Characterization of novel antimicrobial peptides designed on the basis of amino acid sequence of peptides from egg white hydrolysate

Salmonella enterica subsp. enterica serotype Typhimurium ( S . typhimurium ) is one of the most prevalent foodborne pathogens responsible for food poisoning and is spread through the consumption of contaminated poultry products. In this study, four antimicrobial peptides (AMPs) with varying hydrophobicity and helical structure-forming tendencies were designed and synthesized based on the amino acid sequences of peptides from egg white hydrolysate. Two of these AMPs, P1R3 (KSWKKHVVSGFFLR) and P1C (KSWKKHVVSGFFLRLWVHKK), exhibited inhibitory activity against S . typhimurium and compromised its biofilm-forming ability. Investigation of their modes of action revealed that P1R3 and P1C interact with and permeabilize the cytoplasmic membrane of bacteria, leading to membrane potential dissipation, damage to membrane integrity, and consequent bacterial death. P1R3 also bound to S . typhimurium DNA, resulting in DNA aggregation or precipitation. Moreover, both peptides showed negligible cytotoxicity to Vero cells, and P1C displayed significant antimicrobial activity in chicken meat. Peptides P1R3 and P1C, therefore, have the potential to be developed as promising food preservatives, especially against pathogenic S . typhimurium . • P1R3 and P1C with higher helicity and hydrophobicity exhibited improved antimicrobial activities. • P1R3 and P1C damaged membrane functions. • P1R3 and P1C exhibited low cytotoxicity to mammalian cells. • P1C reduced viability of S . typhimurium in chicken meat at 4 °C.