Your browser doesn't support javascript.
loading
Cu2+-binding to S100B triggers polymerization of disulfide cross-linked tetramers with enhanced chaperone activity against amyloid-ß aggregation.
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.
Affiliation
  • Cristóvão JS; Biosystems and Integrative Sciences Institute, Faculdade de Ciências, Universidade de Lisboa, Lisboa 1749-016, Portugal. cmgomes@fc.ul.pt.
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.
Subject(s)
Fulltext
Add to My VHL
Print
XML
PubMed Links
Search on Google

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
Fulltext
Add to My VHL
Print
XML
PubMed Links
Search on Google

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