Antibacterial and anti-inflammatory activity of a temporin B peptide analogue on an in vitro model of cystic fibrosis
Version of Record online: 6 AUG 2014
Copyright © 2014 European Peptide Society and John Wiley & Sons, Ltd.
Journal of Peptide Science
Volume 20, Issue 10, pages 822–830, October 2014
How to Cite
2014), Antibacterial and anti-inflammatory activity of a temporin B peptide analogue on an in vitro model of cystic fibrosis, Journal of Peptide Science, 20, pages 822–830, doi: 10.1002/psc.2674, , , , , , , and (
- Issue online: 9 SEP 2014
- Version of Record online: 6 AUG 2014
- Manuscript Accepted: 16 JUN 2014
- Manuscript Revised: 3 JUN 2014
- Manuscript Received: 16 APR 2014
- Italian Cystic Fibrosis Research Foundation. Grant Number: 15/2004 and 17/2010 to R. G.; grant no. 14/2012
- Pseudomonas aeruginosa;
Natural peptides with antimicrobial properties are deeply investigated as tools to fight bacteria resistant to common antibiotics. Small peptides, as those belonging to the temporin family, are very attractive because their activity can easily be tuned after small modification to their primary sequence. Structure-activity studies previously reported by us allowed the identification of one peptide, analogue of temporin B, TB_KKG6A, showing, unlike temporin B, antimicrobial activity against both Gram-positive and Gram-negative bacteria. In this paper, we investigated the antimicrobial and anti-inflammatory activity of the peptide TB_KKG6A against Pseudomonas aeruginosa. Interestingly, we found that the peptide exhibits antimicrobial activity at low concentrations, being able to downregulate the pro-inflammatory chemokines and cytokines interleukin (IL)-8, IL-1β, IL-6 and tumor necrosis factor-α produced downstream infected human bronchial epithelial cells. Experiments were carried out also with temporin B, which was found to show pro-inflammatory activity. Details on the interaction between TB_KKG6A and the P. aeruginosa LPS were obtained by circular dichroism and fluorescence studies. Copyright © 2014 European Peptide Society and John Wiley & Sons, Ltd.