荧光光谱法研究卡铂与牛血清白蛋白的相互作用

目的研究卡铂与牛血清白蛋白(BSA)在人体生理条件下的相互作用。方法采用荧光光谱法研究卡铂与BSA的荧光猝灭机制、结合位点数、结合常数;利用热力学参数考察其作用力类型;采用同步荧光光谱法探讨卡铂对BSA构象的影响。结果卡铂与BSA形成1∶1的复合物引起BSA的荧光猝灭,其猝灭类型为静态猝灭。卡铂与BSA结合位点数为9.81×103 mol/L,两者以疏水作用为主。卡铂与BSA相互作用使色氨酸残基所处的微环境发生改变。结论卡铂与BSA相互作用形成复合物,并改变BSA的构象。

Interaction of carboplatin with bovine serum albumin by fluoresence spectroscopy

Objective To study the interaction between carboplatin with bovine serum albumin (BSA) under the simulative human physiological condition. Methods The interaction mechanism of BSA with carboplatin was investigated by fluorescence spectrophotometry. Binding site, the binding constant, and the interaction force were studied. The effects of their interaction on conformation change of BSA were investigated by synchronous fluorescence. Results The complex formed between carboplatin and BSA with the radio of 1:1 caused fluorescence quenching of BSA, and the mechanism of fluorescence quenching was static quenching. The binding constant was 9.81×10³ L/mol and the interaction was mainly driven by hydrophobic action. The binding site between carboplatin and BSA was closer to tryptophan residues and the interaction changed the environments of amide acid residues. Conclusion Carboplatin with BSA can form complex, and change the conformation of BSA.