Ions and intrinsically disordered proteins

Ions often interact with intrinsically disordered proteins and their affinity is high enough to compete with structured proteins. When ions have accessible d orbitals, the possible catalytic activity of the species is often out of control and, therefore, potentially dangerous for cells. In this presentation, I shall discuss models of such systems, with the aim at providing tools to dissect the features characterizing structures and properties emerging from disorder. Examples will be given for copper ions interacting with the amyloid-beta peptide [1], complexes that are involved in the production of reactive oxygen species [2], and for magnesium interacting with RNA and osteopontin [3], complexes involved in signaling. [1] P.D.Q. Huy et al., ACS Chem. Neurosci., 2016, http://dx.doi.org/10.1021/acschemneuro.6b00109 [2] C. Cheignon et al., Redox Biol., 2018, http://dx.doi.org/j.redox.2017.10.014 [3] G. La Penna, R. Chelli, Frontiers Chem., 2018.