Journal
JOURNAL OF FUNCTIONAL FOODS
Volume 11, Issue -, Pages 322-329Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jff.2014.10.006
Keywords
Peptides; Antibacterial activity; Mode of action; Membrane permeability; Listeria monocytogenes
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Funding
- Ministry of Higher Education, Scientific Research and Information and Communication Technologies, Tunisia
- CMCU [12G0915]
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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. (C) 2014 Elsevier Ltd. All rights reserved.
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