本文主要通过荧光光谱法与分子对接技术研究了在298, 303, 310 K温度下头孢他啶(CFD)与胰蛋白酶(TRP)之间的作用机制。研究结果表明, CFD与TRP之间是通过1∶1的静态猝灭方式相互作用。依照双对数方程处理荧光猝灭数据得到了CFD与TRP作用的结合常数Ka和结合位点数n。通过热力学方程求得了不同温度下CFD与TRP作用的热力学参数。实验数据表明, 它们之间的作用力主要是疏水作用和氢键作用, 这与分子对接技术所得的结果是一致的。

The binding of ceftazidime (CFD) with trypsin (TRP) was investigated by spectroscopic and molecular docking methods under different temperature conditions (298, 303 and 310 K). The results demonstrate that the interaction between CFD and TRP is taking place via static quenching with 1∶1 binding ratio. The fluorescence data were treated by using the double logarithmic equation, and the binding constants Ka of the interaction of CFD-TRP systems and the number of binding sites n were obtained. The thermodynamic parameters of CFD-TRP systems under different temperatures were obtained by the thermodynamic equation. The experimental data show that the interactions between them are mainly hydrophobic interaction and hydrogen bonding interaction, which is consistent with the molecular docking results.