Structure-activity relationships of benzimidazole-based glutaminyl cyclase inhibitors featuring a heteroaryl scaffold

J Med Chem. 2013 Sep 12;56(17):6613-25. doi: 10.1021/jm4001709. Epub 2013 Aug 19.

Abstract

Glutaminyl cyclase (hQC) has emerged as a new potential target for the treatment of Alzheimer's disease (AD). The inhibition of hQC prevents of the formation of the Aβ3(pE)-40,42 species which were shown to be of elevated neurotoxicity and are likely to act as a seeding core, leading to an accelerated formation of Aβ-oligomers and fibrils. This work presents a new class of inhibitors of hQC, resulting from a pharmacophore-based screen. Hit molecules were identified, containing benzimidazole as the metal binding group connected to 1,3,4-oxadiazole as the central scaffold. The subsequent optimization resulted in benzimidazolyl-1,3,4-thiadiazoles and -1,2,3-triazoles with an inhibitory potency in the nanomolar range. Further investigation into the potential binding mode of the new compound classes combined molecular docking and site directed mutagenesis studies.

MeSH terms

  • Aminoacyltransferases / antagonists & inhibitors*
  • Aminoacyltransferases / chemistry
  • Benzimidazoles / chemistry*
  • Benzimidazoles / pharmacology*
  • Molecular Docking Simulation
  • Spectrometry, Mass, Electrospray Ionization
  • Structure-Activity Relationship

Substances

  • Benzimidazoles
  • Aminoacyltransferases
  • glutaminyl-peptide cyclotransferase