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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,...

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Updated: Jan 16, 2026

Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by γ-Secretase

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Modulation of Aβ_1-42 Aggregation by a SARS-CoV-2 Protein Fragment.

Malinda B Premathilaka¹, Ulrich H E Hansmann¹

¹Department of Chemistry & Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.

Journal of Chemical Information and Modeling

|October 1, 2025

Summary

This summary is machine-generated.

The SARS-CoV-2 Spike protein may promote Alzheimer's disease by interacting with amyloid-beta peptides. This interaction shifts proteins toward aggregation, potentially worsening amyloid pathology in Alzheimer's disease.

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Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

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Published on: November 30, 2018

Area of Science:

Neuroscience
Infectious Diseases
Biochemistry

Background:

Emerging evidence suggests SARS-CoV-2 infection may trigger amyloid diseases.
Alzheimer's disease is characterized by amyloid-beta (Aβ) peptide aggregation.
The link between SARS-CoV-2 and Alzheimer's disease requires further investigation.

Purpose of the Study:

To investigate the interaction between a SARS-CoV-2 Spike protein fragment and Aβ peptides.
To determine if SARS-CoV-2 can modulate Aβ aggregation relevant to Alzheimer's disease.

Main Methods:

Molecular dynamics simulations were employed.
The study focused on the interaction between the Spike protein fragment (FKNIDGYFKI) and Aβ_1-42 monomers and fibrils.
Patient-derived and synthetic Aβ fibril models were utilized.

Main Results:

The viral protein fragment shifts Aβ monomer conformations towards aggregation-prone states.
Patient-derived Alzheimer's disease Aβ fibril polymorphs were more stabilized by the viral fragment than synthetic fibrils.
The study identified specific interactions modulating amyloid formation.

Conclusions:

SARS-CoV-2 Spike protein interactions may promote Aβ aggregation, potentially contributing to Alzheimer's disease pathogenesis.
Viral protein fragments can influence amyloid formation pathways.
Further research is needed to understand the full implications of these interactions for neurodegenerative diseases.