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运用紫外光谱、荧光光谱和圆二色谱研究了具有抗癌活性的N-(2-亚甲基吡啶)脱氢枞胺希夫碱(L)及其铜配合物[Cu(L)2Br]Br(1)在模拟生理条件(p H值7.2)下与牛血清白蛋白(BSA)的相互作用,分析了它们之间相互作用的机制。结果表明,1对BSA的荧光猝灭方式为静态猝灭,L为动态猝灭;通过计算得到了不同温度下的结合常数(Ka)、结合位点数(n)及相关的热力学参数(ΔG<0、ΔH>0和ΔS>0),表明L和1与BSA的相互作用力以疏水作用为主,且结合反应是由焓和熵驱动的自发过程。同步荧光光谱分析表明,化合物与BSA的作用使蛋白质的构象发生改变,圆二色谱也证明了化合物能够显著改变BSA的构象,由典型的α-螺旋结构变为扭曲链。
The anticancer activity of N- (2-methylenepyridine) dehydroabietylamine Schiff base (L) and its copper complex [Cu (L) 2Br] Br were studied by UV spectrum, fluorescence spectrum and circular dichroism (1) Interaction with bovine serum albumin (BSA) under simulated physiological conditions (p H value 7.2), and the mechanism of their interaction was analyzed. The results showed that the fluorescence quenching mode of BSA was static quenching and L was dynamic quenching. The binding constants (Ka), number of binding sites (n) and related thermodynamic parameters (ΔG < 0, ΔH> 0 and ΔS> 0), indicating that the interaction between L and 1 and BSA is dominated by hydrophobic interaction, and the binding reaction is a spontaneous process driven by enthalpy and entropy. Simultaneous fluorescence spectroscopy analysis showed that the conformation of the protein was changed by the interaction of BSA with the compound, and circular dichroism also demonstrated that the compound can significantly change the conformation of BSA from a typical α-helical structure to a twisted chain.