Artículo
Copper Binding to the N‑Terminally Acetylated, Naturally Occurring Form of Alpha-Synuclein Induces Local Helical Folding
Miotto, Marco César
; Valiente Gabioud, Ariel Alejandro
; Rossetti, Giulia; Zweckstetter, Markus; Carloni, Paolo; Selenko, Philipp; Griesinger, Christian; Binolfi, Andrés
; Fernandez, Claudio Oscar
Fecha de publicación:
05/2015
Editorial:
American Chemical Society
Revista:
Journal of the American Chemical Society
ISSN:
0002-7863
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
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.
Palabras clave:
Cu(I)
,
Synuclein
,
Conformational Transition
,
Parkinson
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Licencia
Identificadores
Colecciones
Articulos(CCT - ROSARIO)
Articulos de CTRO.CIENTIFICO TECNOL.CONICET - ROSARIO
Articulos de CTRO.CIENTIFICO TECNOL.CONICET - ROSARIO
Citación
Miotto, Marco César; Valiente Gabioud, Ariel Alejandro; Rossetti, Giulia; Zweckstetter, Markus; Carloni, Paolo; et al.; Copper Binding to the N‑Terminally Acetylated, Naturally Occurring Form of Alpha-Synuclein Induces Local Helical Folding; American Chemical Society; Journal of the American Chemical Society; 137; 20; 5-2015; 6444-6447
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