Exploring protein behavior through electrochemistry and SPR. Human cofilin-1 as model

This presentation will explore the latest findings on the direct electrochemical study of oxidative-induced aggregation of CFL-1. Such study was performed for the protein adsorbed on screen-printed carbon electrodes following the oxidation reaction of the tyrosine amino acid. The proposed label-free electrochemical approach effectively identified the aggregation process of CFL-1 at its earliest stages. Considering that the aggregation process of CFL-1 is indeed connected to the aSyn oligomerization mechanism, the obtained results may contribute to the development of cost-effective and user-friendly strategies for the early detection of aggregates, potentially impacting the diagnosis and treatment of amyloidogenic diseases. Furthermore, this unique platform may also be employed for the screening of novel compounds able to disrupt the amyloidogenic process associated with CFL-1. Previous to the electrochemical discussions, surface plasmon resonance results will be presented to prove the oxidation state of CFL-1 on surface, via the heterogenization of Ellman’s assay.