Ganglioside GM3 stimulates lipid-protein co-assembly in α-synuclein amyloid formation.
Ganglioside
Lipid
NMR spectroscopy
Parkinson's disease
Protein aggregation
Vesicle
α-synuclein
Journal
Biophysical chemistry
ISSN: 1873-4200
Titre abrégé: Biophys Chem
Pays: Netherlands
ID NLM: 0403171
Informations de publication
Date de publication:
02 2023
02 2023
Historique:
received:
03
10
2022
revised:
04
11
2022
accepted:
15
11
2022
pubmed:
10
12
2022
medline:
18
1
2023
entrez:
9
12
2022
Statut:
ppublish
Résumé
Parkinson's disease is characterized by the aggregation of the presynaptic protein α-synuclein (αSyn), and its co-assembly with lipids and other cellular matter in the brain. Here we investigated lipid-protein co-assembly in a system composed of αSyn and model membranes containing the glycolipid ganglioside GM3. We quantified the uptake of lipids into the co-assembled aggregates and investigated how lipid molecular dynamics is altered by being present in the co-assemblies using solution
Identifiants
pubmed: 36493587
pii: S0301-4622(22)00176-4
doi: 10.1016/j.bpc.2022.106934
pii:
doi:
Substances chimiques
alpha-Synuclein
0
G(M3) Ganglioside
0
Amyloid
0
Amyloidogenic Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
106934Informations de copyright
Copyright © 2022 The Authors. Published by Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: Emma Sparr reports financial support was provided by Swedish Research Council. Daniel Topgaard reports financial support was provided by Swedish Research Council. Emma Sparr, Sara Linse, Daniel Topgaard reports financial support was provided by Knut and Alice Wallenberg Foundation. SL is a founder and employee of Wren Therapeutics Ltd.