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Most bromodomain inhibitors mimic the interactions of the natural acetylated lysine (KAc) histone substrate through key interactions with conserved asparagine and tyrosine residues within the binding pocket. Herein we report the optimization of a series of phenyl sulfonamides that exhibit a novel mode of binding to non-bromodomain and extra terminal domain (non-BET) bromodomains through displacement of a normally conserved network of four water molecules. Starting from an initial hit molecule, we report its divergent optimization toward the ATPase family AAA domain containing 2 (ATAD2) and cat eye syndrome chromosome region, candidate 2 (CECR2) domains. This work concludes with the identification of (R)-55 (GSK232), a highly selective, cellularly penetrant CECR2 inhibitor with excellent physicochemical properties.
One of the oldest and most widely used commercial enzyme inhibitors is aspirin, Safety of 2-(Benzofuran-3-yl)acetic acid, which selectively inhibits one of the enzymes involved in the synthesis of molecules that trigger inflammation. you can also check out more blogs about 64175-51-5
Reference：
Benzofuran – Wikipedia,
Benzofuran | C8H2674O – PubChem