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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: Jul 5, 2026

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

Amyloids: friend or foe?

Neal D Hammer¹, Xuan Wang, Bryan A McGuffie

¹Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI 48109-0620, USA.

Journal of Alzheimer'S Disease : JAD

|May 20, 2008

Summary

Amyloidogenesis, the clumping of proteins into fibers, is linked to diseases like Alzheimer's. Studying functional amyloids offers insights into therapeutic development and natural protein roles.

Area of Science:

Biochemistry and Molecular Biology
Neuroscience
Cell Biology

Background:

Amyloidogenesis involves protein aggregation into stable, beta-sheet-rich fibers.
Amyloid formation is implicated in neurodegenerative diseases such as Alzheimer's and prion diseases.
Functional amyloids, utilized by diverse organisms for physiological tasks, present a contrasting model.

Purpose of the Study:

To review amyloidogenesis, comparing disease-associated amyloid-beta with functional amyloids.
To explore the implications of studying functional amyloid formation.
To discuss strategies organisms use to mitigate toxic amyloid intermediates.

Main Methods:

Literature review and comparative analysis of amyloidogenic proteins.
Examination of structural and functional properties of disease-associated and functional amyloids.

More Related Videos

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Related Experiment Videos

Last Updated: Jul 5, 2026

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Discussion of evolutionary and cellular strategies in amyloid formation.

Main Results:

Amyloid fibers share conserved structural features (beta-sheet structure, protease resistance) across disease-associated and functional types.
Functional amyloids demonstrate nature's utilization of protein aggregation for beneficial purposes.
Organisms employ diverse mechanisms to control amyloid formation and prevent toxicity.

Conclusions:

Understanding both pathological and functional amyloidogenesis is crucial for developing targeted therapeutics.
Comparative studies illuminate the dual role of protein aggregation in disease and physiology.
Investigating functional amyloids provides insights into protein self-assembly and biological regulation.