中文摘要：

目的研究姜黄素衍生物C0817与Hsp90的结合作用,及其对Hsp90-ATPase活性抑制作用。方法采用荧光光谱法,研究不同浓度C0817与Hsp90的相互作用;实验选取280 nm为激发波长,290～510 nm内进行荧光光谱扫描。采用孔雀绿磷钼酸铵-无机磷检测法,研究C0817对Hsp90-ATPase活性的抑制。结果 C0817解离常数为（24.740±1.752）μmol·L^-1 ;C0817与Hsp90之间的主要作用力为静电作用力;C0817的存在使得Hsp90构象改变;当ATP为1 mmol·L^-1 时,C0817对Hsp90-ATPase活性无抑制作用。结论经过荧光光谱分析,可以确定C0817与Hsp90的结合机制。

英文摘要：

OBJECTIVE To estimate the interaction between C0817 and Hsp90 and the inhibitory effects C0817 on the activity Hsp90 ATPase. METHODS The fluorescent spectrometry method was applied to examine the affinity between different concentrations C0817 and Hsp90; fluorescence intensities were recorded in the range 290- 510 nm at 293 K,303 K and 310 K,respectively; colorimetric assay for inorganic phosphate based on the formation a phosphomolybdate complex and subsequent reaction with malachite green was used to examine the inhibitory effects C0817 on the activity Hsp90 ATPase. RESULTS The dissociation constant KDvalue C0817was（ 24. 740 ± 1. 752） μmol·L^-1 . The interaction between C0817 and Hsp90 was driven mainly by electrostatic interaction. When the concentration ATP was 1 mmol · L^-1 ,C0817 could not inhibit the ATPase activity Hsp90. CONCLUSION The interaction mechanism between C0817 and Hsp90 can be analyzed by fluorescence spectrum. C0817 doesn＇ t show inhibitory action for ATPase Hsp90.