Site-specific interactions of Cu(II) with alpha and beta-synuclein: bridging the molecular gap between metal binding and aggregation.

@article{Binolfi2008SitespecificIO,
  title={Site-specific interactions of Cu(II) with alpha and beta-synuclein: bridging the molecular gap between metal binding and aggregation.},
  author={Andr{\'e}s Binolfi and Gonzalo R. Lamberto and Rosario Duran and Liliana Quintanar and Carlos W. Bertoncini and Jos{\'e} Roberto Matos Souza and Carlos Cerve{\~n}ansky and Markus Zweckstetter and Christian Griesinger and Claudio O Fern{\'a}ndez},
  journal={Journal of the American Chemical Society},
  year={2008},
  volume={130 35},
  pages={11801-12}
}
The aggregation of alpha-synuclein (AS) is a critical step in the etiology of Parkinson's disease (PD) and other neurodegenerative synucleinopathies. Protein-metal interactions play a critical role in AS aggregation and might represent the link between the pathological processes of protein aggregation and oxidative damage. Our previous studies established a hierarchy in AS-metal ion interactions, where Cu(II) binds specifically to the protein and triggers its aggregation under conditions that… CONTINUE READING

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