Ubiquitin binds the amyloid β peptide and interferes with its clearance pathways.
Journal
Chemical science
ISSN: 2041-6520
Titre abrégé: Chem Sci
Pays: England
ID NLM: 101545951
Informations de publication
Date de publication:
07 Mar 2019
07 Mar 2019
Historique:
received:
31
07
2018
accepted:
09
01
2019
entrez:
19
4
2019
pubmed:
19
4
2019
medline:
19
4
2019
Statut:
epublish
Résumé
Several lines of evidence point to a compromised proteostasis associated with a reduction of the Ubiquitin Proteasome System (UPS) activity in patients affected by Alzheimer's Disease (AD) and suggest that the amyloid β peptide (Aβ) is an important player in the game. Inspired also by many reports, underlining the presence of ubiquitin (Ub) in the amyloid plaques of AD brains, here we set out to test whether Ub may bind the Aβ peptide and have any effect on its clearance pathways. By using an integrated array of MALDI-TOF/UPLC-HRMS, fluorescence, NMR, SPR, Microscale Thermophoresis (MST) and molecular dynamics studies, we consistently demonstrated that Aβ40 binds Ub with a 1 : 1 stoichiometry and
Identifiants
pubmed: 30996991
doi: 10.1039/c8sc03394c
pii: c8sc03394c
pmc: PMC6419943
doi:
Types de publication
Journal Article
Langues
eng
Pagination
2732-2742Références
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