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Copper(II) enhances membrane-bound ?-synuclein helix formation.

ABSTRACT: Interactions of copper and membranes with ?-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 ?-helical content are enhanced for the membrane-bound protein.

SUBMITTER: Lucas HR 

PROVIDER: S-EPMC3196632 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature

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

Lucas Heather R HR   Lee Jennifer C JC  

Metallomics : integrated biometal science 20110203 3

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. ...[more]

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