Screening and in Silico Validation of Anti-Microbial Peptides Derived from Lysostaphin, Entero and Endolysin

Abstract

Introduction: Antimicrobial peptides (AMPs) are small molecules which are known to exert destructive effects upon pathogenic microorganisms. AMPs are designed from proteins obtained from various sources and tested under in vitro conditions to deduce their antimicrobial activity. Materials and Methods: A few of the peptidoglycan hydrolases such as lysostaphin (AAB53783.1), enterolysin (AGG79281.1), and endolysin (YP_009901016.1) were selected for the study based on an extensive text mining process. The protein sequences of the proteins were retrieved from the NCBI (National Centre for Biotechnology Information) database in the FASTA format (https://www.ncbi.nlm.nih.gov/protein/). Results and Discussion :In the antimicrobial protein lysostaphin, three antimicrobial peptide are been found, in which two is active and other is inactive, and one has antifungal property with a score of -0.15, and one having cell penetrating property, in which all are non toxic. Conclusion: The present study predicts AMPs from lysostaphin, entero and endolysins. These peptides were found to possess antifungal, anti-biofilm properties. Most of the peptides predicted were found to be non-cell penetrating and non-toxic.