SCREENING AND IN SILICO VALIDATION OF ANTIMICROBIAL PEPTIDE DERIVED FROM ELASTASE AND MYELOPEROXIDASE

Abstract

Background: Antimicrobial peptides are a group of small molecules intended to serve the purpose as antimicrobial agents. The emergence and resurgence of drug resistant pathogens underscores the need for identifying novel antimicrobial agents. Elastase and myeloperoxidase are enzymes with documented antimicrobial activity. Hence, peptide derivatives of these proteins could be used as antimicrobial agents. 

Aim: The study aims to identify and determine the antimicrobial activity of peptides derived from elastase and myeloperoxidase employing in silico tools. 

Methods: Several in silico tools were used to identify the antimicrobial peptides found in the selected proteins. AMPA was used for the identification of peptide units from the antimicrobial proteins. The dPABB and Anti Fp tools were used to deduce the antibacterial and antifungal property of the peptides. Further, toxicity and cell penetrating ability of the peptides were predicted.

Results: Peptides derived from elastase were shown to exhibit antibiofilm property, whereas a peptide derived from myeloperoxidase was found to be anti-fungal in nature. All peptides were found to be non-cell penetrating and non-toxic.

Discussion: The peptide derivatives of elastase and myeloperoxidase were found to exhibit antimicrobial properties. Further experimental validation is necessary to elucidate the molecular mechanisms associated with the mode of action of these peptide molecules.

Conclusion: Identification of peptide molecules from antimicrobial protein would open novel avenues towards the development of peptide therapy.