AI Article Synopsis
- - A new class of compounds has been identified as effective inhibitors of the enzyme O-GlcNAcase, which is important for removing sugar molecules from proteins.
- - These inhibitors are unique because they are structurally related to the enzyme's transition state, meaning they fit well into the enzyme's active site, and they can bind reversibly.
- - The compounds are easy to make, highly active, stable, and non-toxic, making them potential candidates for developing treatments aimed at reducing tau phosphorylation, a key factor in Alzheimer's disease.
Article Abstract
A new class of compounds, namely highly substituted diaminocyclopentane-l-lysine adducts, have been discovered as potent inhibitors of O-GlcNAcase, an enzyme crucial for protein de-O-glycosylation. These inhibitors exhibit exceptional selectivity and reversibility and are the first example of human O-GlcNAcase inhibitors that are structurally related to the transition state of the rate-limiting step with the "aglycon" still in bond-length proximity. The ease of their preparation, remarkable biological activities, stability, and non-toxicity make them promising candidates for the development of anti-tau-phosphorylation agents holding significant potential for the treatment of Alzheimer's disease.
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| http://dx.doi.org/10.1016/j.bioorg.2024.107452 | DOI Listing |
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