血清白蛋白与酪胺分子的体外相互作用分析

利用毛细管电泳 (capillary electrophoresis, CE)建立牛血清白蛋白(bovine serum albumin, BSA)-酪胺(tyramine, TA)分子作用机制的分析方法，构建TA-BSA相互作用模型，并研究其相互作用机理. 生理条件下，采用HD法(Hummel-Dreyer, HD)，前沿分析法(frontal analysis, FA)和空峰法(vacant peak, VP)研究TA与BSA的结合机制,构建TA-BSA理论模型,获取TA和BSA相互作用参数,分析理论模型的适用度. 通过分子模拟,构建TA与BSA的结合模型，考察TA的BSA结合机制. 结果表明，HD法和VP法均适用于分析TA-BSA体系的相互作用，VP法最优. 模型适用度分析得出双对数方程最适合模拟TA-BSA相互作用，TA与BSA结合强度较弱,且只有单一类型的结合位点. 构建的TA与BSA结合模型表明,TA与BSA的相互作用力主要是氢键和范德华力，兼有疏水作用力. 本文结果可为分析生物胺-蛋白质分子作用机制研究提供有意义的参考.

Analysis of in vitro Binding of Tyramine with Serum Albumin

The interaction between tyramine (TA) and bovine serum albumin (BSA) was investigated by capillary electrophoresis (CE) based on a theoretical model of TA binding with BSA. Under the physiological condition, the models of TA binding with BSA can be built following the Hummel-Dreyer method (HD), the frontal analysis method (FA) and the vacant peak method (VP). The interaction parameters were derived from these models and the degrees of fitness were analyzed by experiments. The CE results showed that both HD and VP were suitable for analyzing the TA-BSA interaction system, and VP performed the best. As the interaction between TA and BSA were maintained by hydrogen bonds and the van der Waals forces, the fact that a double logarithmic equation could simulate the TA-BSA interaction was probably due to the weak binding force and the sloe type of binding sites were involved in the hydrophobic interface. Our study not only helped to select more relevant theoretic models, but also provided meaningful references for evaluating amine protein interaction.