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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...

Protein Folding

Protein Folding

Protein Folding

Protein Folding

Protein Organization

Protein Organization

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Updated: Jun 17, 2026

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Amyloidogenic sequences in native protein structures.

Susan Tzotzos¹, Andrew J Doig

¹Manchester Interdisciplinary Biocentre, The University of Manchester, Manchester M1 7DN, United Kingdom.

Protein Science : a Publication of the Protein Society

|December 23, 2009

Summary

This summary is machine-generated.

Proteins prevent toxic amyloid aggregation by incorporating amyloid-forming sequences into alpha-helices or burying them within the protein structure. This structural adaptation maintains cellular health and protein function.

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Rapid Generation of Amyloid from Native Proteins In vitro

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Area of Science:

Biochemistry
Structural Biology
Molecular Biology

Background:

Short peptides can form beta-sheet amyloid aggregates in vitro.
Amyloidogenic sequences within proteins pose a risk of forming toxic structures within cells.

Purpose of the Study:

Investigate how proteins manage potentially toxic amyloidogenic sequences.
Analyze structural features that prevent protein aggregation.

Main Methods:

Studied secondary structure, hydrogen bonding, solvent accessible surface area, and hydrophobicity.
Examined 30 proteins containing 45 known amyloidogenic sequences.

Main Results:

Amyloidogenic sequences are often found in alpha-helices, despite a preference for beta structure.
Amyloidogenic sequences in beta structure are typically buried within the protein, avoiding surface exposure.
Surface-exposed amyloidogenic sequences in strands are not tolerated due to aggregation risks.

Conclusions:

Proteins utilize alpha-helices to sequester amyloidogenic sequences, requiring unfolding and refolding for aggregation.
Burial of amyloidogenic sequences within protein structures prevents aggregation.
Alpha-helix incorporation is a widespread mechanism for avoiding toxic protein aggregation.