磷脂与Hsp90相互作用的荧光和红外光谱

摘要

To investigate the mechanism underlying the interaction between phosphatidylcholine ( PC) and heat shock protein 90 ( Hsp90) , the fluorescence spectroscopy and infrared spectroscopy were applied to study the changes of in-trinsic fluorescence of Hsp90 and major groups of phosphatidylcholine respectively. The results showed PC was found to have a strong ability to quench the intrinsic fluorescence of Hsp90. It was a static quenching as the result of the formation of PC-Hsp90 complex. The number of binding sites was 0. 92, and based on Van’ t Hoff equation, the binding of PC to Hsp90 was driven mainly by hydrogen bond and Van der Waals forces. The infrared spectroscopy indicated the binding of Hsp90 and PC took place in the polar headgroup and nonpolar fatty acid side chains of PC, and the structure of PC molecules changed. In conclusion, PC could stably bind with Hsp90.%为研究磷脂酰胆碱（ PC）与热休克蛋白90（ Hsp90）的相互作用机制，分别采用荧光光谱和红外光谱法研究Hsp90内源荧光的变化和磷脂主要基团的变化。结果显示：PC对Hsp90内源荧光有较强的猝灭作用，PC对Hsp90的猝灭属于形成复合物产生的静态猝灭，结合位点数为0.92，结合的主要作用力为氢键和范德华力；Hsp90与PC的相互作用发生在磷脂极性头端和非极性侧链上，并使磷脂的结构发生改变。磷脂可以稳定地与Hsp90结合。