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Article Dans Une Revue Chemical Society Reviews Année : 2017

Chemistry of Mammalian Metallothioneins and their Interaction with Amyloidogenic Peptides and Proteins

Résumé

Cu and Zn ions are essential in most living beings. Their metabolism is critical for health and mis-metabolism can be lethal. In the last two decades, a large body of evidence has reported the role copper, zinc and iron, and oxidative stress in several neurodegenerative diseases like Alzheimer, Parkinson, Prion, etc. To what extend this mis-metabolism is causative or a consequence of these diseases is still a matter of research. In this context metallothioneins (MTs) appear to play a central gate-keeper role in controlling aberrant metal-protein interactions. MTs are small proteins that can bind high amounts of Zn(II) and Cu(I) ions in metal-cluster arrangements via their cysteines thiolates. Moreover, MTs are well known antioxidants. The present tutorial outlines the chemistry underlying the interconnection between copper(I/II) and zinc(II) coordination to amyloidogenic proteins and MTs, and their redox properties in generation and/or silencing reactive oxygen species (overproduced in oxidative stress) and other reactants. These studies have revealed the coordination chemistry involved in neurodegenerative diseases and the interactions between MTs with amyloidogenic proteins metal-complexes (like amyloid-β, α-synuclein and prion-protein). Overall, a protective role of MTs in neurodegenerative processes is emerging, serving as a foundation for exploring MTs chemistry as inspiration for therapeutic approaches.
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Dates et versions

hal-01635419 , version 1 (15-11-2017)

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Paternité - Pas d'utilisation commerciale

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Elena Atrián-Blasco, Alice Santoro, Dean L. Pountney, Gabriele Meloni, Christelle Hureau, et al.. Chemistry of Mammalian Metallothioneins and their Interaction with Amyloidogenic Peptides and Proteins. Chemical Society Reviews, 2017, 46 (24), pp.7683-7693. ⟨10.1039/C7CS00448F⟩. ⟨hal-01635419⟩
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