# Affinity purification of cross-ß fibrils using immobilized thioflavin

> **NIH NIH R21** · PURDUE UNIVERSITY · 2024 · $217,876

## Abstract

Project Summary
Neurodegenerative diseases such as Alzheimer’s disease cause a significant socioeconomic burden. These
diseases manifest as protein plaques in the brain tissues. As of today, there are no available drugs to treat
or prevent these diseases. For rational drug design, it is essential to understand the atomic details of the
proteins involved in these plaques. To achieve this, researchers utilize structural biology methods such as
electron cryomicroscopy (cryoEM), nuclear magnetic resonance, and X-ray crystallography.
Neuropathologists isolate these plaques from post-mortem patient brain tissues and assess the disease for
the presence of plaques. Then the samples are subjected to structural studies. Since 2017, a significant
number of atomic structures of the protein molecules involved in the plaques have been reported. However,
isolation of proteins from tissue samples is a bottleneck due to low yield, differences in the protein structures,
and the presence of contaminants. The proteins in the plaques have a distinct arrangement in that they form
a β-strand conformation and stack on top of each other along a helical axis. This arrangement gives rise to
a unique property – they bind to molecules such as thioflavin and exhibit characteristic fluorescence emission.
Such a property enables researchers to know the presence of protein plaques and quantify them in cellular
models. Here, we propose to utilize the specificity of thioflavin to protein filaments of neuropathological
plaques as a new method of plaque purification. The method combines the specificity of thioflavin to the
protein filaments and affinity-based purification methods that are widely used to purify proteins. We propose
that our method would enable researchers to extract and isolate protein filaments from brain tissues with
much improved yields, fewer contaminants, and shorter processing times.

## Key facts

- **NIH application ID:** 10815762
- **Project number:** 5R21AG081686-02
- **Recipient organization:** PURDUE UNIVERSITY
- **Principal Investigator:** Wen Jiang
- **Activity code:** R21 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2024
- **Award amount:** $217,876
- **Award type:** 5
- **Project period:** 2023-04-01 → 2026-03-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10815762

## Citation

> US National Institutes of Health, RePORTER application 10815762, Affinity purification of cross-ß fibrils using immobilized thioflavin (5R21AG081686-02). Retrieved via AI Analytics 2026-05-24 from https://api.ai-analytics.org/grant/nih/10815762. Licensed CC0.

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