Temporins, anti-infective peptides with expanding properties.
Antimicrobial peptides are effector molecules of the innate immune response of all pluricellular organisms, providing them with first-line defence against pathogens. Amphibian skin secretions represent one of the richest natural sources for such peptide antibiotics, and temporins, a large family of antimicrobial peptides from frog skin, are among the smallest ones found in nature to date. Their functional role and modes of action have been described, along with their interesting and unique properties. These properties make temporins good molecules for an in-depth understanding of host defence peptides in general. Furthermore, they are attractive templates for the future design of new therapeutics against infectious diseases with new modes of action, urgently needed due to the increasing resistance of microorganisms to the available drugs.
Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche A. Rossi Fanelli, Università La Sapienza, Piazzale Aldo Moro 5, 00185 Rome, Italy. marialuisa.mangoni@uniroma1.it
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D000818:Animals; D000890:Anti-Infective Agents / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides; D002462:Cell Membrane / Q000378:metabolism; D002463:Cell Membrane Permeability; D016384:Consensus Sequence; D004926:Escherichia coli; D006790:Host-Parasite Interactions; D007113:Immunity, Innate / Q000187:drug effects; D007891:Leishmania; D011506:Proteins / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology*; D011896:Rana temporaria; D017386:Sequence Homology, Amino Acid; D012867:Skin / Q000378:metabolism*; D013329:Structure-Activity Relationship
D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D011506:Proteins; C104501:temporin