Here, we demonstrate an approach which allows for the systematic investigation of biophysical properties of amyloid fibrils subjected to protease treatment. We show that classical bulk measurement approaches of protease treated amyloid fibrils are exceedingly challenging due to flocculation and loss of ThT sensitivity of α-synuclein fibrils, but surface-based biosensing approaches, such as Quartz Cystal Microbalance with Dissipation (QCM-D) provides a suitable experimental platform for such investigations. We compare the growth rate of α-synuclein amyloid fibrils with and without the fuzzy coat "shaven off", and we propose a consistent molecular model that explains the sustained increase in aggregation rate observed after the proteolytic treatment through enhanced secondary processes.