| Literature DB >> 31789032 |
Fei Jiang1,2, Qinghua Hu1, Zhimin Zhang1,3, Hongmei Li1,2, Huili Li1, Dewei Zhang1, Hanwen Li1, Yu Ma1, Jingjing Xu4, Haifang Chen1, Yong Cui1, Yanle Zhi1, Yanmin Zhang1, Junyu Xu1, Jiapeng Zhu4, Tao Lu1,2, Yadong Chen1,2.
Abstract
The bromodomain and extra-terminal domain (BET) family of proteins are readers which specifically recognize histone-acetylated lysine residues. Each BET bromodomain protein contains two highly homologous domains: the first bromodomain (BD1) and the second bromodomain (BD2). Pan-BET bromodomain inhibition is a potential therapy for various cancers and immune-inflammatory diseases, but only few reported inhibitors show selectivity within the BET family. Herein, we identified a series of benzo[cd]indol-2(1H)-ones and pyrrolo[4,3,2-de]quinolin-2(1H)-ones with good selectivity for BET BD1. Through structure-based optimization, highly active and selective compounds are ultimately obtained. The representative compounds are the first reported inhibitors with selectivity more than 100-fold for BRD4(1) over BRD4(2). Among them, we further show that 68 (LT052) mediates BRD4/NF-κB/NLRP3 signaling inflammatory pathways with comparable protein expression and significantly improves symptoms of gout arthritis in a rat model. Therefore, selective pharmacological modulation of individual bromodomains could represent a strategy for the treatment of acute gouty arthritis.Entities:
Year: 2019 PMID: 31789032 DOI: 10.1021/acs.jmedchem.9b01010
Source DB: PubMed Journal: J Med Chem ISSN: 0022-2623 Impact factor: 7.446