In this work, we have started to elucidate the aggregation behavior of proteinase-treated α-synuclein amyloid fibrils. Using bulk solution measurements we demonstrate several challenges with biochemical analysis of proteinase treated fibrils by traditional methods. Shaven fibrils demonstrate low colloidal stability resulting in extensive flocculation. Furthermore, shaving of the fibrils strongly alters their ThT sensitivity. QCM-D has been demonstrated to be a well-adapted label-free methodology for the study of amyloid fibril growth and has been employed for this purpose for over fifteen years . Here we demonstrate that the QCM-D can discriminate between monomer binding to the fibril surface and fibril elongation, enabling not only measurements of fibril elongation rates in complex media, but provides detailed insights into the molecular nature of deposited material. Utilizing this experimental platform we demonstrate that shaven fibrils are fully capable of recruiting intact monomer.