Novel “Enveloping” Mechanism of Prodrug Tramiprosate Inhibits Aß42 Amyloid Misfolding and Blocks Toxic Amyloid Oligomer Formation Early in Pathogenic Amyloid Aggregation Cascade Seen in Alzheimer’s Disease

On April 25, 2017, Alzheon, Inc. announced publication of a newly elucidated molecular mechanism of action for tramiprosate, the active agent in the company's lead clinical drug candidate, ALZ-801. The company's Phase 3-ready candidate ALZ-801 is an optimized prodrug of tramiprosate, with a substantially improved pharmacokinetic and safety profile compared to tramiprosate. Alzheon scientists discovered that tramiprosate acts to inhibit the production of neurotoxic beta amyloid oligomers by “enveloping” the amyloid peptide to prevent its misfolding into soluble amyloid aggregates. Beta amyloid oligomers are believed to be key drivers of the pathogenic process in Alzheimer's disease (AD). This novel enveloping mechanism of tramiprosate prevents the self-assembly of misfolded proteins into beta amyloid oligomers that lead to amyloid aggregation and, subsequently, cause neuronal toxicity and clinical progression in Alzheimer's disease. These peer-reviewed results were published online on April 24, 2017 in the medical journal CNS Drugs, and the paper is available through open access at: The article is titled “Elucidating the Aβ42 Anti-Aggregation Mechanism of Action of Tramiprosate in Alzheimer’s Disease: Integrating Molecular Analytical Methods, Pharmacokinetic and Clinical Data.”
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