Emrusolmin

Emrusolmin (Anle138b), an oligomeric aggregation inhibitor, blocks the formation of pathological aggregates of prion protein (PrPSc) and of α-synuclein (α-syn). Emrusolmin strongly inhibits oligomer accumulation, neuronal degeneration, and disease progression in vivo. Emrusolmin has low toxicity and an excellent oral bioavailability and blood-brain-barrier penetration. Emrusolmin blocks Aβ channels and rescues disease phenotypes in a mouse model for amyloid pathology^[1][2]. In Vitro:Oligomeric aggregates are presumed to be the key neurotoxic agent. Emrusolmin blocksthe formation of pathological aggregates of prion protein and of α-synuclein, which is deposited in Parkinson’s disease and other synucleinopathies such as dementia with Lewy bodies and multiple system atrophy. Emrusolmin strongly inhibits all prion strains tested including BSE-derived and human prions. Emrusolmin shows structure-dependent binding to pathological aggregates and strongly inhibits formation of pathological oligomers both for prion protein and α-synuclein^[1]. In Vivo:Emrusolmin shows structure-dependent binding to pathological aggregates and strongly inhibits formation of pathological oligomers in vitro and in vivo both for prion protein and α-synuclein^[1].
Emrusolmin (0.6-2 g/kg; p.o.) modulates α-synuclein oligomerization^[3].