Cu
Amyloid beta-Peptides
/ antagonists & inhibitors
Binding Sites
Copper
/ chemistry
Cross-Linking Reagents
/ chemical synthesis
Disulfides
/ chemistry
Humans
Models, Molecular
Molecular Chaperones
/ metabolism
Polymerization
Protein Aggregates
/ drug effects
Protein Aggregation, Pathological
/ drug therapy
S100 Calcium Binding Protein beta Subunit
/ chemistry
Journal
Chemical communications (Cambridge, England)
ISSN: 1364-548X
Titre abrégé: Chem Commun (Camb)
Pays: England
ID NLM: 9610838
Informations de publication
Date de publication:
14 Jan 2021
14 Jan 2021
Historique:
pubmed:
17
12
2020
medline:
16
6
2021
entrez:
16
12
2020
Statut:
ppublish
Résumé
S100B is an extracellular protein implicated in Alzheimer's Disease and a suppressor of amyloid-β aggregation. Herein we report a mechanism tying Cu2+ binding to a change in assembly state yielding disulfide cross-linked oligomers with higher anti-aggregation activity. This chemical control of chaperone function illustrates a regulatory process relevant under metal and proteostasis dysfunction as in neurodegeneration.
Substances chimiques
Amyloid beta-Peptides
0
Cross-Linking Reagents
0
Disulfides
0
Molecular Chaperones
0
Protein Aggregates
0
S100 Calcium Binding Protein beta Subunit
0
S100B protein, human
0
Copper
789U1901C5
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM