Open AccessCopper(ii) enhances membrane-bound α-synuclein helix formation
Author(s) -
Heather R. Lucas,
Jennifer C. Lee
Publication year - 2011
Publication title -
metallomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.012
H-Index - 75
eISSN - 1756-591X
pISSN - 1756-5901
DOI - 10.1039/c0mt00088d
Subject(s) - copper , membrane , helix (gastropod) , chemistry , biophysics , crystallography , biochemistry , biology , organic chemistry , ecology , snail
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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