Antibacterial activity of new peptides from barbel protein hydrolysates and mode of action via a membrane damage mechanism against Listeria monocytogenes

•Antibacterial activity of new peptides from barbel protein was studied.•The most active peptide was: Ala-Ala-Gly-Gly-Val.•The minimum inhibitory concentrations toward six strains were determined.•The hemolytic activity toward bovine erythrocytes was determined.•The mode of action against Listeria monocytogenes was determined. There is great interest in the development of antimicrobial peptides as a potentially novel class of antimicrobial agents. In this study we evaluated the mode of action of new peptides (Gly-Val-His, Trp-His-Arg, Trp-His-Phe, Pro-Pro-Ser-Ser, Ala-Ala-Ala-Leu, Ala-Ala-Gly-Gly-Val, Ala-Ala-Val-Lys-Met, Ala-Ser-Ser-Ser), previously characterized, from barbel protein hydrolysates against Listeria monocytogenes via a membrane damage mechanism. The minimum inhibitory concentrations (MIC) of these peptides toward six strains and their hemolytic activity toward bovine erythrocytes were determined. Prediction of peptide secondary structure indicated that these peptides should have random coil structures and high content of hydrophobic amino acids. In addition, results of the determination of extracellular potassium, which is considered a good marker of membrane permeability, revealed that treatment with pure barbel peptides could cause morphological changes of L. monocytogenes and destruction of the cell integrity via irreversible membrane damage. The results could provide information for investigating the antibacterial model of antibacterial peptides derived from fish protein hydrolysates.