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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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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

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Published on: May 22, 2018

Stable Cavitation Interferes with Aβ_16-22 Oligomerization.

Viet Hoang Man¹, Xibing He¹, Junmei Wang¹

¹Department of Pharmaceutical Sciences and Computational Chemical Genomics Screening Center, School of Pharmacy, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, United States.

Journal of Chemical Information and Modeling

|August 3, 2022

Summary

This summary is machine-generated.

Stable cavitation using ultrasound and microbubbles inhibits amyloid-β (Aβ) oligomer formation. This molecular dynamics simulation reveals altered Aβ peptide aggregation pathways, offering potential therapeutic optimization for Alzheimer's disease.

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Area of Science:

Biophysics
Computational Biology
Neuroscience

Background:

Amyloid-β (Aβ) aggregates are implicated in Alzheimer's disease pathogenesis.
Ultrasound and microbubbles show potential for Aβ clearance in preclinical models.
Understanding the molecular mechanisms of Aβ aggregation under ultrasound is crucial for therapeutic development.

Purpose of the Study:

To investigate the molecular mechanism of Aβ oligomerization under stable cavitation using nonequilibrium molecular dynamics simulations.
To determine the effect of stable cavitation on Aβ peptide aggregation pathways.

Main Methods:

Developed and implemented a nonequilibrium molecular dynamics simulation algorithm within the AMBER package.
Simulated Aβ_16-22 peptide oligomerization under stable cavitation conditions.
Utilized network analysis to study state transitions and altered oligomerization pathways.

Main Results:

Stable cavitation inhibited the formation of Aβ oligomers.
Stable cavitation prevented the formation of β-rich Aβ oligomers.
Network analysis demonstrated that stable cavitation altered the oligomerization pathways of Aβ_16-22 peptides.

Conclusions:

Stable cavitation is a promising approach to inhibit Aβ oligomerization at a molecular level.
The developed simulation tool can aid in optimizing ultrasound-based therapeutic strategies for Alzheimer's disease.
Understanding altered aggregation pathways provides insights into potential therapeutic interventions.