Advanced

Inhibition of Snake Venom Metalloproteinase by β-Lactoglobulin Peptide from Buffalo (Bubalus bubalis) Colostrum

Arpitha, Ashok; Sebastin Santhosh, M.; Chougule, Rohit A LU ; Girish, K. S.; Vinod, D. and Aparna, H. S. (2017) In Applied Biochemistry and Biotechnology 182(4). p.1415-1432
Abstract

Bioactive peptide research has experienced considerable therapeutic interest owing to varied physiological functions, efficacy in excretion, and tolerability of peptides. Colostrum is a rich natural source of bioactive peptides with many properties elucidated such as anti-thrombotic, anti-hypertensive, opioid, immunomodulatory, etc. In this study, a variant peptide derived from β-lactoglobulin from buffalo colostrum was evaluated for the anti-ophidian property by targeting snake venom metalloproteinases. These are responsible for rapid local tissue damages that develop after snakebite such as edema, hemorrhage, myonecrosis, and extracellular matrix degradation. The peptide identified by LC-MS/MS effectively neutralized hemorrhagic... (More)

Bioactive peptide research has experienced considerable therapeutic interest owing to varied physiological functions, efficacy in excretion, and tolerability of peptides. Colostrum is a rich natural source of bioactive peptides with many properties elucidated such as anti-thrombotic, anti-hypertensive, opioid, immunomodulatory, etc. In this study, a variant peptide derived from β-lactoglobulin from buffalo colostrum was evaluated for the anti-ophidian property by targeting snake venom metalloproteinases. These are responsible for rapid local tissue damages that develop after snakebite such as edema, hemorrhage, myonecrosis, and extracellular matrix degradation. The peptide identified by LC-MS/MS effectively neutralized hemorrhagic activity of the Echis carinatus venom in a dose-dependent manner. Histological examinations revealed that the peptide mitigated basement membrane degradation and accumulation of inflammatory leucocytes at the venom-injected site. Inhibition of proteolytic activity was evidenced in both casein and gelatin zymograms. Also, inhibition of fibrinolytic and fibrinogenolytic activities was seen. The UV-visible spectral study implicated Zn2+ chelation, which was further confirmed by molecular docking and dynamic studies by assessing molecular interactions, thus implicating the probable mechanism for inhibition of venom-induced proteolytic and hemorrhagic activities. The present investigation establishes newer vista for the BLG-col peptide with anti-ophidian efficacy as a promising candidate for therapeutic interventions.

(Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Colostrum, Molecular dynamics, Peptide, Snake venom metalloproteinases, β-Lactoglobulin
in
Applied Biochemistry and Biotechnology
volume
182
issue
4
pages
1415 - 1432
publisher
Humana Press
external identifiers
  • scopus:85011604821
  • wos:000406655400011
ISSN
0273-2289
DOI
10.1007/s12010-017-2407-6
language
English
LU publication?
yes
id
f9e4f06e-8a35-4e17-8596-668d85308e6e
date added to LUP
2017-02-15 12:30:02
date last changed
2018-01-07 11:50:01
@article{f9e4f06e-8a35-4e17-8596-668d85308e6e,
  abstract     = {<p>Bioactive peptide research has experienced considerable therapeutic interest owing to varied physiological functions, efficacy in excretion, and tolerability of peptides. Colostrum is a rich natural source of bioactive peptides with many properties elucidated such as anti-thrombotic, anti-hypertensive, opioid, immunomodulatory, etc. In this study, a variant peptide derived from β-lactoglobulin from buffalo colostrum was evaluated for the anti-ophidian property by targeting snake venom metalloproteinases. These are responsible for rapid local tissue damages that develop after snakebite such as edema, hemorrhage, myonecrosis, and extracellular matrix degradation. The peptide identified by LC-MS/MS effectively neutralized hemorrhagic activity of the Echis carinatus venom in a dose-dependent manner. Histological examinations revealed that the peptide mitigated basement membrane degradation and accumulation of inflammatory leucocytes at the venom-injected site. Inhibition of proteolytic activity was evidenced in both casein and gelatin zymograms. Also, inhibition of fibrinolytic and fibrinogenolytic activities was seen. The UV-visible spectral study implicated Zn<sup>2+</sup> chelation, which was further confirmed by molecular docking and dynamic studies by assessing molecular interactions, thus implicating the probable mechanism for inhibition of venom-induced proteolytic and hemorrhagic activities. The present investigation establishes newer vista for the BLG-col peptide with anti-ophidian efficacy as a promising candidate for therapeutic interventions.</p>},
  author       = {Arpitha, Ashok and Sebastin Santhosh, M. and Chougule, Rohit A and Girish, K. S. and Vinod, D. and Aparna, H. S.},
  issn         = {0273-2289},
  keyword      = {Colostrum,Molecular dynamics,Peptide,Snake venom metalloproteinases,β-Lactoglobulin},
  language     = {eng},
  month        = {02},
  number       = {4},
  pages        = {1415--1432},
  publisher    = {Humana Press},
  series       = {Applied Biochemistry and Biotechnology},
  title        = {Inhibition of Snake Venom Metalloproteinase by β-Lactoglobulin Peptide from Buffalo (Bubalus bubalis) Colostrum},
  url          = {http://dx.doi.org/10.1007/s12010-017-2407-6},
  volume       = {182},
  year         = {2017},
}