Jessica Fortin, DVM, PhD
Characterization of New Inhibitors of P-Tau Aggregation and Cytotoxicity
Summary
Alzheimer’s disease (AD) represents the most common form of dementia, characterized by intracellular neurofibrillary tangles (NFTs), composed of microtubule-associated tau-protein, and extracellular β-amyloid plaques, made of B-amyloid peptide fragments 1-40 and 1-42. Despite significant efforts in past decades, no disease-modifying therapy has been available to prevent or cure the progression of the disease until now. Due to the rapidly increasing aging population worldwide, there is an urgent need to identify treatment strategies that can solve this challenge. Abnormally hyperphosphorylated tau is considered an early and pivotal point in the pathogenesis of AD and other tauopathies. Compelling evidence suggests that it is a key driver in the accumulation of NFTs and can be directly correlated with the extent of dementia in AD patients. Therefore, inhibiting the abnormal tau hyperphosphorylation induced aggregation can be a viable strategy to develop newer therapeutics targeting AD. Our lab focuses on the discovery of small molecules to stop the aggregation of p-tau responsible for the NFTs in AD.
Research Starter Grant funding allowed me to secure a tenure-track position at Purdue University and recruit a postdoc in medicinal chemistry. It also expanded my research program for the discovery of new molecules with anti-aggregation effect for Alzheimer’s disease. It will enable my team to publish important results and apply to other research funding opportunities.
