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Antibacterial and anti‐inflammatory activity of a temporin B peptide analogue on an in vitro model of cystic fibrosis
Author(s) -
Bezzerri Valentino,
Avitabile Concetta,
Dechecchi Maria Cristina,
Lampronti Ilaria,
Borgatti Monica,
Montagner Giulia,
Cabrini Giulio,
Gambari Roberto,
Romanelli Alessandra
Publication year - 2014
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2674
Subject(s) - antimicrobial , antimicrobial peptides , peptide , in vitro , pseudomonas aeruginosa , microbiology and biotechnology , circular dichroism , chemokine , chemistry , anti inflammatory , antibiotics , antibacterial activity , cystic fibrosis , tumor necrosis factor alpha , bacteria , biology , immunology , biochemistry , receptor , genetics
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‐1 β , 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.