Tau is responsible for microtubule stabilization in neuronal cells and its activity is regulated by kinase catalyzed phosphorylation. However, hyperphosphorylation of tau disturbs and inhibits microtubule assembly and plays a key role in neurodegenerative diseases. There is also some evidence that the disturbance of metal ions levels in the brain are involved in tau biochemistry and may influence tau aggregation and/or its hyperphosphorylation.1-3 We previously reported on the interaction of Cu2+ with tau.4 In this contribution, we probe the interaction of Fe2+ and Fe3+ with tau-410. Immobilized non-phosphorylated tau (n-tau) and phosphorylated tau (p-tau) on gold surfaces are redox silent before exposure to Fe2+ and Fe3+ solutions but exhibit a Fe-based redox response after exposure. The electrochemical response was used for monitoring the iron uptake of n-tau and p-tau. We also investigated the influence of pH, temperature and incubation time on the iron/tau interaction. A competitive study was carried out with Zn2+ and Cu2+ in order to understand the affinity of these metal ions for n-tau and p-tau. X-ray photoelectron spectroscopy (XPS) was used as supporting technique for the characterization of all metal-tau gold surfaces. 1.Greenough, M.A.; Camakaris, J.; Bush, A. Metal dyshomeostasis and oxidative stress in Alzheimer's disease. Neurochem Int. 2013, 62(5),540-55 2.Martic, S.; Beheshti, S.; Rains, M. K.; Kraatz, H. B. Electrochemical investigations into Tau protein phosphorylations. Analyst 2012, 137, 2042-2046 3.Rains, M. K.; Martic, S.; Freeman, D.; Kraatz, H. B. Electrochemical investigations into kinase-catalyzed transformations of tau protein. ACS Chem. Neurosci. 2013, 4, 1194-1203 4.Martic, S.; Rains, M. K.; Kraatz, H.-B. Probing copper/tau protein interactions electrochemically. Anal. Biochem. 2013, 442, 130-137

Protein-based biosensor for probing the iron/tau interaction

249th National Meeting (2015)

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