%0 Journal Article
%A Miotto, Marco C.
%A Valiente-Gabioud, Ariel A.
%A Rossetti, Giulia
%A Zweckstetter, Markus
%A Carloni, Paolo
%A Selenko, Philipp
%A Griesinger, Christian
%A Binolfi, Andres
%A Fernández, Claudio O.
%T Copper Binding to the N-Terminally Acetylated, Naturally Occurring Form of Alpha-Synuclein Induces Local Helical Folding
%J Journal of the American Chemical Society
%V 137
%N 20
%@ 1520-5126
%C Washington, DC
%I American Chemical Society
%M FZJ-2015-05061
%P 6444 - 6447
%D 2015
%X Growing evidence supports a link between brain copper homeostasis, the formation of alpha-synuclein (AS)-copper complexes, and the development of Parkinson disease (PD). Recently it was demonstrated that the physiological form of AS is N-terminally acetylated (AcAS). Here we used NMR spectroscopy to structurally characterize the interaction between Cu(I) and AcAS. We found that the formation of an AcAS–Cu(I) complex at the N-terminal region stabilizes local conformations with α-helical secondary structure and restricted motility. Our work provides new evidence into the metallo-biology of PD and opens new lines of research as the formation of AcAS–Cu(I) complex might impact on AcAS membrane binding and aggregation.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000355383500006
%$ pmid:25939020
%R 10.1021/jacs.5b01911
%U https://juser.fz-juelich.de/record/202935