Two novel monoclonal antibodies were discovered that target pathological conformations of the tau protein. The antibodies were shown in vitro and in vivo to inhibit the spread of pathological tau protein aggregates, which is one of the defining characteristics of AD.

More than 5 million Americans are living with Alzheimer’s disease  which is the 6th leading cause of death (Alzheimer’s Association. 2020 Alzheimer’s Disease Facts and Figures. Alzheimer’s Dement 2020). Current treatments do not adequately slow the progression of the diseases. By 2022, the market for AD therapeutics is expected to reach nearly USD $9 billion, a significant percentage  of which is anticipated to be novel antibodies directed against tau, and beta amyloid proteins (Potential Pipeline Disruptors, Kalorama Information, 2017).

Intracellular tau protein aggregates are a pathological hallmark of AD. In the disease state, misfolded tau spreads from cell to cell thereby introducing seed aggregates in neighboring cells which perpetuate the pathology of the disease.

The novel monoclonal antibodies are designed to bind to the misfolded tau released from neurons and prevent it from entering nearby cells, thus slowing down disease progression.

Two monoclonal antibodies were developed against the pathological form of tau. These antibodies have been fully sequenced and shown to be active in vitro, and in vivo in a murine model of Alzheimer’s disease. The antibodies were generated by immunization of mice using AD-tau paired helical filaments (PHFs).

These novel conformation-selective tau antibodies selectively bind to pathological tau compared to recombinant tau monomer, block the uptake of tau fibrils into cells, and prevent the cell-to-cell transmission of tau pathology in primary neurons and in a mouse model of AD.

• Selective binding to pathological tau conformers
• Prevention of cell-to-cell transmission of aggregated tau
• Potential ability to slow down Alzheimer’s disease progression