文献类型：期刊文献

中文题名：Triazole and Benzotriazole Derivatives as Novel Inhibitors for p90 Ribosomal S6 Protein Kinase 2： Synthesis, Molecular Docking and SAR Analysis

英文题名：Triazole and Benzotriazole Derivatives as Novel Inhibitors for p90 Ribosomal S6 Protein Kinase 2： Synthesis, Molecular Docking and SAR Analysis

作者：Jun Yuan[1];Ye Zhong[1];Shiliang Li[1];Xue Zhao[1];Guoqin Luan[1];Zhenjiang Zhao[1];Jin Huang[1];Honglin Li[1];Yufang Xu[1]

机构：[1]Shanghai Key Laboratory of New Drug Design, State Key Laboratory of Bioreactor Engineering, School of Pharmacy, East China University of Science & Technology, Shanghai 200237, China

年份：2013

卷号：31

期号：9

起止页码：1192

中文期刊名：Chinese Journal of Chemistry

外文期刊名：中国化学（英文版）

收录：CSTPCD;;Scopus;CSCD:【CSCD2013_2014】；

基金：The research is supported in part by the Fundamental Research Funds for the Central Universities,the National Natural Science Foundation of China，the Shanghai Committee of Science and Technology

语种：英文

中文关键词：RSK2;structure-activity relationships;molecular docking

外文关键词：RSK2;structure-activity relationships;molecular docking

摘要：A series of triazole and benzotriazole derivatives as novel p90 ribosomal S6 protein kinase 2 （RSK2） inhibitors were designed and synthesized. The in vitro activities against RSK2 were evaluated, and among 14 compounds, compounds 5, 6, 11, 12, 13 and 14 exhibited enzyme IC50 values of 8.91, 2.86, 3.19, 3.05, 4.49 and 2.09 μmol/L re- spectively. The proposed binding modes were simulated using molecular docking method, and the docking results coupled with the stmcture-activi1：y relationship （SAR） analysis indicated that all these active compounds bound to the RSK2 ATP binding site at NTKD, and the electron-donating groups on the 4-position of phenyl were the deter- minant point for the inhibitory activity.
A series of triazole and benzotriazole derivatives as novel p90 ribosomal S6 protein kinase 2 （RSK2） inhibitors were designed and synthesized. The in vitro activities against RSK2 were evaluated, and among 14 compounds, compounds 5, 6, 11, 12, 13 and 14 exhibited enzyme IC50 values of 8.91, 2.86, 3.19, 3.05, 4.49 and 2.09 μmol/L re- spectively. The proposed binding modes were simulated using molecular docking method, and the docking results coupled with the stmcture-activi1：y relationship （SAR） analysis indicated that all these active compounds bound to the RSK2 ATP binding site at NTKD, and the electron-donating groups on the 4-position of phenyl were the deter- minant point for the inhibitory activity.