The Temporins

RINALDI, ANDREA;Conlon JM

2013-01-01

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Abstract

The temporins belong to a family of short (8–17 amino acids), hydrophobic, C-terminally α-amidated peptides with antibacterial and antifungal properties that are synthesized in the skins of a wide range of North American and Eurasian frogs of the Ranidae family. Temporins adopt an α-helical conformation in hydrophobic environments and have the ability to perturb the integrity of target cell membranes. Not all temporins are cationic, but the number of positively charged amino acids correlates with antimicrobial potency. Temporins are mostly effective against Gram-positive bacteria, but some are also active against Gram-negative bacteria. Temporins show potential for development into therapeutically valuable anti-infective agents, particularly for use against antibiotic- resistant Gram-positive bacteria such as methicillin-resistant Staphylococcus aureus (MRSA) and Enterococcus faecalis, against anaerobic pathogens such as Clostridium difficile, and against the protozoan parasite Leishmania spp. Although the clinical usefulness of naturally occurring temporins is limited by high hemolytic activity, noncytotoxic analogs have been designed