Exploring the Structural Details of Cu(I) Binding to alpha-Synuclein by NMR Spectroscopy

ANDRÉS BINOLFI; ARIEL A. VALIENTE-GABIOUD; ROSARIO DURÁN; MARKUS ZWECKSTETTER; CHRISTIAN GRIESINGER; CLAUDIO O. FERNÁNDEZ

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

AMER CHEMICAL SOC

Lugar: Washington; Año: 2011 vol. 133 p. 194 - 196

0002-7863

The aggregation of alpha-synuclein (AS) is selectively enhanced by copper in vitro, and the interaction is proposed to play a potential role in vivo. In this work, we report the structural, residue-specific characterization of Cu(I) binding to AS and demonstrate that the protein is able to bind Cu(I) with relatively high affinity in a coordination environment that involves the participation of Met1 and Met5 residues. This knowledge is a key to understanding the structural-aggregation basis of the copper-catalyzed oxidation of AS.