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Journal Article
Research Support, Non-U.S. Gov't
Cyclic peptide-based potent and selective SIRT1/2 dual inhibitors harboring N(ε)-thioacetyl-lysine.
Bioorganic & Medicinal Chemistry Letters 2016 November 2
In the current study, we discovered that several N-terminus-to-side chain cyclic tripeptides harboring the catalytic mechanism-based SIRT1/2/3 inhibitory warhead N(ε)-thioacetyl-lysine at their central positions exhibited a comparably strong inhibition (nM level) against the SIRT1/2-catalyzed N(ε)-acetyl-lysine deacetylation reactions. Their dual SIRT1/2 inhibitory action was also found to be stronger than that against SIRT3/5/6. Considering the previous demonstration that a SIRT1/2 dual inhibition could be instrumental in achieving an anti-cancer effect on those cancers retaining the wild-type tumor suppresser p53 protein, these compounds could be employed as leads for developing novel anti-cancer agents.
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