ArticleACS omega2026
Fragment-Based Discovery of BRD4-BD2 Selective Binders: Biophysical Validation and Structural Insights for Domain-Selective Inhibitor Design.
Article in ACS omega, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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8 authors.
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Abstract
BRD4, a member of the bromodomain and extra-terminal (BET) family of epigenetic readers, plays a central role in transcriptional regulation and is implicated in a wide spectrum of diseases. Although BRD4 inhibitors targeting both bromodomains have advanced into clinical studies, their development and therapeutic use are limited by dose-limiting toxicities associated with nonselective BET inhibition. These limitations underscore the need for domain-selective targeting strategies. In this study, we performed fragment-based screening of a 200-compound diversity library against BRD4-BD2, identifying three chemically distinct hits: CCBT-T-226 (methyl 2-(2-(3,5-dimethylisoxazol-4-yl)-acetamido)-5-propylthiazole-4-carboxylate), CCBT-F-70 (2-(benzylamino)-pyrimidin-4-(3H)-one), and CCBT-F-182 (3-(8-methyl-3,8a-dihydroimidazo-[1,2-
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