Design, synthesis and biological evaluation of novel imidazo[4,5-c]pyridinecarboxamide derivatives as PARP-1 inhibitors

Bioorg Med Chem Lett. 2013 Apr 1;23(7):1993-6. doi: 10.1016/j.bmcl.2013.02.032. Epub 2013 Feb 16.

Abstract

A series of novel cyclic amine-substituted imidazo[4,5-c]pyridinecarboxamide analogs were designed and synthesized. All the target compounds were evaluated for their PARP inhibition activity, and the result indicated that most of the compounds possessed inhibitory effect on PARP at the concentration of 1μM, among which compound 8d (IC50=0.528 μM) was selected for evaluating the antitumor effect in vivo. The result showed the antitumor efficacy of the compound 8d and cisplatin combination group in a mouse A549 model is similar with that of the ABT-888 and cisplatin combination group.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antineoplastic Combined Chemotherapy Protocols / chemical synthesis
  • Antineoplastic Combined Chemotherapy Protocols / chemistry
  • Antineoplastic Combined Chemotherapy Protocols / pharmacology*
  • Cell Line, Tumor
  • Cell Proliferation / drug effects
  • Dose-Response Relationship, Drug
  • Drug Design*
  • Enzyme Inhibitors / chemical synthesis
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / pharmacology*
  • Humans
  • Imidazoles / chemical synthesis
  • Imidazoles / chemistry
  • Imidazoles / pharmacology*
  • Mice
  • Molecular Structure
  • Neoplasms, Experimental / drug therapy*
  • Neoplasms, Experimental / pathology
  • Niacinamide / analogs & derivatives*
  • Niacinamide / chemistry
  • Niacinamide / pharmacology*
  • Poly (ADP-Ribose) Polymerase-1
  • Poly(ADP-ribose) Polymerase Inhibitors*
  • Poly(ADP-ribose) Polymerases / metabolism
  • Structure-Activity Relationship
  • Xenograft Model Antitumor Assays

Substances

  • Enzyme Inhibitors
  • Imidazoles
  • Poly(ADP-ribose) Polymerase Inhibitors
  • Niacinamide
  • PARP1 protein, human
  • Poly (ADP-Ribose) Polymerase-1
  • Poly(ADP-ribose) Polymerases