Please use this identifier to cite or link to this item:
Title: Differences in the Binding of Copper(I) to α- and β-Synuclein
Authors: Riccardo De, Ricco
Valensin, Daniela 
Simone, Dell’Acqua
Luigi, Casella
Gaggelli, Elena 
Valensin, Gianni 
Luigi, Bubacco
Mangani, Stefano 
Issue Date: 2015
Project: None 
Parkinson's disease (PD) is a neurodegenerative disorder characterized by the presence of abnormal α-synuclein (αS) deposits in the brain. Alterations in homeostasis and metal-induced oxidative stress may play a crucial role in the progression of αS amyloid assembly and pathogenesis of PD. Contrary to αS, β-synuclein (βS) is not involved in the PD etiology. However, it has been suggested that the βS/αS ratio is altered in PD, indicating that a correct balance of these two proteins is implicated in the inhibition of αS aggregation. αS and βS share similar abilities to coordinate Cu(II). In this study, we investigated and compared the interaction of Cu(I) with the N-terminal portion of βS and αS by means of NMR, circular dichroism, and X-ray absorption spectroscopies. Our data show the importance of M10K mutation, which induces different Cu(I) chemical environments. Coordination modes 3S1O and 2S2O were identified for βS and αS, respectively. These new insights into the bioinorganic chemistry of copper and synuclein proteins are a basis to understand the molecular mechanism by which βS might inhibit αS aggregation.
ISSN: 0020-1669
DOI: 10.1021/ic502407w
Appears in Collections:Publications

Show full item record

Google ScholarTM



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.