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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: Mar 23, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Single molecule study of initial structural features on the amyloidosis process.

Yong-Xu Hu¹, Yi-Lun Ying¹, Zhen Gu¹

¹Key Laboratory for Advanced Materials & Department of Chemistry, East China University of Science and Technology, Shanghai 200237, P. R. China. yilunying@ecust.edu.cn ytlong@ecust.edu.cn.

Chemical Communications (Cambridge, England)

|March 30, 2016

Summary

Alpha-hemolysin nanopores distinguish initial structures of beta-amyloid peptides, revealing distinct aggregate dynamics crucial for understanding amyloidosis progression.

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Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

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Last Updated: Mar 23, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

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Published on: September 17, 2017

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging

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Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Published on: April 28, 2022

Area of Science:

Biophysics
Biochemistry
Nanotechnology

Background:

Amyloidosis is a complex process involving protein misfolding and aggregation.
Understanding the initial structural influences on amyloid formation is critical for disease research.
Beta-amyloid (Aβ) peptides are key players in Alzheimer's disease pathogenesis.

Purpose of the Study:

To utilize a single-molecule nanopore technique to probe the impact of initial peptide structure on amyloidosis.
To differentiate between the aggregation pathways of Aβ25-35 and Aβ35-25 peptides.
To analyze the real-time dynamics of Aβ aggregate formation.

Main Methods:

Employing an alpha-hemolysin (α-HL) protein nanopore as a single-molecule sensor.
Monitoring characteristic ionic current blockades generated by individual Aβ peptides within the nanopore.
Analyzing the frequency and duration of blockades over time to infer aggregate dynamics.

Main Results:

Distinct blockade patterns were observed for Aβ25-35 and Aβ35-25 peptides, enabling real-time structural differentiation.
The study successfully distinguished the initial structural states of the two Aβ fragments.
Monitoring blockade frequency provided insights into the differing aggregate dynamics of the two peptide variants.

Conclusions:

Alpha-hemolysin nanopore technology offers a powerful tool for investigating the initial structural determinants of amyloidosis.
Distinct initial structures of beta-amyloid peptides lead to measurable differences in aggregation pathways.
This single-molecule approach facilitates the real-time analysis of amyloid aggregate dynamics.