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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...

Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

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Related Experiment Video

Updated: Jun 13, 2026

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Enzymatically triggered amyloid formation: an approach for studying peptide aggregation.

Malgorzata Broncel¹, Sara C Wagner, Christian P R Hackenberger

¹Institut für Chemie und Biochemie, Freie Universität Berlin, Takustr. 3, 14195 Berlin, Germany.

Chemical Communications (Cambridge, England)

|April 29, 2010

Summary

Researchers used a phosphatase enzyme to control amyloid formation in a coiled coil peptide model. This strategy mimics physiological conditions, offering a new approach to studying amyloid aggregation.

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Area of Science:

Biochemistry
Molecular Biology
Biophysics

Background:

Amyloid formation is implicated in various diseases.
Controlling amyloid aggregation under physiological conditions is challenging.
Coiled coil peptides serve as models for studying protein self-assembly.

Purpose of the Study:

To demonstrate a strategy for triggering and controlling amyloid formation.
To utilize a phosphatase as a tool for amyloid formation control.
To investigate amyloid formation in a coiled coil peptide model under near-physiological conditions.

Main Methods:

Employing a phosphatase enzyme for controlled peptide modification.
Utilizing a coiled coil peptide model system.
Conducting experiments under conditions mimicking a physiological environment.

Main Results:

Successful demonstration of a phosphatase-mediated strategy for amyloid formation.
Achieved control over the triggering and progression of amyloid aggregation.
Validated the approach within a relevant physiological context.

Conclusions:

Phosphatase activity can be harnessed to regulate amyloid formation.
The coiled coil peptide model provides insights into physiologically relevant amyloid processes.
This strategy offers a novel method for studying and potentially modulating amyloid aggregation.