RESEARCH ARTICLE
Recombinant Production and Molecular Docking Studies of Casoplatelin, a Bioactive Peptide
Ragothaman M. Yennamalli1, 2, Pulkit Anupam Srivastava3, Sheena D. Sarswati3, Vijay Kumar Garlapati3, *
Article Information
Identifiers and Pagination:
Year: 2020Volume: 14
First Page: 84
Last Page: 92
Publisher ID: TOBIOTJ-14-84
DOI: 10.2174/1874070702014010084
Article History:
Received Date: 07/01/2020Revision Received Date: 23/04/2020
Acceptance Date: 15/05/2020
Electronic publication date: 19/08/2020
Collection year: 2020

open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: (https://creativecommons.org/licenses/by/4.0/legalcode). This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Abstract
Background:
Bioactive peptides from κ-casein have immense therapeutic potential as prophylactic formulations. Among these, casoplatelin is a κ-casein derived bioactive peptide with anti-thrombotic activities.
Aim:
Herein, we report the production of casoplatelin in an E. coli expression system (using a pBAD vector) and show in silico modeling of its interactions.
Methods:
A synthetic DNA construct encoding casoplatelin was designed with pepsin cleavage sites before and after the synthetic construct to allow the release of the peptide from the pro-peptide.
Results:
A novel recombinant approach was demonstrated for the production of casoplatelin, and anti-platelet aggregation activities of the product were confirmed. Also, casoplatelin structures were characterized in silico and then implemented to determine potential structural interactions with fibrinogen.
Conclusion:
The present study showcases the recombinant approach for biopeptide production and its interaction with fibrinogen through in silico approach.