ArticleChemMedChem2026
Synthesis and Evaluation of Iminosugar-Based Analogs of UDP-GlcNAc as Putative OGT Inhibitors.
Article in ChemMedChem, 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
O-GlcNAc transferase (OGT) is an essential mammalian enzyme that regulates numerous cellular processes through the attachment of O-linked N-acetylglucosamine (O-GlcNAc) residues to nuclear and cytoplasmic proteins. Inhibitors of OGT are needed as research tools and for evaluating the potential of OGT as a therapeutic target. As little effort has been made to incorporate mimicry of the glycosyl oxocarbenium character of the OGT transition state, we report herein the synthesis of a series of glycomimetics of the OGT substrate UDP-GlcNAc, in which the GlcNAc motif has been replaced by an imino-C-glycoside and the pyrophosphate moiety has been either conserved, replaced by a squaramide linker, or truncated to remove the terminal phosphate and base. While their affinity for human OGT both in vitro and in cells proved modest (>300 µM), an imino-C-glycoside of α-D-GalNAc-1-phosphate showed, surprisingly, micromolar noncompetitive inhibition of OGT (IC
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