Recombinant Production and Molecular Docking Studies of Casoplatelin, a Bioactive Peptide

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.