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Issue 3, 2011
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Copper(II) enhances membrane-bound α-synuclein helix formation

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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.

Graphical abstract: Copper(ii) enhances membrane-bound α-synuclein helix formation

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Publication details

The article was received on 24 Nov 2010, accepted on 20 Jan 2011 and first published on 03 Feb 2011


Article type: Communication
DOI: 10.1039/C0MT00088D
Citation: Metallomics, 2011,3, 280-283
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    Copper(II) enhances membrane-bound α-synuclein helix formation

    H. R. Lucas and J. C. Lee, Metallomics, 2011, 3, 280
    DOI: 10.1039/C0MT00088D

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