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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,...

Amyloid Fibrils

Amyloid Fibrils

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Related Experiment Video

Updated: Nov 29, 2025

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

Published on: October 20, 2017

Visualizing and trapping transient oligomers in amyloid assembly pathways.

Emma E Cawood¹, Theodoros K Karamanos², Andrew J Wilson³

¹Astbury Centre for Structural Molecular Biology, School of Chemistry, University of Leeds, LS2 9JT, UK; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds, LS2 9JT, UK.

Biophysical Chemistry

|November 21, 2020

Summary

Oligomers are key to amyloid disease, but hard to study. New methods help detect and stabilize these amyloid intermediates for better understanding of their structure and toxicity.

Keywords:

Amyloid disease Chemical tool NMR Oligomer stabilization Single particle Transient intermediate

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Area of Science:

Biochemistry
Structural Biology
Neuroscience

Background:

Oligomers forming during amyloid fibril assembly are implicated in amyloid diseases.
The transient and heterogeneous nature of these intermediates poses significant challenges for study.

Purpose of the Study:

To discuss strategies for overcoming challenges in studying amyloid oligomers.
To enable a clearer understanding of oligomeric intermediates in amyloid formation and disease.

Main Methods:

Utilizing methods for detecting low-population species: NMR, single particle methods (fluorescence, force spectroscopy), and mass spectrometry.
Employing chemical and biological tools to bias the amyloid energy landscape towards specific oligomeric states.

Main Results:

Detection methods are suitable for studying amyloid assembly kinetics and obtaining low-resolution structures.
Biasing tools can yield oligomer samples for high-resolution structural studies and structure-toxicity relationship inference.

Conclusions:

Combining detection and biasing strategies offers a comprehensive approach to studying amyloid oligomers.
These integrated approaches are crucial for elucidating the role of oligomeric intermediates in amyloid diseases.