目的 研究卡鉑與牛血清白蛋白(BSA)在人體生理?xiàng)l件下的相互作用。方法 采用熒光光譜法研究卡鉑與BSA的熒光猝滅機(jī)制、結(jié)合位點(diǎn)數(shù)、結(jié)合常數(shù);利用熱力學(xué)參數(shù)考察其作用力類型;采用同步熒光光譜法探討卡鉑對(duì)BSA構(gòu)象的影響。結(jié)果 卡鉑與BSA形成1:1的復(fù)合物引起B(yǎng)SA的熒光猝滅,其猝滅類型為靜態(tài)猝滅?？ㄣK與BSA結(jié)合位點(diǎn)數(shù)為9.81×10³mol/L,兩者以疏水作用為主?？ㄣK與BSA相互作用使色氨酸殘基所處的微環(huán)境發(fā)生改變。結(jié)論 卡鉑與BSA相互作用形成復(fù)合物,并改變BSA的構(gòu)象。

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.

河北省醫(yī)學(xué)科學(xué)研究重點(diǎn)課題計(jì)劃項(xiàng)目(ZD20140167);張家口市科技局科技計(jì)劃項(xiàng)目(1421132D)