It is intriguing to speculate that changes in cohesive properties of α-synuclein fibrils upon proteolytic truncation of the fuzzy coat, such as colloidal stability and formation of strongly adhering secondary daughter fibrils, may play an important role in disease and formation of LBs. Flocculation and higher order assembly of fibrils and further growth by elongation and secondary pathways could indeed form structures similar to LBs, with a dense core and radiating filaments . However, our study does not investigate if LB-like structures form from these conditions. It may be the case that the fuzzy-coat generally could inhibit and slow down the aggregation of proteins and formation of toxic inclusion bodies, and hence be an evolved protective feature. QCM-D proves to be a particularly useful platform for studying the properties of modified fibrils as the flow-cell platform allows for easy removal of modifying enzymes post treatment. The instrument does not rely on reporter-molecules such as fluorescent dyes, avoiding complications of alterations in ThT sensitivity upon modification as observed in this study and can provide insights into the nature of the interactions. It is clear that the QCM-D proves an interesting platform for studying relative binding affinities to other species commonly found in LBs, such as lipids and other proteins. Systematic study of PTMs and fibril binding affinities may allow for a bottom-up approach to the study of LB formation, not easily available by other in vitro platforms.