荧光光谱法研究卡铂与牛血清白蛋白的相互作用.pdfVIP

现代药物与临床 Drugs Clinic 第 31 卷 第 5 期 2016 年 5 月 ·587 · 荧光光谱法研究卡铂与牛血清白蛋白的相互作用 郑茂东，颜 娟，庞茜茜，赵秀花，王爱萍，徐今宁 河北北方学院附属第一医院 药学部，河北 张家口 075000 摘 要：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 3 9.81 ×10 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。 关键词：卡铂；牛血清白蛋白；荧光光谱；同步荧光光谱 中图分类号：R965.2 文献标志码：A 文章编号：1674 - 5515(2016)05 - 0587 - 04 DOI:10.7501/j.issn.1674-5515.2016.05.005 Interaction of carboplatin with bovine serum albumin by fluoresence spectroscopy ZHENG Mao-dong, YAN Juan, PANG Qian-qian, ZHAO Xiu-hua, WANGAi-ping, XU Jin-ning Department of Pharmacy, The First Affiliated Hospital of Hebei North University, Zhangjiakou 075000, China Abstract: 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 3 quenching. The binding constant was 9.81×10 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. K