Cargando…
Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides
Alzheimer's disease (AD) is a common neurodegenerative condition that involves the extracellular accumulation of amyloid plaques predominantly consisting of Aβ peptide aggregates. The amyloid plaques and soluble oligomeric species of Aβ are believed to be the major cause of synaptic dysfunction...
Autores principales: | , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8286822/ https://www.ncbi.nlm.nih.gov/pubmed/34156433 http://dx.doi.org/10.1042/BST20201244 |
_version_ | 1783723791530065920 |
---|---|
author | Rajput, Sunnia Sani, Marc-Antoine Keizer, David W. Separovic, Frances |
author_facet | Rajput, Sunnia Sani, Marc-Antoine Keizer, David W. Separovic, Frances |
author_sort | Rajput, Sunnia |
collection | PubMed |
description | Alzheimer's disease (AD) is a common neurodegenerative condition that involves the extracellular accumulation of amyloid plaques predominantly consisting of Aβ peptide aggregates. The amyloid plaques and soluble oligomeric species of Aβ are believed to be the major cause of synaptic dysfunction in AD brain and their cytotoxic mechanisms have been proposed to involve interactions with cell membranes. In this review, we discuss our solid-state nuclear magnetic resonance (ssNMR) studies of Aβ interactions with model membranes. |
format | Online Article Text |
id | pubmed-8286822 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-82868222021-08-02 Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides Rajput, Sunnia Sani, Marc-Antoine Keizer, David W. Separovic, Frances Biochem Soc Trans Review Articles Alzheimer's disease (AD) is a common neurodegenerative condition that involves the extracellular accumulation of amyloid plaques predominantly consisting of Aβ peptide aggregates. The amyloid plaques and soluble oligomeric species of Aβ are believed to be the major cause of synaptic dysfunction in AD brain and their cytotoxic mechanisms have been proposed to involve interactions with cell membranes. In this review, we discuss our solid-state nuclear magnetic resonance (ssNMR) studies of Aβ interactions with model membranes. Portland Press Ltd. 2021-06-30 2021-06-22 /pmc/articles/PMC8286822/ /pubmed/34156433 http://dx.doi.org/10.1042/BST20201244 Text en © 2021 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY-NC-ND) (https://creativecommons.org/licenses/by-nc-nd/4.0/) . Open access for this article was enabled by the participation of University of Melbourne in an all-inclusive Read & Publish pilot with Portland Press and the Biochemical Society under a transformative agreement with CAUL. |
spellingShingle | Review Articles Rajput, Sunnia Sani, Marc-Antoine Keizer, David W. Separovic, Frances Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides |
title | Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides |
title_full | Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides |
title_fullStr | Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides |
title_full_unstemmed | Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides |
title_short | Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides |
title_sort | utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides |
topic | Review Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8286822/ https://www.ncbi.nlm.nih.gov/pubmed/34156433 http://dx.doi.org/10.1042/BST20201244 |
work_keys_str_mv | AT rajputsunnia utilizingmagneticresonancetechniquestostudymembraneinteractionsofamyloidpeptides AT sanimarcantoine utilizingmagneticresonancetechniquestostudymembraneinteractionsofamyloidpeptides AT keizerdavidw utilizingmagneticresonancetechniquestostudymembraneinteractionsofamyloidpeptides AT separovicfrances utilizingmagneticresonancetechniquestostudymembraneinteractionsofamyloidpeptides |