The thermodynamic stability of amyloids fibrils can provide the missing link for understanding the mechanisms driving fibril polymorphism. In contrast to the kinetics of amyloid formation which has been extensively studied and characterized in detail for many pathologically relevant proteins such as Amyloid-β , Tau , or α-Synuclein (αSyn) , systematic analysis of amyloid stability has only recently started to gain more attention . The thermodynamic stability of amyloid fibrils may contribute to defining their persistence in vivo, which is influenced by many factors including posttranslational modifications , proteasomal degradation , or clearance by chaperones . The dysregulation and insufficient efficiency of these clearance mechanisms leads to pathological states.