In the first year of my PhD, We investigated the interplay between protein aggregates characteristic and membrane composition and organization as a key factor in the cytotoxicity of amyloid aggregates. we used a protocol developed for preparing defect-free Supported Lipid Bilayers (SLBs) with the coexistence of both fluid and gel lipid phases. In particular, we employed two different lipid mixtures, mimicking the composition of both the external and internal leaflet of the neuronal cell membranes . Among all the possible protein misfolding diseases, we focused on Parkinson's disease (PD). We found that the interaction with alpha-synuclein, the principal peptide involved in PD, induced significant damages in SLBs with different extents in the two investigated lipid mixtures. Currently, We are going to perform correlative AFM-STED recordings to study the molecular mechanism of misfolded protein diseases and the formation of amyloid aggregates. In particular, we want to investigate the in vitro aggregation of alpha-synnuclein amyloid peptides.