TY  - JOUR
AU  - Miotto, Marco C.
AU  - Valiente-Gabioud, Ariel A.
AU  - Rossetti, Giulia
AU  - Zweckstetter, Markus
AU  - Carloni, Paolo
AU  - Selenko, Philipp
AU  - Griesinger, Christian
AU  - Binolfi, Andres
AU  - Fernández, Claudio O.
TI  - Copper Binding to the N-Terminally Acetylated, Naturally Occurring Form of Alpha-Synuclein Induces Local Helical Folding
JO  - Journal of the American Chemical Society
VL  - 137
IS  - 20
SN  - 1520-5126
CY  - Washington, DC
PB  - American Chemical Society
M1  - FZJ-2015-05061
SP  - 6444 - 6447
PY  - 2015
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000355383500006
C6  - pmid:25939020
DO  - DOI:10.1021/jacs.5b01911
UR  - https://juser.fz-juelich.de/record/202935
ER  -