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

[Image: see text] 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...

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Detalles Bibliográficos
Autores principales: Lee, Jennifer C., Gray, Harry B., Winkler, Jay R.
Formato: Texto
Lenguaje:English
Publicado: American Chemical Society 2008
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2664836/
https://www.ncbi.nlm.nih.gov/pubmed/18465859
http://dx.doi.org/10.1021/ja711415b
Descripción
Sumario:[Image: see text] 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.

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