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• W2793313601 abstract "Sirtuins are protein deacylases that regulate metabolism and stress responses and are implicated in aging-related diseases. Modulators of the human sirtuins Sirt1-7 are sought as chemical tools and potential therapeutics, e.g., for cancer. Selective and potent inhibitors are available for Sirt2, but selective inhibitors for Sirt5 with Ki values in the low nanomolar range are lacking. We synthesized and screened 3-arylthiosuccinylated and 3-benzylthiosuccinylated peptide derivatives yielding Sirt5 inhibitors with low-nanomolar Ki values. A biotinylated derivative with this scaffold represents an affinity probe for human Sirt5 that is able to selectively extract this enzyme out of complex biological samples like cell lysates. Crystal structures of Sirt5/inhibitor complexes reveal that the compounds bind in an unexpected manner to the active site of Sirt5." @default.
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• W2793313601 date "2018-03-01" @default.
• W2793313601 modified "2023-10-17" @default.
• W2793313601 title "Potent and Selective Inhibitors of Human Sirtuin 5" @default.
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• W2793313601 doi "https://doi.org/10.1021/acs.jmedchem.7b01648" @default.
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