Owing to its presence in
several biological processes Sirt1 served as a potential therapeutic target for
many diseases. Here we report the synthesis of two distinct series of novel
Sirt1 selective inhibitors, benzimidazole monopeptides and 5-pyrazolyl
methylidene rhodanine carboxylic acid derived amino acids, constructed using
structure-guided computational approaches. Furthermore, compounds were
evaluated, against human Sirt1-3 for in-vitro inhibitory activity
compared to Ex527 (reported Sirt1-selective inhibitor), in liver and breast cancer cell lines for cytotoxicity. The
tryptophan conjugates 13h (IC50 = 0.66 µM) and 7d (IC50 =
0.77 µM) demonstrated maximum efficacy to inhibit Sirt1. Molecular dynamics
simulations unveil the interaction map and electrostatic complementarity at
substrate binding site, could be a cause of selective Sirt1 inhibition. Furthermore, the Sirt1 inhibition was monitored
via increased p53 acetylation status checked in HepG2 cells. These findings will pave the pathway for developing novel
selective Sirt1-inhibitors in cancer therapeutics.