Copper(II) enhances membrane-bound α-synuclein helix formation

Heather R. Lucas; Jennifer C. Lee

doi:10.1039/C0MT00088D

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Copper(ii) enhances membrane-bound α-synuclein helix formation†‡

Heather R. Lucas^a and Jennifer C. Lee*^a

Author affiliations

* Corresponding authors

^a Laboratory of Molecular Biophysics, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, USA
E-mail: leej4@mail.nih.gov

Abstract

Interactions of copper and membranes with α-synuclein have been implicated in pathogenic mechanisms of Parkinson's disease, yet work examining both concurrently is scarce. We have examined the effect of copper(II) on protein/vesicle binding and found that both the copper(II) affinity and α-helical content are enhanced for the membrane-bound protein.