A transition of amyloidogenic protein by alternative folding pathway under certain conditions leads to the formation of protease resistant amyloid fibrils, having a predominantly cross (3 structure. These amyloids are related to various neurodegenerative diseases and the clearance of such amyloid can be the targets to treat amyloid-related diseases. Insulin is a protein that can form amyloids and is widely used as a model amyloidogenic protein for the study of various amyloid related diseases. In this study, insulin amyloids were formed in vitro and the potential of Serratiopeptidase (SP), a fibrinolytic-like serine protease, towards the dissociation of insulin amyloids was explored. The dissociation of the amyloids was demonstrated in vitro and in vivo using zebrafish model. The amyloid dissociation property was compared with a standard amyloid dissociating enzyme nattokinase (NK) showing the better dissociation ability of SP. Therefore, SP can be treated as a potential amyloid dissociating agent as well-as possible drug candidate for different amyloid related disorders.
