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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

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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.
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Related Experiment Video

Updated: Jun 27, 2026

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Amyloid formation by globular proteins under native conditions.

Fabrizio Chiti¹, Christopher M Dobson

¹Dipartimento di Scienze Biochimiche, Università degli Studi di Firenze, Viale Morgagni 50, I-50134 Firenze, Italy. fabrizio.chiti@unifi.it

Nature Chemical Biology

|December 18, 2008

Summary

This summary is machine-generated.

Protein misfolding and aggregation into fibrils are linked to diseases like neurodegenerative conditions and amyloidosis. Aggregation can initiate from partially unfolded protein states, not necessarily requiring full unfolding, offering insights into disease mechanisms and potential treatments.

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Area of Science:

Biochemistry
Molecular Biology
Pathology

Background:

Protein misfolding and fibril formation are implicated in numerous diseases, including neurodegenerative disorders and systemic amyloidoses.
Understanding the initial steps of protein aggregation is crucial for disease pathogenesis and therapeutic strategies.

Purpose of the Study:

To review the mechanisms of globular protein aggregation from initially folded states.
To explore the role of partially unfolded states in initiating protein aggregation under physiological conditions.

Main Methods:

Literature review of recent evidence on protein aggregation mechanisms.
Analysis of conformational changes and energy barriers in protein unfolding and aggregation.

Main Results:

Protein aggregation does not always require a complete transition across the major unfolding energy barrier.
Aggregation can be initiated from locally unfolded protein states accessible via thermal fluctuations.

Conclusions:

Protein aggregation can commence from partially unfolded states under physiological conditions.
This understanding is significant for elucidating the onset of protein aggregation diseases and developing inhibition strategies.