Identification of 2,3-dihydro-1H-pyrrolo[3,4-c]pyridine-derived ureas as potent inhibitors of human nicotinamide phosphoribosyltransferase (NAMPT)

Bioorg Med Chem Lett. 2013 Sep 1;23(17):4875-85. doi: 10.1016/j.bmcl.2013.06.090. Epub 2013 Jul 6.

Abstract

Potent nicotinamide phosphoribosyltransferase (NAMPT) inhibitors containing 2,3-dihydro-1H-pyrrolo[3,4-c]pyridine-derived ureas were identified using structure-based design techniques. The new compounds displayed improved aqueous solubilities, determined using a high-throughput solubility assessment, relative to previously disclosed urea and amide-containing NAMPT inhibitors. An optimized 2,3-dihydro-1H-pyrrolo[3,4-c]pyridine-derived compound exhibited potent anti-NAMPT activity (18; BC NAMPT IC50 = 11 nM; PC-3 antiproliferative IC50 = 36 nM), satisfactory mouse PK properties, and was efficacious in a PC-3 mouse xenograft model. The crystal structure of another optimized compound (29; NAMPT IC50 = 10nM; A2780 antiproliferative IC50 = 7 nM) in complex with the NAMPT protein was also determined.

Keywords: Aqueous solubility; NAMPT; Nicotinamide phosphoribosyltransferase; Tumor metabolism; X-ray crystal structure.

MeSH terms

  • Animals
  • Antineoplastic Agents / chemistry*
  • Antineoplastic Agents / pharmacokinetics
  • Antineoplastic Agents / pharmacology
  • Antineoplastic Agents / therapeutic use*
  • Cell Line, Tumor
  • Cytokines / antagonists & inhibitors*
  • Cytokines / metabolism
  • Humans
  • Mice
  • Mice, Nude
  • Models, Molecular
  • Neoplasms / drug therapy
  • Neoplasms / enzymology
  • Nicotinamide Phosphoribosyltransferase / antagonists & inhibitors*
  • Nicotinamide Phosphoribosyltransferase / metabolism
  • Pyridines / chemistry*
  • Pyridines / pharmacokinetics
  • Pyridines / pharmacology
  • Pyridines / therapeutic use*
  • Structure-Activity Relationship
  • Urea / chemistry*
  • Urea / pharmacokinetics
  • Urea / pharmacology
  • Urea / therapeutic use*

Substances

  • Antineoplastic Agents
  • Cytokines
  • Pyridines
  • Urea
  • Nicotinamide Phosphoribosyltransferase
  • nicotinamide phosphoribosyltransferase, human