阿德福韦酯与牛血清白蛋白相互作用的光谱法研究

Spectroscopic Studies on the Interaction of Adefovir Dipivoxil and Bovine Serum Albumin

本文利用荧光光谱法研究并确定了药物阿德福韦酯与牛血清白蛋白的作用机制,研究结果表明:低温时两者间的作用机制为静态猝灭,而在较高温度和较大浓度时表现为静态和动态混合猝灭方式.求得它们在15℃和25℃下结合常数分别为K1=2.534×104L/mol和K2=1.968×104L/mol,结合位点数分别为n1=0.836和n2=0.442;根据不同温度下的结合常数求得阿德福韦酯与牛血清白蛋白的热力学参数(15℃)为:ΔH=2.44 KJ.mol-1、ΔS=93.59 J.mol-1.K-1,其主要结合作用力的类型为疏水作用力,并讨论了药物对蛋白构象的影响.

The mechanism of interaction between adfovir dipivoxil （AD） and bovine serum albumin （BSA） is investigated by fluorescence spectrometry. The result indicates that the mechanism of quenching belongs to static quench at lower temperature, while at higher temperature and with higher drug concentrations the interaction mechanism is mixedquench modes. Their binding constants are K1 = 2. 534 × 10^4 L/tool and K2 = 1. 968 × 10^4 L/mol, and the number of binding sites are n1 = 0.836 and n2 = 0.442, respectively ,at 15 ℃C and 25 ℃. At 25 ℃, the thermodynamic parameters of interaction between AD and BSA are △H=2.44KJ·mol^-1、△S=93.59J·mol^-1·K^-1. The effect of enoxacin on the conformation of BSA is also analyzed using synchronous fluorescence spectrosco- py. The experiments show that there is a strong interaction between AD and BSA, and the main dominant sort of binding forces is hydrophobic interaction.