Fibrillization of amyloid β peptides is implicated in Alzheimer’s disease, and emerging evidence suggests that metal ions play a significant role in this process. Specifically, the interaction between redox-active metal ions and amyloid β peptides can lead to the generation of reactive oxygen species (ROS), which may trigger toxicity associated with neurodegenerative diseases.
To understand the mechanism by which metal ions contribute to amyloid fibrilization, we employed advanced Electron Paramagnetic Resonance (EPR) spectroscopy. Our focus was on elucidating the structures of intermediates formed during the reactions of metal-amyloid peptide complexes. EPR spectroscopy is particularly valuable for characterizing geometrical structures, and coordination sphere of metal ions in these complexes.
In my presentation, I will discuss recent findings from our laboratory that investigate the interaction between copper and amyloid peptides in the presence of oxygen using various EPR spectroscopic techniques. These results promise to provide critical insights into the role of metal ions in amyloid fibril formation and the associated neurotoxicity.