Copper(II) Binding to α-Synuclein, the Parkinson’s Protein
Open Access
- 9 May 2008
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 130 (22), 6898-6899
- https://doi.org/10.1021/ja711415b
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 (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.Keywords
This publication has 32 references indexed in Scilit:
- Copper and the Prion Protein: Methods, Structures, Function, and DiseaseAnnual Review of Physical Chemistry, 2007
- Copper Homeostasis and Neurodegenerative Disorders (Alzheimer's, Prion, and Parkinson's Diseases and Amyotrophic Lateral Sclerosis)Chemical Reviews, 2006
- Copper(ii) binding by fragments of α-synuclein containing M1-D2- and -H50-residues; a combined potentiometric and spectroscopic studyDalton Transactions, 2006
- The new mutation, E46K, of α‐synuclein causes parkinson and Lewy body dementiaAnnals of Neurology, 2003
- α-Synuclein Locus Triplication Causes Parkinson's DiseaseScience, 2003
- Certain Metals Trigger Fibrillation of Methionine-oxidized α-SynucleinJournal of Biological Chemistry, 2003
- Transition Metal Speciation in the Cell: Insights from the Chemistry of Metal Ion ReceptorsScience, 2003
- Metal-triggered Structural Transformations, Aggregation, and Fibrillation of Human α-SynucleinJournal of Biological Chemistry, 2001
- AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's diseaseNature Genetics, 1998
- Mutation in the α-Synuclein Gene Identified in Families with Parkinson's DiseaseScience, 1997