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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,...

Amyloid Fibrils

Amyloid Fibrils

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Related Experiment Video

Updated: Oct 29, 2025

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Exploring amyloid oligomers with peptide model systems.

Tuan D Samdin¹, Adam G Kreutzer¹, James S Nowick²

¹Department of Chemistry, University of California, Irvine, CA 92697-2025, United States.

Current Opinion in Chemical Biology

|July 6, 2021

Summary

This summary is machine-generated.

Amyloid oligomers are key to diseases like Alzheimer's. Researchers use peptide models to study their structures and properties, advancing our understanding of these complex conditions.

Keywords:

Amyloid Amyloid oligomers Amyloidogenic peptides and proteins CryoEM Fibrils Human prion protein hPrP Macrocyclic β-hairpin peptides Model peptide systems Molecular docking Molecular modeling NMR Oligomer mimics Peptide fragments Stabilized β-hairpins Superoxide dismutase 1 (SOD1)X-ray crystallography α-Synuclein αB crystallin β-amyloid peptide (Aβ)

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Area of Science:

Biochemistry
Molecular Biology
Neuroscience

Background:

Amyloidogenic proteins (e.g., beta-amyloid, alpha-synuclein) assemble into fibrils and oligomers, linked to neurodegenerative diseases.
Amyloid oligomers are implicated in diseases like Alzheimer's, Parkinson's, and type II diabetes.
High-resolution structures of full-length amyloid oligomers remain challenging to determine.

Purpose of the Study:

To summarize recent advances in using peptide model systems to study amyloid oligomers.
To investigate the structural, biophysical, and biological properties of amyloid oligomers.
To enhance understanding of the mechanisms underlying amyloid diseases.

Main Methods:

Utilizing peptide fragments and stabilized beta-hairpin segments of amyloidogenic proteins.
Employing biophysical techniques to analyze oligomer assembly and properties.
Investigating the biological impact of these model oligomers.

Main Results:

Peptide model systems provide insights into the elusive structures of amyloid oligomers.
These models illuminate the biophysical characteristics of oligomer formation.
The study highlights the biological relevance of oligomer structures in disease.

Conclusions:

Peptide model systems are valuable tools for understanding amyloid oligomer structure and function.
Advances in studying these models contribute to deciphering the pathogenesis of amyloid diseases.
Further research using these systems can lead to therapeutic strategies for Alzheimer's and related disorders.