As an intrinsically disordered protein, α-synuclein is prone to aggregation into amyloid fibrils a hallmark of Parkinson’s disease. A network of proteins known as the molecular chaperones are able to prevent protein aggregation into fibrils. In particular, the small heat-shock proteins (sHsps) αB-crystallin and Hsp27 are able to inhibit α-synuclein fibril elongation and stably bind to mature α-synuclein fibrils. It has been hypothesised that one mechanism by which sHsps inhibit fibril elongation involves the preferential binding of sHsps to the ends of fibrils, preventing monomer association at these points. In addition, the Hsp70 system of molecular chaperones are capable of disaggregating α-synuclein fibrils; disassembling the fibrils into fragments or monomers. Hsp70 and its co-chaperone Hsp40 recognise and bind to α-synuclein fibrils at high density during this disaggregation. This disaggregation process is also hypothesised to begin at fibril ends. To develop a framework to investigate sHsp binding to fibril ends, computational analysis was conducted to investigate if sHsp isoforms (αB-crystallin, wild-type Hsp27 and a phosphomimetic mutant of Hsp27) preferentially bind to mature α-synuclein fibril ends from TIRF microscopy images. We will report on any preferential binding to fibril ends by αB-crystallin, Hsp27, Hsp273D (a phosphomimetic mutant of Hsp27 that exists primarily as dimers). Furthermore, mature α-synuclein fibrils were pre-incubated with αB-crystallin or Hsp27 prior to the addition of the Hsp70 molecular chaperone system. We found that the addition of sHsps stabilised mature α-synuclein fibrils in preparation for their disaggregation by the Hsp70 system, increasing the amount of disaggregation occurring.