α-synuclein is a protein normally involved in synaptic vesicle transport and exocytosis for neurotransmission . Aggregation of α-synuclein is a primary feature of the synucleinopathies, such as Parkinson's Disease (PD), multiple system atrophy (MSA) and Lewy Body dementia (LBD) . Neuropathological examination of PD and LBD brains reveals the formation of intra-cellular inclusions called Lewy Bodies (LBs) . LBs are spherical structures consisting of aggregated α-synuclein in an amyloid conformation , lipids, organelles and other proteins, such as cytoskeletal proteins . While the pathological importance of LBs has been well known for decades, the mechanism behind their formation remains incompletely understood . α-synuclein molecules within LBs are mostly post-translationally modified, with ubiquitination, phosphorylation and truncations being particularly prominent . C-terminal truncations of α-synuclein species are expected to occur post fibril formation, demonstrated in neuronal models capable of recreating LB-like inclusions . The strongly negatively charged C-terminal region of α-synuclein is located outside the fibril core of the amyloid conformation and constitutes part of the so-called "fuzzy coat" . Within recent years an increasing number of amyloid core structures have been determined at an atomic level by cryo-EM techniques . However, the fuzzy coat is effectively invisible or only available in low resolution to modern imaging techniques due to its highly dynamic and disordered nature . This means that, in many cases, a large part of the total amino acid sequence, and more than half of the total sequence in the case of α-synuclein fibrils remains structurally uncharacterized. The fuzzy coat remains important for the biophysical properties of amyloid, having significant effects on kinetic parameters and can even govern the mechanical and adhesive properties of amyloid fibrils . The oligomeric assemblies of α-synuclein, which are suspected to be the drivers of amyloid neurotoxicity, are indeed also formed by fibril-surface catalyzed pathways . Furthermore the disordered flank regions may control the access of chaperones to the fibril core, such as Hsp70 which is able to depolymerize α-synuclein amyloid fibrils under ATP consumption . Increased knowledge of the roles of the fuzzy coat and its implications for amyloid kinetics and cellular interactions would therefore provide an important step towards understanding the role of amyloid in disease as well as identifying new targets for drug development. It is therefore important to establish experimental approaches which allow for systematic investigation of the biophysical properties of the fuzzy coat. Indeed Ulamec and coworkers recently called for the development of assays of protease treated fibrils, with the fuzzy coat "shaven off", to study which parts of the fibril are driving binding and intracellular interactions .