Abstract
AIMS: The emergence of antibiotic resistance is one of the most significant issues today. Modifying antimicrobial peptides (AMPs) can improve their effects. In this study, the active region of Listeriolysin S (LLS) as a peptidic toxin has been recognized, and its antibacterial properties have been evaluated by modifying that region. METHODS: After extracting the sequence, the structure of LLS was predicted by PEP-FOLD3. AntiBP and AMPA servers identified its antimicrobial active site. It was modified by adding arginine residue to its 3- and N-terminal regions. Its antimicrobial properties on Staphylococcus aureus, Escherichia coli, and Lactobacillus Plantarum were estimated. FINDINGS: The results of AntiBP and AntiBP servers demonstrated that a region of 15 amino acids has the most antimicrobial properties (score = 1.696). After adding arginine to the chosen region, the physicochemical evaluation and antimicrobial properties revealed that the designed peptide is a stable AMP with a positive charge of 4, which is not toxic to human erythrocyte cells and has antigenic properties. The results of in vitro and colony counting indicated that at different hours, it caused a significant reduction in the count of S aureus, E coli, and L Plantarum compared with the control sample. CONCLUSIONS: Upcoming research implies that identifying and enhancing the active sites of natural peptides can help combat bacteria.