News Release (Apr 22, 2014)
GAIM molecules can not only prevent the formation of new toxic protein aggregates but can also clear existing aggregates in the form of both soluble oligomers and insoluble fibers, such as plaques and tangles."The research published today describes GAIM, NeuroPhage's unique approach to treat diseases characterized by misfolded proteins. GAIM has the potential to provide a more robust response than previous therapies because it enables the simultaneous targeting of multiple pathologies within a single disease," said Dr. Richard Fisher, Chief Scientific Officer at NeuroPhage.
"Symptoms of neurodegenerative diseases often appear well after the troublesome aggregates have begun to accumulate in the brain. By then, therapies that only target newly forming aggregates are likely to only slow the progression of the disease and are believed to be too late once the aggregates are formed," said Dr. Gregory A. Petsko, Professor of Neurology at Weill Cornell Medical College in New York City, and Tauber Professor of Biochemistry and Chemistry, Emeritus, at Brandeis University in Waltham, Massachusetts.
"Therapies based on GAIM would represent a completely new paradigm in the treatment of many neurodegenerative diseases with their potential to ameliorate existing symptoms and prevent disease progression. The hope is this will eventually lead to a real treatment for Alzheimer's disease, but for now, the science behind it is quite compelling."
The discovery of GAIM has led to the creation of NeuroPhage's lead candidate, NPT088, which is the GAIM motif fused to a portion of a human antibody. The result is a potential therapeutic that can be easily delivered to patients. NeuroPhage has accumulated extensive preclinical data on this candidate, demonstrating its efficacy across disease models of Alzheimer's, Parkinson's and related diseases characterized by aggregation of the tau protein. NeuroPhage expects that NPT088 will be ready for human studies in late 2015.
"With recent advances in imaging agents for beta-amyloid and tau in Alzheimer's disease, we believe we should be able to demonstrate clinical proof of mechanism in a Phase 1b study with NPT088," said Jonathan Solomon, CEO at NeuroPhage. "If successful, we would then have the opportunity to pursue many therapeutic options in several neurodegenerative diseases of protein aggregation."
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