论文部分内容阅读
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。
Objective To study the binding of curcumin C0817 to Hsp90 and its inhibitory effect on Hsp90-ATPase activity. Methods Fluorescence spectroscopy was used to study the interaction between C0817 and Hsp90 at different concentrations. The excitation wavelength of 280 nm was selected in the experiment, and the fluorescence spectra were scanned within 290-510 nm. The malachite green phosphomolybdate ammonium-inorganic phosphorus assay was used to study the inhibitory effect of C0817 on the activity of Hsp90-ATPase. Results The dissociation constant of C0817 was (24.740 ± 1.752) μmol·L-1. The main force between C0817 and Hsp90 was electrostatic force. The conformation of Hsp90 was changed by the presence of C0817. When ATP was 1 mmol·L-1, C0817 has no inhibitory effect on Hsp90-ATPase activity. Conclusions After fluorescence spectroscopy, the binding mechanism of C0817 to Hsp90 can be determined.