Inhibition of Snake Venom Metalloproteinase by β-Lactoglobulin Peptide from Buffalo (Bubalus bubalis) Colostrum
(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.
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- author
- Arpitha, Ashok ; Sebastin Santhosh, M. ; Chougule, Rohit A LU ; Girish, K. S. ; Vinod, D. and Aparna, H. S.
- organization
- publishing date
- 2017-02-02
- 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
- pmid:28155167
- 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
- 2025-01-07 07:05:03
@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}},
keywords = {{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}},
doi = {{10.1007/s12010-017-2407-6}},
volume = {{182}},
year = {{2017}},
}