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Amyloid Fibrils

Amyloid Fibrils

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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Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease

Published on: May 13, 2010

A genetically encoded selection for amyloid-β oligomer binders.

ByungUk Lee¹, John A Mannone¹, Tina Wang²

¹Department of Chemistry, University of Wisconsin-Madison, Madison, WI, USA.

Nature Chemical Biology

|July 15, 2025

Summary

Researchers developed a biosensor to detect toxic amyloid-β oligomers (AβOs) in Alzheimer disease. This tool rapidly identifies potent binding proteins, accelerating the discovery of new diagnostics and therapeutics for neurodegenerative diseases.

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Published on: May 13, 2010

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

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A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

Published on: March 27, 2017

Area of Science:

Neuroscience
Biochemistry
Molecular Biology

Background:

Soluble amyloid-β oligomers (AβOs) are implicated in Alzheimer disease neurotoxicity.
Identifying specific binders to transient AβOs is difficult due to their short lifespan and low concentration.
Existing methods face challenges in detecting AβOs generated during the aggregation cascade.

Purpose of the Study:

To develop a novel strategy for detecting binding to AβOs.
To enable rapid and reproducible measurement of AβO binder activity.
To facilitate the selection of new, high-potency AβO binders.

Main Methods:

Utilized a genetically encoded biosensor to detect AβOs.
Applied the biosensor to Aβ42 aggregation process.
Measured the activity of existing and novel AβO binders.

Main Results:

Demonstrated rapid and reproducible measurement of AβO binder activity.
Identified novel binders with >20-fold greater potency than reported binders.
Showcased the ability to select for improved binder potency.

Conclusions:

The genetically encoded biosensor strategy accelerates the discovery of AβO binding proteins.
This approach enhances the characterization of binders targeting toxic AβOs.
The findings may lead to improved diagnostic and therapeutic strategies for Alzheimer disease.