Fragment-Based Discovery of a Series of Allosteric-Binding Site Modulators of β-Glucocerebrosidase.
Nick PalmerChristopher AgnewCaroline BennWilliam J BuffhamJoan N CastroGianni ChessariMellissa ClarkBenjamin D ConsJoseph E CoyleLee A DawsonChristopher C F HamlettCharlotte HodsonFinn HoldingChristopher N JohnsonJohn W LiebeschuetzPravin MahajanJames M McCarthyChristopher W MurrayMarc O'ReillyTorren PeakmanAmanda PriceMagdalini RaptiJudith ReeksPatrick SchöpfJeffrey D St DenisChiara ValenzanoNicola G WallisReto WalserHeather WeirNicola E WilsherAndrew WoodheadCarla F BentoDominic TisiPublished in: Journal of medicinal chemistry (2024)
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.
Keyphrases
- small molecule
- protein protein
- drug discovery
- induced apoptosis
- heat shock
- high resolution
- mild cognitive impairment
- photodynamic therapy
- cell cycle arrest
- parkinson disease
- cognitive impairment
- genome wide
- amino acid
- cell death
- copy number
- replacement therapy
- oxidative stress
- endoplasmic reticulum stress
- cell proliferation
- dna methylation
- smoking cessation
- magnetic resonance