PUBLICATION

In vitro and in vivo insulin amyloid degradation mediated by Serratiopeptidase

Authors
Metkar, S.K., Girigoswami, A., Murugesan, R., Girigoswami, K.
ID
ZDB-PUB-161025-13
Date
2017
Source
Materials science & engineering. C, Materials for biological applications   70: 728-735 (Journal)
Registered Authors
Keywords
Amyloidosis, In vivo live animal imaging, Insulin amyloid dissociation, Serine proteases, Serratiopeptidase
MeSH Terms
  • Amyloid/metabolism*
  • Animals
  • Circular Dichroism
  • Dynamic Light Scattering
  • Fibrinolysis
  • Humans
  • Insulin/metabolism*
  • Microscopy, Atomic Force
  • Particle Size
  • Peptide Hydrolases/metabolism*
  • Zebrafish
PubMed
27770948 Full text @ Mater Sci Eng C Mater Biol Appl
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.
Genes / Markers
Figures
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping