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

Jennifer C. Lee, Harry B. Gray, Jay R. Winkler

Journal of the American Chemical Society · 2008 · ▲ 248 citations

Loss of proteostasis

Abstract

Variations in tryptophan fluorescence intensities confirm that copper(II) interacts with alpha-synuclein, a protein implicated in Parkinson's disease. Trp4 fluorescence decay kinetics measured for the F4W protein show that Cu(II) binds tightly (Kd 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.

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Provenance

Source: OpenAlex
DOI: 10.1021/ja711415b
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Fetched: 2026-10-27 MST

Cite this

APA

Lee, J.C., Gray, H.B., & Winkler, J.R. (2008). Copper(II) Binding to α-Synuclein, the Parkinson’s Protein. <em>Journal of the American Chemical Society</em>. https://doi.org/10.1021/ja711415b

Vancouver

Lee JC, Gray HB, Winkler JR. Copper(II) Binding to α-Synuclein, the Parkinson’s Protein. Journal of the American Chemical Society. 2008. doi:10.1021/ja711415b.

BibTeX

@article{jennifer2008Copper, title = {Copper(II) Binding to α-Synuclein, the Parkinson’s Protein}, author = {Jennifer C. Lee and Harry B. Gray and Jay R. Winkler}, journal = {Journal of the American Chemical Society}, year = {2008}, doi = {10.1021/ja711415b}, }