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Updated: Jun 4, 2026

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time
Published on: May 30, 2021
Copper(II) enhances membrane-bound α-synuclein helix formation
Heather R Lucas1, Jennifer C Lee
1Laboratory of Molecular Biophysics, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.
Abstract:
Interactions of copper and membranes with α-synuclein have been implicated in pathogenic mechanisms of Parkinson's disease, yet work examining both concurrently is scarce. We have examined the effect of copper(ii) on protein/vesicle binding and found that both the copper(ii) affinity and α-helical content are enhanced for the membrane-bound protein.
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