Title
In vitro and in vivo insulin amyloid degradation mediated by Serratiopeptidase
Author
Sanjay Kisan Metkar, Agnishwar Girigoswami, Ramachandran Murugesan, Koyeli Girigoswami
Year
2017
Journal
Materials Science and Engineering: C
Abstract
A transition of amyloidogenic protein by alternative folding pathway under certain conditions leads to the formation of protease resistant amyloid fibrils, having predominantly cross β structure. These amyloids are related to various neurodegenerative diseases and clearance of such amyloids may be a therapeutic approach for amyloid-related diseases. Insulin, that can form amyloids, 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 using in vitro and in vivousing zebrafish model. The amyloid dissociation property was compared with a standard amyloid dissociating enzyme nattokinase (NK). SP shows better amyloid dissociation ability than NK and therefore, SP can be considered as amyloid dissociating agent with potential as a drug candidate for different amyloid related disorders.
Instrument
J-715
Keywords
Circular dichroism, Secondary structure, Aggregation, Biochemistry