Fragment-Based Discovery of a Series of Allosteric-Binding Site Modulators of β-Glucocerebrosidase

J Med Chem. 2024 Jul 11;67(13):11168-11181. doi: 10.1021/acs.jmedchem.4c00702. Epub 2024 Jun 27.

Abstract

β-Glucocerebrosidase (GBA/GCase) mutations leading to misfolded protein cause Gaucher's disease and are a major genetic risk factor for Parkinson's disease and dementia with Lewy bodies. The identification of small molecule pharmacological chaperones that can stabilize the misfolded protein and increase delivery of degradation-prone mutant GCase to the lysosome is a strategy under active investigation. Here, we describe the first use of fragment-based drug discovery (FBDD) to identify pharmacological chaperones of GCase. The fragment hits were identified by using X-ray crystallography and biophysical techniques. This work led to the discovery of a series of compounds that bind GCase with nM potency and positively modulate GCase activity in cells.

MeSH terms

  • Allosteric Site*
  • Crystallography, X-Ray
  • Drug Discovery*
  • Glucosylceramidase* / antagonists & inhibitors
  • Glucosylceramidase* / chemistry
  • Glucosylceramidase* / metabolism
  • Humans
  • Models, Molecular
  • Small Molecule Libraries / chemistry
  • Small Molecule Libraries / metabolism
  • Small Molecule Libraries / pharmacology
  • Structure-Activity Relationship

Substances

  • Glucosylceramidase
  • Small Molecule Libraries