Tau protein has multiple normal functions including the modulation of microtubule stability, axonal transport, modulation of signaling pathways and adult neurogenesis. Recent work has shown that toxicity is mediated by a gain of toxic function caused by tau that has become modified by conformational changes accompanied by oligomer formation and aggregation.
Alzheimer’s Disease is continually impacting millions of people at a global and national level. For Americans over 65, 1 in 8 will be affected by the disease. Globally, nearly 44 million people are believed to be living with AD or other dementia related diseases. It estimated that nearly 500,000 new cases will be diagnosed this year alone, and if breakthroughs are not discovered by 2030, this will rise to nearly 76 million cases. By 2050, rates could exceed 152 million. AD is also one of the leading drivers of healthcare costs in the US with a financial burden of over $290 billion annually in healthcare and long-term care costs and is estimated to increase to $1.1 trillion by 2050 (Alzheimer’s Association Facts and Figures, 2019).
Targeting tau oligomer formation should modify the course of Alzheimer’s disease. Oligomerix is highly differentiated from other groups targeting tau because of its approach to block tau self-association, the first step in aggregation, with small molecules. Small molecules can penetrate the brain entering individual neurons and extracellular vesicles to directly interfere with tau aggregation. Antibodies only bind a small subset of aggregated tau, whereas our small molecules were selected to inhibit the formation of all tau aggregates. Oligomerix’s small molecule formulation offers a critical competitive advantage that would enable cost-effective, patient-centered treatment for the rapidly growing, unserved AD market in the context of significant and growing global healthcare system cost pressures.