4.8 Article

Copper(II) binding to α-synuclein, the Parkinson's protein

Journal

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 130, Issue 22, Pages 6898-+

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/ja711415b

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Funding

  1. Intramural NIH HHS [Z01 HL001055-01] Funding Source: Medline
  2. NIDDK NIH HHS [DK19038, R37 DK019038, R01 DK019038] Funding Source: Medline
  3. NIGMS NIH HHS [GM068461, R01 GM068461] Funding Source: Medline

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Variations in tryptophan fluorescence intensities confirm that copper(II) interacts with a-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 similar to 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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