A novel ESKAPE-sensitive peptide with enhanced stability and its application in controlling multiple bacterial contaminations in chilled fresh pork

Abstract

The co-existence of various pathogenic bacteria on the surface of pork products exacerbates difficulties in food safety control. Developing broad-spectrum and stable antibacterial agents that are not antibiotics is an unmet need. To address this issue, all l-arginine residues of a reported peptide (IIRR)₄-NH₂ (zp80) were substituted with the corresponding D enantiomers. This novel peptide (IIrr)₄-NH₂ (zp80r) was expected to maintain favourable bioactivity against ESKAPE strains and have enhanced proteolytic stability compared with zp80. In a series of experiments, zp80r maintained favourable bioactivities against starvation-induced persisters. Electron microscopy and fluorescent dye assays were used to verify the antibacterial mechanism of zp80r. Importantly, zp80r reduced bacterial colonies in chilled fresh pork contaminated with multiple bacterial species. This newly designed peptide is a potential antibacterial candidate to combat problematic foodborne pathogens during storage of pork.

Keywords: Broad-spectrum antibacterial; Foodborne pathogen; Helical peptide; Membrane targeting; Proteolytic stability.