In the November 2010 issue of the high impact journal Nature Reviews Drug Discovery, the News&Analysis column has been entirely devoted to the growing interest in targeting protein misfolding to therapeutically treat both rare and common diseases. The column highlights amongst others reMYND’s technology platform and the recently announced Roche-reMYND collaboration for the development of first-in-class disease-modifying treatments for Parkinson's and Alzheimer's disease.
Excerpt from Nature Reviews Drug Discovery 9, 825-827 (November 2010):
Two recent deals highlight growing interest in therapeutically targeting protein misfolding to treat both rare and common diseases.
In September 2010, Pfizer announced plans to acquire the biotech company FoldRx Pharmaceuticals (…). In the same month, Roche announced a new strategic alliance with the biotech company reMYND — which is also focused on protein-misfolding disorders — under which the two companies will collaborate to develop novel therapies for Parkinson’s disease (PD) and Alzheimer’s disease (AD).
(…) Roche says that reMYND’s focus complements its own in-house activities. “At Roche we have a major interest in neurodegeneration and already have antibodies against misfolded amyloid-β protein in Phase I clinical development for AD,” says Hansruedi Loetscher, Head of Molecular Neuroscience, Central Nervous System Discovery, Roche. “The approach taken by reMYND is based on a completely different mechanism, and against different targets.”
(…) Efforts are also being directed towards harnessing the power of protein-destroying pathways. This is the strategy taken by reMYND, which has developed small-molecule compounds that bind to intracellular targets in the endosomal–lysosomal sorting pathway and facilitate proteolytic degradation of specific misfolded, toxic proteins. reMYND currently has four compound series in preclinical development for AD, two for PD and two for type 2 diabetes. “This small-molecule approach complements Roche’s antibody-based strategy for targeting aggregates of misfolded proteins in neurodegenerative diseases,” says Loetscher.
Source: Nature Reviews Drug Discovery 9, 825-827 (November 2010) | doi:10.1038/nrd3316.