NeuroMolecular Medicine

, Volume 11, Issue 4, pp 239–251

Interaction Between α-Synuclein and Metal Ions, Still Looking for a Role in the Pathogenesis of Parkinson’s Disease


  • Marco Bisaglia
    • Department of BiologyUniversity of Padova
  • Isabella Tessari
    • Department of BiologyUniversity of Padova
  • Stefano Mammi
    • Department of Chemical SciencesUniversity of Padova
    • Department of BiologyUniversity of Padova
Original Paper

DOI: 10.1007/s12017-009-8082-1

Cite this article as:
Bisaglia, M., Tessari, I., Mammi, S. et al. Neuromol Med (2009) 11: 239. doi:10.1007/s12017-009-8082-1


The most recent literature on the interaction between α-synuclein in its several aggregation states and metal ions is discussed. This analysis shows two major types of interactions. Binding sites are present in the C-terminal region, and similar, low affinity (in the millimolar range) is exhibited toward many different metal ions, including copper and iron. A more complex scenario emerges for these latter metal ions, which are also able to coordinate with high affinity (in the micromolar range) to the N-terminal region of α-synuclein. Moreover, these redox-active metal ions may induce chemical modifications on the protein in vitro and in the reducing intracellular environment, and these modifications might be relevant for the aggregation properties of α-synuclein. Finally, an attempt is made to contextualize the interaction between α-synuclein and these metal ions in the framework of the elusive and multifactorial pathogenesis of Parkinson’s disease.



Copyright information

© Humana Press Inc. 2009