数在0.901→1.376之间,BSA与富勒醇结合位点数略大于HAS。同时采用分子模拟对接方法,预测富勒醇对牛血清白蛋白的结合部位和作用方式;通过AlignX序列分析法得到BSA与HSA的氨基酸序列相似度较高,在序列160和185附近氨基酸序列差异性较大,推测这是影响两种蛋白质之间与富勒醇作用方式的关键位点。
[Abstract]:The interaction mechanism of fullerenol with serum albumin at different temperatures was studied by fluorescence spectrometry and UV-Vis absorption spectrometry. The results showed that fullethanol had obvious quenching effect on the endogenous fluorescence of human and bovine serum albumin. The quenching process was all static quenching, and the binding constant of fullerenol reaction with serum albumin at different temperatures was determined and calculated. The binding constant of HSAC 273K 1.546 脳 104K 1.546 脳 104K was determined and calculated. By analyzing the thermodynamic data of the binding reaction, it is inferred that the binding strength of fullerenol to BSA is significantly higher than that of fullethanol to HSA, and that the binding constant of fullerenol and serum albumin is more affected by temperature than that of fullethanol by hydrophobic interaction. The binding sites of human and bovine serum albumin at 273 and 293K were between 0.901 and 1.376. The binding sites of human and bovine serum albumin to fullerenol were slightly higher than those of HASs. At the same time, molecular simulation docking method was used to predict the binding site and action mode of fullerenol to bovine serum albumin, and the amino acid sequence similarity between BSA and HSA was obtained by AlignX sequence analysis. The amino acid sequences near sequence 160 and 185 are quite different, which is supposed to be the key site affecting the interaction between the two proteins and fullerenol.
【作者单位】：浙江理工大学生命科学学院浙江省生物医药重点实验室;江南大学生物工程学院糖化学与生物技术教育部重点实验室;
【基金】：国家自然科学基金项目(21405140);国家自然科学基金面上项目(21271162)资助浙江省自然科学基金项目(LQ14B050003) 浙江理工大学科研启动基金项目(15042089-Y)
【分类号】：O657.3;TQ460.1

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