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

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Abstract

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.

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Authors and Affiliations

  1. Department of Biology, University of Padova, Via U. Bassi 58/B, 35121, Padova, Italy

    Marco Bisaglia, Isabella Tessari & Luigi Bubacco

  2. Department of Chemical Sciences, University of Padova, Via F. Marzolo 1, 35131, Padova, Italy

    Stefano Mammi

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  1. Marco Bisaglia
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  2. Isabella Tessari
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  3. Stefano Mammi
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  4. Luigi Bubacco
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Correspondence to Luigi Bubacco.

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Bisaglia, M., Tessari, I., Mammi, S. et al. Interaction Between α-Synuclein and Metal Ions, Still Looking for a Role in the Pathogenesis of Parkinson’s Disease. Neuromol Med 11, 239–251 (2009). https://doi.org/10.1007/s12017-009-8082-1

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  • DOI: https://doi.org/10.1007/s12017-009-8082-1

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