In order to design treatments that are effective in modifying the disease, it is imperative to ascertain what the mechanism is behind the formation of aSyn pathology in PD (or the respective proteinopathy in the respective disease), and whether it is driven by fibril accumulation, protein-membrane interactions or both. As there is currently no animal model which can faithfully recreate human neurodegenerative pathology, mechanistic information must come from post-mortem human brain.
Our projects utilise our newly developed room-temperature CLEM pipeline to investigate the ultrastructure of the diverse spectrum of aSyn, Tau, Amyloid Beta and TDP-43 pathology seen in the post-mortem human brain of brain donors. By characterising the molecular components and corresponding 3D ultrastructures for the different pathological phenotypes of protein accumulation we hope to gain a deeper understanding of the driving forces behind disease progression.