期刊
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
卷 28, 期 9, 页码 1490-1494出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmcl.2018.03.083
关键词
Epigenetics; Histone lysine demethylase; KDM5; Tri-methylated H3K4; Structure-based design
Histone lysine demethylases (KDMs) play a key role in epigenetic regulation and KDM5A and KDM5B have been identified as potential anti-cancer drug targets. Using structural information from known KDM4 and KDM5 inhibitors, a potent series of pyrazolylpyridines was designed. Structure-activity relationship (SAR) exploration resulted in the identification of compound 33, an orally available, potent inhibitor of KDM5A/5B with promising selectivity. Potent cellular inhibition as measured by levels of tri-methylated H3K4 was demonstrated with compound 33 in the breast cancer cell line ZR-75-1. (C) 2018 Elsevier Ltd. All rights reserved.
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