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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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Related Experiment Video

Updated: Sep 29, 2025

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Endogenous Human Proteins Interfering with Amyloid Formation.

Anna L Gharibyan¹, Sanduni Wasana Jayaweera¹, Manuela Lehmann²

¹Department of Clinical Microbiology, Umeå University, 901 87 Umeå, Sweden.

|March 25, 2022

Summary

Certain endogenous proteins like transthyretin and apolipoprotein E can inhibit amyloid formation, offering potential therapeutic strategies for degenerative diseases such as Alzheimer's and Parkinson's.

Keywords:

BRICHOS IAPP alpha-synuclein amyloid inhibition amyloid-beta apolipoprotein E clusterin endogenous proteins transthyretin

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Last Updated: Sep 29, 2025

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

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

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

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Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

Published on: October 17, 2015

Area of Science:

Biochemistry and Molecular Biology
Neurodegenerative Diseases
Protein Misfolding Disorders

Background:

Amyloid formation is a key pathological hallmark in various degenerative disorders, including Alzheimer's and Parkinson's diseases.
The abnormal accumulation of misfolded proteins leads to tissue damage, inflammation, and organ dysfunction.
Targeting amyloid formation presents a promising therapeutic avenue for these debilitating conditions.

Purpose of the Study:

To review endogenous proteins with demonstrated anti-amyloidogenic properties.
To discuss the mechanisms by which these proteins interfere with amyloid formation.
To explore their therapeutic potential in human and animal models of amyloid-related diseases.

Main Methods:

Literature review of studies investigating endogenous anti-amyloidogenic proteins.
Analysis of in vitro experimental data on protein-amyloid interactions.
Examination of clinical and animal model data regarding the impact of these proteins.

Main Results:

Transthyretin, apolipoprotein E, clusterin, and BRICHOS protein domain exhibit significant in vitro anti-amyloidogenic activity.
These proteins have shown clinical relevance and impact in animal models of amyloidosis.
Their diverse mechanisms effectively inhibit or disrupt amyloid fibril formation and aggregation.

Conclusions:

Endogenous proteins possess potent anti-amyloidogenic capabilities.
Understanding their mechanisms can inspire novel therapeutic strategies for amyloidosis.
These proteins represent valuable targets for developing treatments for neurodegenerative and other amyloid-related diseases.