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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...

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 21, 2026

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

beta(2)-microglobulin: from physiology to amyloidosis.

Niels H H Heegaard¹

¹Department of Clinical Biochemistry and Immunology, Statens Serum Institut, Copenhagen, Denmark. nhe@ssi.dk <nhe@ssi.dk>

Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis

|August 7, 2009

Summary

Dialysis-related amyloidosis occurs when beta(2)-microglobulin (beta(2)m) forms amyloid deposits. Understanding factors like Cu(2+) that destabilize beta(2)m is key to preventing this condition in kidney failure patients.

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

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Last Updated: Jun 21, 2026

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

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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

Area of Science:

Biochemistry
Pathology
Nephrology

Background:

Beta(2)-microglobulin (beta(2)m) forms amyloid in patients with kidney failure undergoing hemodialysis.
Dialysis-related amyloidosis affects osteoarticular structures.
The exact mechanisms of beta(2)m amyloidogenesis remain unclear.

Purpose of the Study:

To review current knowledge on factors influencing beta(2)m conformation and amyloid formation.
To link these factors to beta(2)m structure, function, and pathology.
To provide an overview of beta(2)m modifications and fibrillogenesis conditions.

Main Methods:

Literature review of studies on beta(2)m conformation and amyloid formation.
Analysis of factors affecting beta(2)m stability, including truncations, cleavages, substitutions, and divalent cations (e.g., Cu(2+)).
Compilation of tables detailing beta(2)m modifications in patient amyloid and laboratory fibrillogenesis conditions.

Main Results:

Various modifications and conditions, particularly Cu(2+), destabilize beta(2)m, promoting unfolding pathways.
Understanding these destabilizing factors is crucial for elucidating amyloid formation mechanisms.
Specific modifications found in patient amyloid and conditions favoring in vitro fibrillogenesis are cataloged.

Conclusions:

Conformational destabilization of beta(2)m by various factors is central to dialysis-related amyloidosis.
Further research into these factors can guide therapeutic strategies.
This review consolidates knowledge on beta(2)m amyloidogenesis, aiding future investigations.