光谱法及分子模拟研究三唑类化合物与人血清白蛋白的相互作用

Studies on the interaction between triazole derivative and human serum albumin by spectroscopy and molecular modeling

利用荧光光谱法和分子模拟来研究三唑类化合物1-苄基-4-苯基-1,2,3-三氮唑(BPT)与人血清白蛋白(HSA)的相互结合作用机理。利用同步荧光光谱、三维荧光考察了BPT对HSA构象的影响。研究表明,BPT的加入诱导HSA构象发生变化;HSA内部残基所处环境的疏水性增强。采用分子模拟技术,确定BPT的结合位置是HSA的亚结构域IIA,推断BPT与HSA上残基Arg222间存在氢键作用力。

The interaction between 1-benzyl-4-phenyl- 1 H- 1,2,3-triazole （BIYF） and human serum albumin （HSA） was investigated by spectroscopic methods and the molecular modeling technique. Synchronous fluorescence and three-dimensional fluorescence spectroscopy suggested perturbation in the structure of HSA in the presence of BPT and an increase in the hydrophobicity around the fluorophore in HSA. Molecular modeling indicated that the binding of BPT to HSA was most likely located within a hydrophobic cavity of subdomain IIA. The results of molecular modeling revealed that there were hydrogen bonds between Arg222 and BPT.