Rigidifying of the internal dynamics of amyloid-beta fibrils generated in the presence of synaptic plasma vesicles-Reference-Cited by-同舟云学术

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Rigidifying of the internal dynamics of amyloid-beta fibrils generated in the presence of synaptic plasma vesicles

Published:2024 Issue:6 Volume:26 Page:5466-5478
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Vugmeyster Liliya¹^ORCID,Au Dan Fai¹,Frazier Bailey¹,Qiang Wei²,Ostrovsky Dmitry³

Affiliation:

1. Department of Chemistry, University of Colorado Denver, Denver, CO, USA, 80204

2. Department of Chemistry, Binghamton University, Binghamton, New York, USA, 13902

3. Department of Mathematics, University of Colorado Denver, Denver, CO, USA, 80204

Abstract

We probed the changes in internal flexibility of amyloid-β fibrils grown with synaptic plasma vesicles using 2H solid-state NMR methods and TEM. A rigidifying effect is observed in comparison to the wild-type fibrils made without the vesicles.

Funder

National Institute of General Medical Sciences

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/CP/D3CP04824A

Reference77 articles.

1. Amyloid-β oligomers have a profound detergent-like effect on lipid membrane bilayers, imaged by atomic force and electron microscopy

2. Membrane and surface interactions of Alzheimer’s Aβ peptide - insights into the mechanism of cytotoxicity

3. Synaptotoxicity of Alzheimer Beta Amyloid Can Be Explained by Its Membrane Perforating Property

4. Amyloid β Ion Channels in a Membrane Comprising Brain Total Lipid Extracts

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