Amyloidogenic protein aggregation into fibrils is linked to several neurodegenerative disorders, such as Alzheimer's or Parkinson's disease. An amyloid specific fluorescent dye thioflavin-T (ThT) is often used to track the formation of these fibrils in vitro. Despite its wide application, it is still unknown how many types of ThT binding modes to amyloids exist, with multiple studies indicating varying numbers. In this work, we examine the binding of ThT to insulin fibrils generated at pH 2.4 and reveal a possible inner core binding mode which is not accessible to the dye molecule after aggregation occurs.