Cu2+-binding to S100B triggers polymerization of disulfide cross-linked tetramers with enhanced chaperone activity against amyloid-β aggregation

Cu2+-binding to S100B triggers polymerization of disulfide cross-linked tetramers with enhanced chaperone activity against amyloid-β aggregation

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...

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Veröffentlicht in:Chemical communications (Cambridge, England) England), 2021-01, Vol.57 (3), p.379-382
Hauptverfasser: Cristóvão, Joana S, Moreira, Guilherme G, Rodrigues, Filipe E P, Carapeto, Ana P, Rodrigues, Mário S, Cardoso, Isabel, Ferreira, António E N, Machuqueiro, Miguel, Fritz, Guenter, Gomes, Cláudio M
Format: Artikel
Sprache:eng
Schlagworte:
Agglomeration
Alzheimer's disease
Binding
Chemical activity
Copper
Crosslinking
Oligomers
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Beschreibung
Zusammenfassung: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.
ISSN:1359-7345
1364-548X
DOI:10.1039/d0cc06842j