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本文采用荧光分光光度法测定了乙烷硒啉与牛血清白蛋白的结合常数和结合位点数并采用Atodock软件分析了乙烷硒啉和人血清白蛋白分子对接的作用方式。计算得出乙烷硒啉与BSA形成复合物的结合常数K为3.5×104L/mol,结合位点数n=0.9。从不同温度下的结合常数可计算出热力学常数ΔH>0,ΔS>0,因此乙烷硒啉与BSA作用力主要应为疏水作用力。结合在人血清白蛋白的高亲和位点上的乙烷硒啉与人血清白蛋白分子中的Cys34未达到能产生相互作用的有效距离,因此乙烷硒啉与人血清白蛋白分子相互作用主要为疏水作用力。
In this paper, the binding constants and binding sites of ethaselen with bovine serum albumin (BSA) were determined by fluorescence spectrophotometry and the interaction between ethaneselen and human serum albumin was analyzed by Atodock software. The calculated binding constant K of the complex formed by ethaselen and BSA was 3.5 × 10 4 L / mol and the number of binding sites was n = 0.9. The thermodynamic constants ΔH> 0 and ΔS> 0 can be calculated from the binding constants at different temperatures. Therefore, the interaction between ethane selenide and BSA should mainly be hydrophobic. Ethaselenine interacts with human serum albumin molecules without reaching an effective distance for interaction with ethaselen and human serum albumin molecules that bind to high affinity sites on human serum albumin Mainly hydrophobic force.