4.7 Article

Esculentin(1-21), an amphibian skin membrane-active peptide with potent activity on both planktonic and biofilm cells of the bacterial pathogen Pseudomonas aeruginosa

Journal

CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 70, Issue 15, Pages 2773-2786

Publisher

SPRINGER BASEL AG
DOI: 10.1007/s00018-013-1291-7

Keywords

Antimicrobial peptide; Anti-biofilm activity; Cystic fibrosis; Membrane-permeation; Anti-Pseudomonas activity; Scanning electron microscopy

Funding

  1. Sapienza Universita di Roma
  2. Italian Foundation for Cystic Fibrosis (Project FFC) [14/2011]

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Pseudomonas aeruginosa is an opportunistic bacterial pathogen that forms sessile communities, named biofilms. The non-motile forms are very difficult to eradicate and are often associated with the establishment of persistent infections, especially in patients with cystic fibrosis. The resistance of P. aeruginosa to conventional antibiotics has become a growing health concern worldwide and has prompted the search for new anti-infective agents with new modes of action. Naturally occurring antimicrobial peptides (AMPs) represent promising future template candidates. Here we report on the potent activity and membrane-perturbing effects of the amphibian AMP esculentin(1-21), on both the free-living and sessile forms of P. aeruginosa, as a possible mechanism for biofilm disruption. Furthermore, the findings that esculentin(1-21) is able to prolong survival of animals in models of sepsis and pulmonary infection indicate that this peptide can be a promising template for the generation of new antibiotic formulations to advance care of infections caused by P. aeruginosa.

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