中国药理学通报Issue(10)：1408-1413,6.DOI:10.3969/j.issn.1001-1978.2014.10.017
姜黄素衍生物C085与Hsp90及其不同片段相互作用以及对Hsp90 ATPase活性的影响
Interactions between curcumin derivatives C085 and various constructs of Hsp90 and effects of C085 on Hsp90 ATPase activity
摘要
Abstract
Aim To estimate the affinity between C085 and Hsp90 and the inhibitory effects of C085 on the activity of Hsp90 ATPase. Methods The fluores-cence spectrum experiment was applied to examine the affinity between different C085 concentrations and Hsp90 , NHsp90 , MHsp90 , CHsp90; fluorescence in-tensities were recorded in the range of 290-510 nm at 293 K, 303 K and 310 K, respectively;a colorimetric assay for inorganic phosphate based on the formation of a phosphomolybdate complex and subsequent reaction with malachite green was used to examine the inhibitory effects of C085 on the activity of Hsp90 ATPase. Re-sults The dissociation constant KD value of C085 was (11. 163 ± 0. 316 ) μmol · L-1 . The interaction be-tween C085 and Hsp90 was driven mainly by electro-static interaction. C085 showed strongest affinity with CHsp90. When the concentration of ATP was 1 mmol· L-1 ,the inhibition of Hsp90 ATPase activity of C085 with the IC50 value was 6. 04μmol·L-1 . Conclusions The interaction mechanism between C085 and Hsp90 can be analyzed by fluorescence spectrum. C085 shows strong inhibition ATPase activity of Hsp90 .关键词
C085/Hsp90/ATPase活性/荧光光谱法/相互作用/抑制作用Key words
C085/Hsp90/ATPase activity/fluores-cence spectrometry/interaction/inhibition分类
医药卫生引用本文复制引用
范莹娟,张连茹,刘洋,许建华..姜黄素衍生物C085与Hsp90及其不同片段相互作用以及对Hsp90 ATPase活性的影响[J].中国药理学通报,2014,(10):1408-1413,6.基金项目
国家自然科学基金资助项目( No 81173096) （ No 81173096）
科技部“重大新药创制”科技重大专项(No 2012ZX09103-101-028)。 （No 2012ZX09103-101-028）
