中文摘要：

目的研究抗结核药对氨基水杨酸的希夫碱（PAS-Schiff）的化学表征及其与牛血清蛋白（BSA）的作用。方法以水杨醛和PAS为原料合成了水杨醛缩对氨基水杨酸Schiff碱,通过元素分析、IR、1H-NMR等手段对其结构进行了表征。采用荧光光谱法研究了水杨醛缩对氨基水杨酸Schiff碱与BSA的相互作用。结果得到抗结核药PAS-Schiff碱,该化合物与牛血清蛋白的结合使蛋白的荧光被猝灭,得出15℃、25℃和35℃的两者结合常数为2.72×105,2.08×105,7.55×104L/mol,且结合位点数均为1。通过计算其与牛血清蛋白的热力学参数得出两者间相互作用为典型的疏水作用过程。结论化学表征表明得到新型PAS-Schiff碱化合物,并得出其与牛血清蛋白是通过疏水作用相结合,由此可建立其与BSA的结合模型。

英文摘要：

Objective To investigate the characterization of p-aminosalicylic acid（PAS）-Schiff as a new antimyobacterial drug and its interaction with bovine serum albumin（BSA）.Methods Schiff base was prepared with salicylaldehyde and 4-aminosalicylic acid as materials.The complex was measured by elemental analysis,IR and 1 H-NMR.The interaction between Schiff base and bovine serum albumin （BSA） was studied by fluorescence spectra.Results Schiff base was successfully obtained.The combination of BSA with the complex was a static quenching procedure.The conditional stability constant was 2.72×105,2.08×105,7.55×104 mol/L at 15℃,25℃and 35℃,respectively,and the number of binding site was one at 15℃,25℃and 35℃.Meanwhile,the interaction was mainly driven by hydrophobic force between Schiff base and BSA.Conclusion The results suggest that a new PAS-Schiff base is obtained and the binding force between Schiff base and BSA is hydrophobic.The binding model could be demonstrated by the binding parameters of schiff base and BSA.