Antibacterial effect of lactoperoxidase protein and its peptides on some bacteria causing mastitis in dairy cattle by molecular docking method.

Unfortunately, using the antibiotics to treat mastitis is increasing in which leads to undesirable side effects. One of the antibiotics alternatives with high potential are antimicrobial proteins like lactoperoxidase. The aim of this study was to predict the peptides of lactoperoxidase protein and compare them in six different species (human, camel, sheep, goat, buffalo and cattle) and also investigate its antibacterial properties against Staphylococcus aureus and Escherichia coli strains through Molecular docking. The study of physicochemical properties of the lactoperoxidase protein and the derived bioactive peptides has been done using the CLC Main Workbench 5 software. The Swiss-model server was applied to predict the third (three-dimensional) structure of lactoperoxidase protein for camel and human. The peptides of lactoperoxidase protein were predicted and ultimately, the interactions of this protein and its derived peptides with the outer membrane proteins of the mentioned names were survived using ClusPro2.0 online software. The results of the position and energy of bonding assessment using molecular docking show that the most suitable binding location, in which the derived lactoperoxidase protein is bound to the outer membrane proteins of bactria membrane, with the lowest energy, related to cattle and goat, respectively. Bioinformatics study of the seven derived peptides from this protein showed that the third peptide of cattle, goat, buffalo, and sheep has a better performance in binding and degrading the outer membrane protein of these bacteria. These peptides can be proposed as replacement antibiotics for the treatment of mastitis in the future.