Insights into the thermodynamics of copper association with amyloid-β, α-synuclein and prion proteins.
This review examines recent studies on the thermodynamics of copper association with amyloid-β, α-synuclein and prion protein, with an eye towards using this information to understand the etiology of associated neurodegenerative diseases. A variety of binding affinities and binding sites, which are essential to understand the function and consequence of copper-protein interaction, have been reported for copper to these three neurobiologic systems. This current review reconciles the disparate models presented in the literature.
Department of Chemistry, Duke University, Durham, NC 27708, USA. Lian.hong@duke.edu
Lian
L
Hong
John D
JD
Simon
D016229:Amyloid beta-Peptides / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D003300:Copper / Q000378:metabolism*; D006801:Humans; D019636:Neurodegenerative Diseases / Q000378:metabolism*; D011328:Prions / Q000378:metabolism*; D011485:Protein Binding; D051844:alpha-Synuclein / Q000378:metabolism*
D016229:Amyloid beta-Peptides; D011328:Prions; D051844:alpha-Synuclein; D003300:Copper