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Amphibian skin secretions represent a rich source of antimicrobial peptides (AMPs). In particular, temporins constitute a large family and are among the smallest amphipathic -helical AMPs (10-16 residues) found in nature to date, and with the lowest number of positively charged amino acids (1). Some of them possess unique properties including: (i) a fast membranolytic effect against a large spectrum of microorganisms; (ii) a synergism, when combined one with each other, in inhibiting bacterial growth and in endotoxin neutralization (2). Another interesting small-sized and membrane-active AMP is esculentin(1-18) corresponding to the N-terminal 1-18 fragment of esculentin-1b, isolated from frog skin. It displays a rapid bactericidal activity against important nosocomial pathogens, such as the gram-negative Pseudomonas aeruginosa. Its in vivo antimicrobial activity and mode of action have been studied using the mini-host model of Caenorhabditis elegans infected by a multidrug-resistant strain of P. aeruginosa (4). Furthermore, promising results have been obtained from peptide-treatment of cows with clinical mastitis. Overall, these studies suggest frog-skin AMPs as attractive molecules to assist in the future design and manufacturing of new peptide-based anti-infective drugs. 1. Mangoni, M. L. and Shai Y. Cell Mol Life Sci. 2011; 68:2267-80. 2. Mangoni ML et al. J. Biol Chem. 2008; 283:22907-17 3. Bhunia A, et al. J. Biol Chem. 2011; 286:24394-406 4. Uccelletti D. et al. Antimicrob Agents Chemother. 2010;54:3853-60.

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