α-Synuclein-derived lipoparticles in the study of α-Synuclein amyloid fibril formation.
Amyloid formation
Lipid-modulated protein aggregation
Membrane interaction
Nanodiscs
α-Synuclein
αSyn-LiPs
Journal
Chemistry and physics of lipids
ISSN: 1873-2941
Titre abrégé: Chem Phys Lipids
Pays: Ireland
ID NLM: 0067206
Informations de publication
Date de publication:
05 2019
05 2019
Historique:
received:
31
10
2018
revised:
21
02
2019
accepted:
22
02
2019
pubmed:
4
3
2019
medline:
15
2
2020
entrez:
4
3
2019
Statut:
ppublish
Résumé
Aggregation of the protein α-Synuclein (αSyn) is of great interest due to its involvement in the pathology of Parkinson's disease. However, under in vitro conditions αSyn is very soluble and kinetically stable for extended time periods. As a result, most αSyn aggregation assays rely on conditions that artificially induce or enhance aggregation, often by introducing rather non-native conditions. It has been shown that αSyn interacts with membranes and conditions have been identified in which membranes can promote as well as inhibit αSyn aggregation. It has also been shown that αSyn has the intrinsic capability to assemble lipid-protein-particles, in a similar way as apolipoproteins can form lipid-bilayer nanodiscs. Here we show that these αSyn-lipid particles (αSyn-LiPs) can also effectively induce, accelerate or inhibit αSyn aggregation, depending on the applied conditions. αSyn-LiPs therefore provide a general platform and additional tool, complementary to other setups, to study various aspects of αSyn amyloid fibril formation.
Identifiants
pubmed: 30826264
pii: S0009-3084(18)30213-5
doi: 10.1016/j.chemphyslip.2019.02.009
pmc: PMC6451039
pii:
doi:
Substances chimiques
Amyloid
0
Lipids
0
alpha-Synuclein
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
57-65Informations de copyright
Copyright © 2019 The Authors. Published by Elsevier B.V. All rights reserved.
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