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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 Tisi
Published 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.
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