Aggregation of the amyloid-β peptide (Aβ40) within condensates generated through liquid-liquid phase separation.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
30 Sep 2024
30 Sep 2024
Historique:
received:
18
05
2024
accepted:
05
09
2024
medline:
1
10
2024
pubmed:
1
10
2024
entrez:
30
9
2024
Statut:
epublish
Résumé
The deposition of the amyloid-β (Aβ) peptide into amyloid fibrils is a hallmark of Alzheimer's disease. Recently, it has been reported that some proteins can aggregate and form amyloids through an intermediate pathway involving a liquid-like condensed phase. These observations prompted us to investigate the phase space of Aβ. We thus explored the ability of Aβ to undergo liquid-liquid phase separation, and the subsequent liquid-to-solid transition that takes place within the resulting condensates. Through the use of microfluidic approaches, we observed that the 40-residue form of Αβ (Αβ40) can undergo liquid-liquid phase separation, and that accessing a liquid-like intermediate state enables Αβ40 to self-assemble and aggregate into amyloid fibrils through this pathway. These results prompt further studies to investigate the possible role of Αβ liquid-liquid phase separation and its subsequent aggregation in the context of Alzheimer's disease and more generally on neurodegenerative processes.
Identifiants
pubmed: 39349560
doi: 10.1038/s41598-024-72265-7
pii: 10.1038/s41598-024-72265-7
doi:
Substances chimiques
Amyloid beta-Peptides
0
Peptide Fragments
0
Protein Aggregates
0
amyloid beta-protein (1-40)
0
Amyloid
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
22633Subventions
Organisme : UK Research and Innovation
ID : 10059436
Organisme : UKRI
ID : 10061100
Informations de copyright
© 2024. The Author(s).
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