Fragment-based discovery of BACE1 inhibitors using functional assays

Biochemistry. 2009 Nov 17;48(45):10743-51. doi: 10.1021/bi901061a.

Abstract

Novel nonpeptidic inhibitors of beta-secretase (BACE1) have been discovered by employing a fragment-based biochemical screening approach. A diverse library of 20000 low-molecular weight compounds were screened and yielded 26 novel hits that were confirmed by biochemical and surface plasmon resonance secondary assays. We describe here fragment inhibitors cocrystallized with BACE1 in a flap open and flap closed conformation as determined by X-ray crystallography.

MeSH terms

  • Amyloid Precursor Protein Secretases / antagonists & inhibitors*
  • Aspartic Acid Endopeptidases / antagonists & inhibitors*
  • Crystallography, X-Ray
  • Models, Molecular
  • Molecular Structure
  • Protease Inhibitors / chemistry
  • Protease Inhibitors / pharmacology*

Substances

  • Protease Inhibitors
  • Amyloid Precursor Protein Secretases
  • Aspartic Acid Endopeptidases
  • BACE1 protein, human

Associated data

  • PDB/3HVG
  • PDB/3HW1