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Download Hi-Res ImageDownload to MS-PowerPointCite This:Inorg. Chem. 2009, 48, 19, 9303-9307
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Identification of the Minimal Copper(II)-Binding α-Synuclein Sequence

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Laboratory of Molecular Biophysics, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892-8013
*To whom correspondence should be addressed. E-mail: [email protected]
Cite this: Inorg. Chem. 2009, 48, 19, 9303–9307
Publication Date (Web):September 10, 2009
https://doi.org/10.1021/ic901157w
Copyright © 2009 American Chemical Society
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    Abstract

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    Parkinson’s disease has been long linked to environmental factors, such as transition metals and recently to α-synuclein, a presynaptic protein. Using tryptophan-containing peptides, we identified the minimal Cu(II)-binding sequence to be within the first four residues, MDV(F/W), anchored by the α-amino terminus. In addition, mutant peptide 1−10 (Lys → Arg) verified that neither Lys6 nor Lys10 are necessary for Cu(II) binding. Interestingly, Trp4 excited-state decay kinetics measured for peptides and proteins reveal two quenching modes, possibly arising from two distinct Cu(II)−polypeptide structures.

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