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.
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