Antimicrobial Activity of a Lipidated Temporin L Analogue against Carbapenemase-Producing <i>Klebsiella pneumoniae</i> 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. <i>Klebsiella pneumoniae...
Guardado en:
| Autores principales: | , , , , , , , |
|---|---|
| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
MDPI AG
2021
|
| Materias: | |
| Acceso en línea: | https://doaj.org/article/1ad3760843114b6ebd6ac427c755dd40 |
| Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
| Sumario: | 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. <i>Klebsiella pneumoniae</i> 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 <i>K. pneumoniae</i> clinical isolates. According to the antibiotic susceptibility assay, all the <i>K. pneumoniae</i> strains were resistant to at least one other class of antibiotics, in addition to beta-lactams. Peptides <b>1B</b> and <b>C</b> showed activity on all test strains, but the lipidated analogue <b>C</b> expressed the greater antimicrobial properties, with MIC values ranging from 6.25 to 25 µM. Furthermore, the peptide <b>C</b> 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. |
|---|