氟达拉滨和人血清白蛋白相互作用机制研究

Studies on the Interaction Mechanism Between Fludarabine and Human Serum Albumin

氟达拉滨(Flu)常被用于治疗慢性淋巴细胞白血病,人血清白蛋白(HSA)是一种重要的载体蛋白。采用多光谱法联用和分子对接模拟技术,研究Flu和HSA的相互作用机制。实验结果表明:Flu与HSA的相互作用符合荧光静态猝灭机制,结合的位点为siteⅠ,其相互作用过程是由疏水作用力和氢键作用力驱动的。Flu可以改变HSA的二级结构。在310 K时,结合常数为1.552×10~4 L·mol^(-1)。分子对接模拟技术实验结果表明Flu和HSA之间的最低结合能为-11.15 kcal·mol^(-1)。

Fludarabine(Flu)is widely used to treat chronic lymphocytic leukemia.Human serum albumin(HSA)is an important carrier protein.In this paper,the interaction mechanism between Flu and HSA was studied by using multispectral method and molecular docking simulation.Experimental results showed that the interaction between Flu and HSA conformed to the static fluorescence quenching mechanism and the biding site was siteⅠ.The process was driven by hydrophobic force and hydrogen bond force.Flu can alter the secondary structure of HSA.At 310 K,the binding constant was 1.552×104 L·mol-1.The experimental results of molecular docking simulation showed that the lowest binding energy between Flu and HSA was-11.15 kcal·mol-1.