Cu2+-binding to S100B triggers polymerization of disulfide cross-linked tetramers with enhanced chaperone activity against amyloid-β aggregation. Issue 3 (16th December 2020)

• Record Type: Journal Article
• Authors: 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.
• Is Part Of: Chemical communications. Volume 57:Issue 3(2021)
• Page Start: 379
• Page End: 382
• Publication Date: 2020-12-16
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/d0cc06842j
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : A mechanism of chemical regulation of the S100B chaperone via Cu 2+ induced assembly of S100B cross-linked oligomers with enhanced anti-amyloid aggregation activity. Abstract : S100B is an extracellular protein implicated in Alzheimer's Disease and a suppressor of amyloid-β aggregation. Herein we report a mechanism tying Cu 2+ 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.