Electrochemical analysis Aβ42 peptide adsorption and aggregation on spectroscopic graphite

Formation of pathological amyloid fibrils in brain accompanies a number of neurodegenerative disorders, including Alzheimer's disease (AD) associated with the presence of senile plaques formed by self-aggregated beta-amyloid peptide (A beta) fibrils. Any analytical technique for fast and reliable monitoring of A beta aggregation pathways is thus of evident biomedical interest. Here, electrochemical oxidation of A beta tyrosine residues, surface exposed in its native state and hidden in aggregates, allowed discrimination of different states of A beta adsorbed on high-surface area spectroscopic graphite and analysis of amyloid formation rates. The suggested system allows the development of fast and cost-effective analytical platforms for in vitro analysis of mechanisms of fibril formation and screening of AD treatments.