ArticleACS medicinal chemistry letters2026
Design and Optimization of Benzoic Acid Inhibitors Targeting the EBNA1 DNA-Binding Interface.
Article in ACS medicinal chemistry letters, 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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Abstract
Epstein-Barr nuclear antigen 1 (EBNA1) is an essential viral DNA-binding protein required for maintenance of Epstein-Barr virus (EBV) episomes and is expressed in all EBV-associated malignancies, making it an attractive therapeutic target. Using fragment-based screening and X-ray crystallography, we identified a 2,3-disubstituted benzoic acid scaffold that binds at the EBNA1 DNA-binding interface. Structure-guided optimization revealed that the carboxylic acid pharmacophore engages Asn519 and Thr590, while electron-rich heterocycles are positioned between Lys477 and Lys586, forming a cation-π-cation "lysine sandwich" that drives potency. Iterative medicinal chemistry improved binding affinity and physicochemical stability, leading to compound
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