Abstract
Signal peptides (SPs) are essential tools for sorting or translocating synthesized proteins. However, except for a few examples, their studies in isolation are quite limited. Here, we asked a question about the aggregation propensity of signal peptides (residues 1-18) of Human Serum Albumin (HSA). Molecular dynamic simulations were used to observe the mechanism through which signal peptides of HSA self-aggregated under physiological conditions. Further, we confirmed our results by combining dye-based assays, atomic force microscopy, and transmission electron microscopy techniques. It was noted that the signal peptide of HSA (regions 1-18) forms typical amyloid-like fibrils.