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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, normally used to...

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Related Experiment Video

Updated: Jun 3, 2026

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Published on: April 28, 2022

Insight into amyloid structure using chemical probes.

Ashley A Reinke¹, Jason E Gestwicki

¹Department of Biological Chemistry, Pathology and the Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109-2216, USA.

Chemical Biology & Drug Design

|April 5, 2011

Summary

Alzheimer's disease (AD) involves brain amyloids, specifically amyloid-beta (Aβ) peptides. Chemical probes help study these diverse Aβ structures and their roles in AD pathogenesis.

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Published on: October 20, 2017

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Last Updated: Jun 3, 2026

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Published on: April 28, 2022

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

Area of Science:

Neuroscience
Biochemistry
Pathology

Background:

Alzheimer's disease (AD) is a prevalent neurodegenerative disorder.
AD pathogenesis involves the aggregation of amyloid-beta (Aβ) peptides in the brain.
Aβ amyloids exhibit structural heterogeneity, with varying sizes, shapes, and peptide counts.

Purpose of the Study:

To review the utility of chemical probes in understanding amyloid structure and function in AD.
To explore the potential of conformationally selective probes in testing AD models.

Main Methods:

Review of existing literature on chemical probes like Congo red and thioflavin T.
Discussion of the application of these probes in studying amyloid structure.
Exploration of the design principles for conformationally selective probes.

Main Results:

Chemical probes have been instrumental in elucidating amyloid structure and function.
Different amyloid conformations may have distinct roles in AD progression.
Conformationally selective probes offer a promising avenue for future AD research.

Conclusions:

Chemical probes are vital tools for investigating the complexities of amyloid structures in Alzheimer's disease.
Targeted probes can help differentiate the roles of various amyloid conformations in disease.
Further development of selective probes is crucial for advancing our understanding and treatment of AD.