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The identification, synthesis and evaluation of a series of rhodanine and thiazolidin-2,4-dione derivatives as selective inhibitors of human arylamine N-acetyltransferase 1 and mouse arylamine N-acetyltransferase 2 is described. The most potent inhibitors identified have submicromolar activity and inhibit both the recombinant proteins and human NAT1 in ZR-75 cell lysates in a competitive manner. (1)H NMR studies on purified mouse Nat2 demonstrate that the inhibitors bind within the putative active site of the enzyme.

Original publication




Journal article


Bioorg Med Chem

Publication Date





905 - 918


Animals, Arylamine N-Acetyltransferase, Binding Sites, Biomarkers, Tumor, Breast Neoplasms, Enzyme Inhibitors, Female, Humans, Isoenzymes, Mice, Rhodanine, Thiazolidinediones