AFM-STED correlative nanoscopy applied to the study of in-vitro misfolded protein aggregation

Abstract

The aggregation process of amyloidogenic peptides can be characterized by advanced correlative techniques to understand the molecular mechanisms of misfolded protein diseases. We performed correlative AFM-STED measurements to study amyloid aggregates formation starting from monomeric peptides. A previous study, performed by our group on insulin and β-amyloid peptides (MW∼ 4kDa) suggested that the presence of fluorophores not only decreased the kinetics of the aggregation, a very well-known effect, but also favored the coexistence of labeled and unlabeled fibrils.