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Bacteriocins are biologically active compounds produced by a large number of bacteria, including lactic acid bacteria (LAB), which exhibit antimicrobial activity against various saprophytic and pathogenic microorganisms. In recent decades, bacteriocins are increasingly becoming more important in different branches of the industry due to their broad antibacterial and antifungal spectrum - in the food industry for natural food preservation and expiry date extension; in the health sector for preparation of probiotic foods and beverages; in the clinical practice as alternatives of conventional antibiotics; in the agriculture as biocontrol agents of plant pathogens and alternatives of chemical pesticides for plant protection. The broad antimicrobial spectrum of bacteriocins has stimulated the research attention on their application mainly in the food industry as natural preservatives. Most scientific achievements concerning the application food biopreservation are related to bacteriocins produced by LAB. The lactic acid bacteria bacteriocins can be produced in the food substrate during its natural fermentation or can be added in the food products after obtaining byin vitrofermentations under optimal physical and chemical conditions. Moreover, the immobilization of LAB bacteriocins on different matrices of organic and inorganic origin has been proposed as an advanced approach in the natural food preservation for their specific antimicrobial activity, anti-biofilm properties and potential use as tools for pathogen detection.

The frog skin-derived peptide Temporin 1Tb (TB) has gained increasing attention as novel antimicrobial agent for the treatment of antibiotic-resistant and/or biofilm-mediated infections. Nevertheless, such a peptide possesses a preferential spectrum of action against Gram-positive bacteria. In order to improve the therapeutic potential of TB, the present study evaluated the antibacterial and antibiofilm activities of two TB analogs against medically relevant bacterial species. Of the two analogs, TB_KKG6A has been previously described in the literature, while TB_L1FK is a new analog designed by us through statistical-based computational strategies. Both TB analogs displayed a faster and stronger bactericidal activity than the parental peptide, especially against Gram-negative bacteria in planktonic form. Differently from the parental peptide, TB_KKG6A and TB_L1FK were able to inhibit the formation of Staphylococcus aureus biofilms by more than 50% at 12 μM, while only TB_KKG6A prevented the formation of Pseudomonas aeruginosa biofilms at 24 μM. A marked antibiofilm activity against preformed biofilms of both bacterial species was observed for the two TB analogs when used in combination with EDTA. Analysis of synergism at the cellular level suggested that the antibiofilm activity exerted by the peptide-EDTA combinations against mature biofilms might be due mainly to a disaggregating effect on the extracellular matrix in the case of S. aureus, and to a direct activity on biofilm-embedded cells in the case of P. aeruginosa. Both analogs displayed a low hemolytic effect at the active concentrations and, overall, TB_L1FK resulted less cytotoxic toward mammalian cells. Collectively, the results obtained demonstrated that subtle changes in the primary sequence of TB may provide TB analogs that, used alone or in combination with adjuvant molecules such as EDTA, exhibit promising features against both planktonic and biofilm cells of medically relevant bacteria.