Amyloid-β oligomers have a profound detergent-like effect on lipid membrane bilayers, imaged by atomic force and electron microscopy.
Alzheimer disease
amyloid-beta (AB)
atomic force microscopy (AFM)
cytotoxicity
electron microscopy (EM)
large unilamellar vesicles
membrane bilayer
membrane disruption
mica surface
nanoscale imaging
neurodegeneration
oligomer
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
10 05 2019
10 05 2019
Historique:
received:
17
12
2018
revised:
27
03
2019
pubmed:
6
4
2019
medline:
18
12
2019
entrez:
6
4
2019
Statut:
ppublish
Résumé
The ability of amyloid-β peptide (Aβ) to disrupt membrane integrity and cellular homeostasis is believed to be central to Alzheimer's disease pathology. Aβ is reported to have various impacts on the lipid bilayer, but a clearer picture of Aβ influence on membranes is required. Here, we use atomic force and transmission electron microscopies to image the impact of different isolated Aβ assembly types on lipid bilayers. We show that only oligomeric Aβ can profoundly disrupt the bilayer, visualized as widespread lipid extraction and subsequent deposition, which can be likened to an effect expected from the action of a detergent. We further show that Aβ oligomers cause widespread curvature and discontinuities within lipid vesicle membranes. In contrast, this detergent-like effect was not observed for Aβ monomers and fibers, although Aβ fibers did laterally associate and embed into the upper leaflet of the bilayer. The marked impact of Aβ oligomers on membrane integrity identified here reveals a mechanism by which these oligomers may be cytotoxic.
Identifiants
pubmed: 30948512
pii: S0021-9258(20)35455-7
doi: 10.1074/jbc.AC118.007195
pmc: PMC6514634
doi:
Substances chimiques
Amyloid beta-Peptides
0
Lipid Bilayers
0
Banques de données
PDB
['2MXU']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
7566-7572Subventions
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/M023877/1
Pays : United Kingdom
Informations de copyright
© 2019 Bode et al.
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