HTRF-based method for determination of HSP90-HOP inhibition activity and its application
10.16438/j.0513-4870.2016-1177
- VernacularTitle:基于均相时间分辨荧光技术(HTRF)的HSP90-HOP相互作用抑制剂活性测试方法的构建及其应用
- Author:
Hui-jie WANG
1
;
Zi-han ZHOU
2
;
Jia-chen XU
1
;
Fen JIANG
1
;
Qi-dong YOU
1
;
Xiao-li XU
1
Author Information
1. Jiang Su Key Laboratory of Drug Design and Optimization, China Pharmaceutical University, Nanjing 210009, China
2. Nanjing Foreign Language School, Nanjing 210008, China
- Publication Type:ORIGINAL ARTICLES
- Keywords:
heat shock protein 90;
HSP-organizing protein;
homogeneous time-resolved fluorescence;
protein-protein interaction
- From:
Acta Pharmaceutica Sinica
2017;52(4):592-597
- CountryChina
- Language:Chinese
-
Abstract:
HSP90 is widely expressed in cells with the main function in assisting the maturation of other proteins that are called clients. Many clients play critical roles in the occurrence and development of cancer. Inhibition of HSP90 can lead to degradation of the oncogenic proteins, and result in potent anti-cancer effects. HSP90-HOP interaction is critical for the chaperone function of HSP90, thereby disruption of the HSP90-HOP interaction is a novel strategy in the inhibition of HSP90. Based on the technology of homogeneous time-resolved fluorescence (HTRF), we developed a new assay for the identification of new inhibitors of HSP90-HOP interaction. This method was evaluated in the study of the HSP90-HOP inhibition activity of the pentapeptide MEEVD from HSP90 C-terminal and its derivatives. This study can provide a basis for the screening and discovery of novel HSP90-HOP disruptors.
