Work

Copper(ii) enhances membrane-bound α-synuclein helix formation

Year: 2011

Type: article

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. Copper(ii) binding to the N-terminus of α-synuclein affects its helical propensity and affinity for lipid vesicles.

Source: Metallomics

DOI: 10.1039/c0mt00088d

Authors: Heather R. Lucas, Jennifer C. Lee

Institutions: National Institutes of Health, National Heart, Lung, and Blood Institute

Language: English

Topic: Parkinson's Disease Mechanisms and Treatments

Subfield: Neurology

Field: Medicine

Domain: Health Sciences

SDG: Good health and well-being

Open Access status: green

Funder: National Institutes of Health