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• W3004905117 abstract "The sirtuin enzymes are potential drug targets for intervention in a series of diseases. Efforts to inhibit enzymes of this class with thioamide- and thiourea-containing, substrate-mimicking entities have produced a number of high-affinity binders. However, less attention has been dedicated to the investigation of the stability of these inhibitors under various conditions. Here, we provide evidence of an unprecedented degree of cleavage of short-chain ε-N-thioacyllysine modifications meant to target these sirtuins and further provide insights into the serum stability of compounds containing both thioamides and thioureas. Our study questions the utility short-chain thioamide-based inhibitors of sirtuins for drug development and points to monoalkylated thiourea-based chemotypes as being more stable in human serum." @default.
• W3004905117 created "2020-02-14" @default.
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• W3004905117 date "2020-02-06" @default.
• W3004905117 modified "2023-10-09" @default.
• W3004905117 title "Dethioacylation by Sirtuins 1–3: Considerations for Drug Design Using Mechanism-Based Sirtuin Inhibition" @default.
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• W3004905117 doi "https://doi.org/10.1021/acsmedchemlett.9b00580" @default.
• W3004905117 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7549274" @default.
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