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Published June 4, 2008 | Supplemental Material + Published
Journal Article Open

Copper(II) Binding to α-Synuclein, the Parkinson's Protein

Abstract

Variations in tryptophan fluorescence intensities confirm that copper(II) interacts with α-synuclein, a protein implicated in Parkinson's disease. Trp4 fluorescence decay kinetics measured for the F4W protein show that Cu(II) binds tightly (K_d ∼ 100 nM) near the N-terminus at pH 7. Work on a F4W/H50S mutant indicates that a histidine imidazole is not a ligand in this high-affinity site.

Additional Information

© 2008 American Chemical Society. ACS AuthorChoice. Received December 26, 2007; Publication Date (Web): May 9, 2008. Supported by the Intramural Research Program of the National Institutes of Health, the National Heart, Lung, and Blood Institute (JCL), and grants from the Ellison Medical Foundation (Senior Scholar Award in Aging to H.B.G.) and NIH (GM068461 to J.R.W.; DK19038 to H.B.G.). Initial work was supported by a Beckman Senior Research Fellowship (J.C.L.).

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Supplemental Material - ja711415b-file002.pdf

Supplemental Material - ja711415b-file003.pdf

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Supplemental Material - ja711415b-file005.pdf

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