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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: May 16, 2026

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Generating extracellular amyloid aggregates using E. coli cells.

Viknesh Sivanathan¹, Ann Hochschild

¹Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115 USA.

Genes & Development

|November 21, 2012

Summary

This summary is machine-generated.

Researchers developed a new method using Escherichia coli to identify amyloid-forming proteins. This system aids in discovering proteins with inherent amyloid propensity and potential aggregation modulators.

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Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by γ-Secretase

Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by γ-Secretase

Published on: June 24, 2025

Area of Science:

Biochemistry
Molecular Biology
Microbiology

Background:

Diverse proteins can form amyloid aggregates, which are implicated in both biological functions and diseases.
Identifying amyloidogenic proteins is crucial for understanding their roles and developing therapeutic strategies.

Purpose of the Study:

To develop a generalizable cell-based method for identifying amyloidogenic proteins.
To leverage the natural amyloid fibril formation capabilities of Escherichia coli.

Main Methods:

Utilized Escherichia coli for cell-surface amyloid aggregate generation.
Employed a specialized protein export pathway in E. coli.
Tested yeast prion proteins and human huntingtin protein for amyloid formation propensity.

Main Results:

Protein secretion via the E. coli export pathway promoted amyloid fold acquisition in proteins with inherent amyloid-forming propensity.
Demonstrated the system's efficacy with known amyloidogenic proteins.

Conclusions:

The E. coli-based system is a viable method for generating and identifying amyloidogenic proteins.
This platform facilitates high-throughput screening for amyloidogenic proteins and modulators of amyloid aggregation.