Development Programs

Anti-TauC3 Monoclonal Antibody

In 2012, we obtained from Northwestern University an exclusive license to worldwide diagnostic and therapeutic applications of a novel monoclonal antibody targeted to caspase cleaved TauC3.

Scientific research and pre-clinical experiments have demonstrated that fragments of Tau protein are present in brains of patients suffering from various neurodegenerative diseases, commonly known as “tauopathies”, and that the truncated form of Tau, known as TauC3, is especially toxic.

We have conducted experiments to demonstrate that caspase cleaved TauC3 is present in models of various tauopathies at a level detectable by our anti-TauC3 antibody and that our anti-TauC3 antibody shows sufficient binding specificity to the target TauC3 protein to indicate that the antibody may be a viable treatment agent.

In 2014, we reported positive top line data from a pre-clinical study conducted on our behalf at UC Irvine showing proof of concept for the antibody in an Alzheimer's disease (AD) mouse model.

In April 2016, we obtained positive data from an in-vitro study conducted on our behalf at Harvard Medical School and the MassGeneral Institute for Neurodegenerative Disease. The experiments demonstrated that our anti-TauC3 antibody significantly blocks TauC3 fragment seeding, aggregation and toxicity, demonstrating that caspase cleaved TauC3 is a potential target for treatment in Progressive Supranuclear Palsy, Traumatic Brain Injury and other tauopathies and that our antibody may be a viable treatment agent.

We are initiating experimental treatment trials of our anti-TauC3 antibody in mouse models of progressive supranuclear palsy (PSP) and traumatic brain injury (TBI). These conditions are rare, “orphan”, neurological diseases of high unmet medical need with no approved therapies.

Presence of TauC3 in Tauopathies

Scientific evidence has proven that caspase cleaved TauC3 promotes formation of neurofibrillary tangles (NFTs), which are aggregates of hyper-phosphorylated tau found in numerous tauopathies.

Truncation of tau by caspases may occur relatively early in neurodegenerative disease, prior to the key folding steps that lead to the formation of phosphorylated pathological forms of tau. Also, it has been demonstrated that tau truncated at Asp421 (TauC3) aggregates more rapidly and to a greater degree than full-length tau.

Collectively, these studies suggest that the caspase cleavage of tau propagates the formation of NFTs and facilitates filament formation, which are disease- triggering events that are associated with various neurodegenerative conditions, such as Alzheimer’s disease, PSP and TBI.

Illustrative Diagram of Presence of TauC3 in Pick’s Disease, TBI and PSP