# Developing a screening platform to identify inhibitors of pathological self-assembly of Tau

> **NIH NIH R03** · STATE UNIVERSITY OF NEW YORK AT BUFFALO · 2022 · $157,711

## Abstract

Alzheimer’s disease (AD) is an irreversible and progressive neurodegenerative disorder that currently affects
an estimated 5.7 million individuals in the USA. This age onset disorder affects elderly individuals
disproportionately. It is estimated that by 2050, the number of AD patients in the US will increase to ~14 million.
In the absence of effective therapeutic interventions that can prevent or reverse AD pathologies, the disease is
likely to impose a significant economic burden, estimated to be $234 billion (in addition to the $259 billion spent
in the medical care of AD patients). Therefore, there is a dire need to identify pharmacologic agents that can
prevent/reverse/slow-down AD progression.
 Recent advances in our understandings of Tau biology suggest that liquid-liquid phase separation (LLPS)
plays crucial roles in both Tau physiology and pathology. For example, LLPS of Tau aids microtubule assembly
and/or stabilizes pre-formed microtubule bundles (physiologic role of Tau LLPS). On the other hand, Tau
condensates can initiate pathologic protein aggregation (role of LLPS in Tau pathology).
 Based on these observations and our preliminary data, here, we propose to develop and implement a
screening pipeline that selectively targets pathologic liquid-to-solid transformation of Tau. For our screening
program, we will employ state-of-the-art optical tweezer-based condensate fusion assay that provides a label-
free method for characterizing condensate material state(s). In Aim 1, we will identify pharmacologic compounds
that prevent Tau condensate-derived protein aggregation without altering (or minimally perturbing) Tau’s
physiologic condensation. In Aim 2, we will validate these compounds’ effectiveness using biochemical and cell
biology methods. We posit that our proposed approach will be broadly applicable to many other physiologic
protein condensates whose aggregations are linked to degenerative disorders.

## Key facts

- **NIH application ID:** 10323679
- **Project number:** 5R03AG070510-02
- **Recipient organization:** STATE UNIVERSITY OF NEW YORK AT BUFFALO
- **Principal Investigator:** Priya R. Banerjee
- **Activity code:** R03 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2022
- **Award amount:** $157,711
- **Award type:** 5
- **Project period:** 2021-01-15 → 2024-12-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10323679

## Citation

> US National Institutes of Health, RePORTER application 10323679, Developing a screening platform to identify inhibitors of pathological self-assembly of Tau (5R03AG070510-02). Retrieved via AI Analytics 2026-05-23 from https://api.ai-analytics.org/grant/nih/10323679. Licensed CC0.

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