On the Cluster Formation of α-Synuclein Fibrils.
Lewy bodies (LB)
alpha-synuclein
amyloid fibril
fractal cluster
rigid-rod cluster modeling
small-angle neutron scattering (SANS)
Journal
Frontiers in molecular biosciences
ISSN: 2296-889X
Titre abrégé: Front Mol Biosci
Pays: Switzerland
ID NLM: 101653173
Informations de publication
Date de publication:
2021
2021
Historique:
received:
31
08
2021
accepted:
30
09
2021
entrez:
5
11
2021
pubmed:
6
11
2021
medline:
6
11
2021
Statut:
epublish
Résumé
The dense accumulation of α-Synuclein fibrils in neurons is considered to be strongly associated with Parkinson's disease. These intracellular inclusions, called Lewy bodies, also contain significant amounts of lipids. To better understand such accumulations, it should be important to study α-Synuclein fibril formation under conditions where the fibrils lump together, mimicking what is observed in Lewy bodies. In the present study, we have therefore investigated the overall structural arrangements of α-synuclein fibrils, formed under mildly acidic conditions, pH = 5.5, in pure buffer or in the presence of various model membrane systems, by means of small-angle neutron scattering (SANS). At this pH, α-synuclein fibrils are colloidally unstable and aggregate further into dense clusters. SANS intensities show a power law dependence on the scattering vector,
Identifiants
pubmed: 34738016
doi: 10.3389/fmolb.2021.768004
pii: 768004
pmc: PMC8560691
doi:
Types de publication
Journal Article
Langues
eng
Pagination
768004Informations de copyright
Copyright © 2021 Dubackic, Idini, Lattanzi, Liu, Martel, Terry, Haertlein, Devos, Jackson, Sparr, Linse and Olsson.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
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