Antimicrobial Activity of a Lipidated Temporin L Analogue against Carbapenemase-Producing Clinical Isolates.

Over the years, the increasing acquisition of antibiotic resistance genes has led to the emergence of highly resistant bacterial strains and the loss of standard antibiotics' efficacy, including β-lactam/β-lactamase inhibitor combinations and the last line carbapenems. is considered one of the major exponents of a group of multidrug-resistant ESKAPE pathogens responsible for serious healthcare-associated infections. In this study, we proved the antimicrobial activity of two analogues of Temporin L against twenty carbapenemase-producing clinical isolates. According to the antibiotic susceptibility assay, all the strains were resistant to at least one other class of antibiotics, in addition to beta-lactams. Peptides and showed activity on all test strains, but the lipidated analogue expressed the greater antimicrobial properties, with MIC values ranging from 6.25 to 25 µM. Furthermore, the peptide showed bactericidal activity at MIC values. The results clearly highlight the great potential of antimicrobial peptides both as a new treatment option for difficult-to-treat infections and as a new strategy of drug-resistance control.