pH-dependent disruption of Escherichia coli ATCC 25922 and model membranes by the human antimicrobial peptides hepcidin 20 and 25 (pages 2842–2854)
Giuseppantonio Maisetta, Alberto Vitali, Mariano A. Scorciapino, Andrea C. Rinaldi, Raffaele Petruzzelli, Franca L. Brancatisano, Semih Esin, Annarita Stringaro, Marisa Colone, Carla Luzi, Argante Bozzi, Mario Campa and Giovanna Batoni
Version of Record online: 9 MAY 2013 | DOI: 10.1111/febs.12288
The human hepcidin 25 (hep-25) and its isoform hepcidin 20 (hep-20) are histidine-containing, cystein rich, β-sheet structured peptides endowed with antimicrobial activity which is highly enhanced at acidic pH. The data obtained by using different approaches strongly suggested that the mode of hep-25 and hep-20 action and their ability to perturb Escherichia coli and model membranes is markedly pH-dependent.