In vitro and in vivo insulin amyloid degradation mediated by Serratiopeptidase

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...

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Published inMaterials Science & Engineering C Vol. 70; no. Pt 1; pp. 728 - 735
Main Authors Metkar, Sanjay Kisan, Girigoswami, Agnishwar, Murugesan, Ramachandran, Girigoswami, Koyeli
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.01.2017
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Summary: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 vivo using 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. [Display omitted] •Amyloidosis is a disorder caused by insoluble protein aggregate (amyloids) deposition.•Insulin amyloids are used as a model protein for various amyloid associated diseases.•The insulin amyloid degradation potential of Serratiopeptidase (SP) was explored in vitro and in vivo.
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ISSN:0928-4931
1873-0191
DOI:10.1016/j.msec.2016.09.049