Journal article

Cu2 binding modes of recombinant alpha-synuclein - Insights from EPR spectroscopy

Simon C Drew, Su Ling Leong, Chi LL Pham, Deborah J Tew, Colin L Masters, Luke A Miles, Roberto Cappai, Kevin J Barnham

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | AMER CHEMICAL SOC | Published : 2008

Abstract

The interaction of the small (140 amino acid) protein, alpha-synuclein (alphaS), with Cu(2+) has been proposed to play a role in Parkinson's disease (PD). While some insight from truncated model complexes has been gained, the nature of the corresponding Cu(2+) binding modes in the full length protein remains comparatively less well characterized. This work examined the Cu(2+) binding of recombinant human alphaS using Electron Paramagnetic Resonance (EPR) spectroscopy. Wild type (wt) alphaS was shown to bind stoichiometric Cu(2+) via two N-terminal binding modes at physiological pH. An H50N mutation isolated one binding mode, whose g parallel, A parallel, and metal-ligand hyperfine parameters..

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