5-Aminomethylbenzimidazoles as potent ITK antagonists

Bioorg Med Chem Lett. 2009 Mar 15;19(6):1588-91. doi: 10.1016/j.bmcl.2009.02.012. Epub 2009 Feb 8.

Abstract

Benzamide 1 demonstrated good potency as a selective ITK inhibitor, however the amide moiety was found to be hydrolytically labile in vivo, resulting in low oral exposure and the generation of mutagenic aromatic amine metabolites. Replacing the benzamide with a benzylamine linker not only addressed the toxicity issue, but also improved the cellular and functional potency as well as the drug-like properties. SAR studies around the benzylamines and the identification of 10n and 10o as excellent tools for proof-of-concept studies are described.

MeSH terms

  • Animals
  • Benzimidazoles / chemical synthesis*
  • Benzimidazoles / pharmacology
  • CD3 Complex / biosynthesis
  • Chemistry, Pharmaceutical / methods*
  • Drug Design
  • Enzyme Inhibitors / chemical synthesis*
  • Enzyme Inhibitors / pharmacology
  • Female
  • Hepatocytes / metabolism
  • Humans
  • Inhibitory Concentration 50
  • Mice
  • Mice, Inbred BALB C
  • Protein-Tyrosine Kinases / antagonists & inhibitors*
  • Rats
  • Rats, Sprague-Dawley
  • Structure-Activity Relationship

Substances

  • Benzimidazoles
  • CD3 Complex
  • Enzyme Inhibitors
  • benzimidazole
  • Protein-Tyrosine Kinases
  • emt protein-tyrosine kinase