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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。
Fluorescence spectroscopy and molecular simulation were used to study the interaction mechanism of triazole compounds 1-benzyl-4-phenyl-1,2,3-triazole (BPT) and human serum albumin (HSA). Synchronous fluorescence spectra and three-dimensional fluorescence were used to investigate the effect of BPT on the conformation of HSA. Studies have shown that addition of BPT induces changes in the conformation of HSA; the hydrophobicity of the environment inside the HSA residues is enhanced. Using molecular modeling techniques, it was confirmed that the binding site of BPT was subdomain IIA of HSA, suggesting hydrogen bonding between BPT and Arg222 on HSA.