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Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...

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High-throughput Screening for Chemical Modulators of Post-transcriptionally Regulated Genes

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A Robust and Scalable High-Throughput Compatible Assay for Screening Amyloid-β-Binding Compounds.

Richard McClure¹, Rey Redha², Paige Vinson^2,3

¹Vanderbilt University Institute of Imaging Science, Vanderbilt University, Nashville, TN, USA.

Journal of Alzheimer'S Disease : JAD

|June 10, 2019

Summary

Researchers developed a new fluorescent assay to screen for amyloid-binding molecules using real amyloid from mouse brains. This robust method identified 8 potential new drug candidates from 3,500 tested compounds.

Keywords:

Alzheimer’s disease amyloid high throughput screening

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Area of Science:

Biochemistry
Neuroscience
Drug Discovery

Background:

Amyloid aggregation is a hallmark of neurodegenerative diseases.
Developing effective amyloid-binding molecules is crucial for therapeutic strategies.
Existing screening methods may lack the physiological relevance needed for accurate drug discovery.

Purpose of the Study:

To develop and optimize a robust fluorescent readout assay for screening amyloid-binding molecules.
To enhance the physiological relevance of the assay by using endogenous amyloid.
To identify novel amyloid-binding agents from a diverse compound library.

Main Methods:

Utilized topologically-sensitive dyes for fluorescent readout.
Incorporated endogenous amyloid sourced from 5XFAD mouse brains.
Optimized assay conditions for high-throughput screening (HTS) achieving Z-prime values >0.6.
Screened a library of 3,500 compounds, including known drugs, natural products, and random molecules.

Main Results:

Established a robust and realistic fluorescent assay for amyloid-binding molecule screening.
Achieved high assay performance with Z-prime values >0.6, indicating suitability for HTS.
Identified 8 unique molecules demonstrating potential amyloid-binding activity.
The identified molecules represent diverse chemical classes, including known drugs and natural products.

Conclusions:

The developed fluorescent assay is a powerful tool for identifying novel amyloid-binding agents.
The use of endogenous amyloid significantly increases the assay's physiological relevance.
The identified 8 compounds warrant further investigation as potential therapeutics for amyloid-related diseases.