Recombinant Production and Molecular Docking Studies of Casoplatelin, a Bioactive Peptide
Ragothaman M. Yennamalli1, 2, Pulkit Anupam Srivastava3, Sheena D. Sarswati3, Vijay Kumar Garlapati3, *
Identifiers and Pagination:Year: 2020
First Page: 84
Last Page: 92
Publisher ID: TOBIOTJ-14-84
Article History:Received Date: 07/01/2020
Revision 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.
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.
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.
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.
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.
The present study showcases the recombinant approach for biopeptide production and its interaction with fibrinogen through in silico approach.