Format

Send to

Choose Destination
Mater Sci Eng C Mater Biol Appl. 2017 Jan 1;70(Pt 1):728-735. doi: 10.1016/j.msec.2016.09.049. Epub 2016 Sep 24.

In vitro and in vivo insulin amyloid degradation mediated by Serratiopeptidase.

Author information

1
Medical Bionanotechnology Laboratory, Faculty of Allied Health Sciences, Chettinad Academy of Research and Education (CARE), Chettinad Health City, Kelambakkam, Chennai 603103, India.
2
Medical Bionanotechnology Laboratory, Faculty of Allied Health Sciences, Chettinad Academy of Research and Education (CARE), Chettinad Health City, Kelambakkam, Chennai 603103, India. Electronic address: koyelig@gmail.com.

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 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.

KEYWORDS:

Amyloidosis; In vivo live animal imaging; Insulin amyloid dissociation; Serine proteases; Serratiopeptidase

PMID:
27770948
DOI:
10.1016/j.msec.2016.09.049
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center