Redox-Dependent Copper Ion Modulation of Amyloid-β (1-42) Aggregation In Vitro.
Alzheimer’s disease
aggregation
amyloid
amyloid-β
copper
inhibition
kinetics
Journal
Biomolecules
ISSN: 2218-273X
Titre abrégé: Biomolecules
Pays: Switzerland
ID NLM: 101596414
Informations de publication
Date de publication:
18 06 2020
18 06 2020
Historique:
received:
15
05
2020
revised:
12
06
2020
accepted:
16
06
2020
entrez:
24
6
2020
pubmed:
24
6
2020
medline:
13
4
2021
Statut:
epublish
Résumé
Plaque deposits composed of amyloid-β (Aβ) fibrils are pathological hallmarks of Alzheimer's disease (AD). Although copper ion dyshomeostasis is apparent in AD brains and copper ions are found co-deposited with Aβ peptides in patients' plaques, the molecular effects of copper ion interactions and redox-state dependence on Aβ aggregation remain elusive. By combining biophysical and theoretical approaches, we here show that Cu
Identifiants
pubmed: 32570820
pii: biom10060924
doi: 10.3390/biom10060924
pmc: PMC7355640
pii:
doi:
Substances chimiques
Amyloid beta-Peptides
0
Ions
0
Peptide Fragments
0
Protein Aggregates
0
Recombinant Proteins
0
amyloid beta-protein (1-42)
0
Copper
789U1901C5
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Vetenskapsrådet
ID : 2016-03902
Pays : International
Organisme : Vetenskapsrådet
ID : 2019-03673
Pays : International
Organisme : Knut och Alice Wallenbergs Stiftelse
ID : Wallenberg Scholar Program
Pays : International
Organisme : Nanoscience and Nanotechnology Area of Advance, Chalmers Tekniska Högskola
ID : Excellence PhD program
Pays : International
Organisme : Nanoscience and Nanotechnology Area of Advance, Chalmers Tekniska Högskola
ID : n/a
Pays : International
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