A novel hydrophobic peptide FGMp11: Insights into antimicrobial properties, hydrophobic sites on Staphylococcus aureus and its application in infecting pasteurized milk

Abstract

Hydrophobic peptides have received considerable attention in food preservation. The elucidation of the hydrophobic points of hydrophobic peptides is helpful in revealing the antimicrobial mechanism, and screening strategies for novel antimicrobials such as molecular docking and deep learning. A novel antimicrobial peptide (AMP) FGMp11 was identified and screened from fermented goat milk with strong hydrophobic properties, β-turn structure, and the amino acid sequence of TPVVVPPFLQP. The hydrophobic properties of FGMP11 could significantly damage the integrity of the cell membrane, resulting in changes in cell morphology. Hydrophobic interactions of FGMp11 with Mur enzymes (MurC, MurD, MurE, MurF, and MurG) are ideal targets for antimicrobial therapy, as these targets are involved in peptidoglycan synthesis via hydrogen bond interactions. The electrostatic binding sites of FGMp11 and the key amino acids GLN, LEU, PRO, and VAL were mainly -OH, -NH2, and -C=O groups, reducing cell activity. FGMp11 was able to significantly inhibit the growth of S. aureus during the storage of pasteurized milk. Overall, these findings provide a scientific basis for the antimicrobial activity of FGMp11 against food-borne pathogens and its application in food preservation.