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 |
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| container_end_page | 382 |
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| container_issue | 3 |
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| container_title | Chemical communications (Cambridge, England) |
| container_volume | 57 |
| creator | 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 |
| description | 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. |
| doi_str_mv | 10.1039/d0cc06842j |
| format | Article |
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| fulltext | fulltext |
| identifier | ISSN: 1359-7345 |
| ispartof | Chemical communications (Cambridge, England), 2021-01, Vol.57 (3), p.379-382 |
| issn | 1359-7345 1364-548X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2470897541 |
| source | Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
| subjects | Agglomeration Alzheimer's disease Binding Chemical activity Copper Crosslinking Oligomers |
| title | Cu2+-binding to S100B triggers polymerization of disulfide cross-linked tetramers with enhanced chaperone activity against amyloid-β aggregation |
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