In the current study, bivalent compounds 1–17 constructed by covalently linking the ?-amino group of lysine in a tripeptidic scaffold to a functionality via a linker were prepared and examined for their inhibitory potencies against SIRT1, a prototypical member of the β-nicotinamide adenine dinucleotide (β-NAD+)-dependent sirtuin family of protein Nε-acyl-lysine deacylases. A few of them were found to be stronger SIRT1 inhibitors than the N?-acetyl-lysine-containing monovalent counterparts 18 and 19. As exemplified with compounds 6 and 18, a bivalent SIRT1 inhibitor could exhibit a greater degree of inhibitory selectivity among SIRT1/2/3 than the corresponding monovalent counterpart. This study has laid a foundation for the future development of superior bivalent inhibitors against the (patho)physiologically and therapeutically important sirtuin family of deacylase enzymes.
Synthesis and Reactions of 2-Mercaptobenzothiazole Derivatives of Expected Biological Activity. 2
The amides and anilides of benzothiazol-2-ylthioacetic acid and 3-(benzothiazol-2-ylthio)propanoic acid were prepared by the reaction of the corresponding acid chlorides with amines and anilines.Also the arylhydrazones, the cycloalkanone hydrazones, and pyrazoline derivatives were prepared.
Hammam, Abou El-Fotooh G.,Youssif, Nabil M.
p. 207 - 208
(2007/10/02)
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