Cu2+-binding to S100B triggers polymerization of disulfide cross-linked tetramers with enhanced chaperone activity against amyloid-ß aggregation.
Chem Commun (Camb)
; 57(3): 379-382, 2021 Jan 14.
Article
in En
| MEDLINE
| ID: mdl-33326534
ABSTRACT
S100B is an extracellular protein implicated in Alzheimer's Disease and a suppressor of amyloid-ß 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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Amyloid beta-Peptides
/
Copper
/
Cross-Linking Reagents
/
Disulfides
/
S100 Calcium Binding Protein beta Subunit
/
Protein Aggregation, Pathological
Limits:
Humans
Language:
En
Journal:
Chem Commun (Camb)
Journal subject:
QUIMICA
Year:
2021
Document type:
Article
Affiliation country:
Portugal