Related Experiment Video
Updated: Aug 8, 2026
05:48
Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
Protein misfolding, functional amyloid, and human disease
Fabrizio Chiti1, Christopher M Dobson
1Dipartimento di Scienze Biochimiche, Università degli Studi di Firenze, I-50134 Firenze, Italy. fabrizio.chiti@unifi.it
Annual Review of Biochemistry
|June 8, 2006
Summary
Proteins can form ordered fibrillar aggregates, causing diseases like neurodegenerative disorders and amyloidoses. Understanding these protein aggregation mechanisms is key to developing treatments and exploring beneficial biological functions.
Area of Science:
- Biochemistry
- Molecular Biology
- Pathology
Background:
- Proteins can transition from soluble forms to ordered fibrillar aggregates under specific conditions.
- This protein aggregation is linked to various pathological conditions, including neurodegenerative disorders and systemic amyloidoses.
Purpose of the Study:
- To identify diseases associated with fibrillar aggregate formation and the specific peptides/proteins involved.
- To explore the beneficial biological functions derived from protein self-assembly.
- To review advances in understanding amyloid fibril structures and formation mechanisms.
Main Methods:
- Literature review of diseases linked to protein aggregation.
- Analysis of structural data and formation mechanisms of amyloid fibrils.
- Discussion of protein-protein interactions driving aggregation propensity.
Main Results:
- Catalog of diseases and associated protein aggregates.
- Insights into the molecular mechanisms of fibril formation.
- Identification of key interactions governing protein aggregation.
Conclusions:
- Protein aggregation underlies significant human diseases but also serves biological functions.
- Oligomeric fibril precursors are implicated as the primary cause of pathology.
- Further research into aggregation mechanisms can inform therapeutic strategies.
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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 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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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 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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