Understanding the lag phase variability of insulin fibrillation

Conversion of misfolded protein into amyloid-like fibrillar aggregates is thought to proceed in 2 phases: slow formation of energetically unfavorable nuclei followed by subsequent rapid elongation of these nuclei. In this study, we focus on the first phase, commonly called the lag phase. In particular, we aim to determine whether the variability of the lag phase length observed for apparently identical samples could result from the inherent stochastic nature of the nucleation process as suggested by other works. To do this, we use bovine insulin as our model protein and adopt an approach that combines experiments and numerical simulations.