My research interests lie at the intersection of protein misfolding and neurodegenerative diseases, particularly focusing on the role of α-Synuclein (α-Syn) in Parkinson's disease pathology. My recent work has delved into the intricate structural arrangements of α-Syn amyloid fibrils, which are pivotal in driving neurodegeneration. By employing advanced spectroscopic techniques, we have elucidated the spatial distribution of surface polarity along these fibrils, shedding light on the nanoscale organization of polar and nonpolar domains within them. Our findings not only unveil the heterogeneous nature of α-Syn fibrils but also hint at the influence of structural polymorphism on their surface characteristics. Understanding the nuances of fibril architecture and surface polarity holds immense significance, as it could pave the way for targeted therapeutic interventions aimed at disrupting fibril formation or mitigating their toxic effects. Moving forward, I am keen on exploring how these insights can be translated into novel imaging modalities for studying other complex biological systems with similar structural intricacies, thereby advancing our understanding of various protein misfolding disorders beyond Parkinson's disease.