Biological characterization and modes of action of temporins and bombinins H, multiple forms of short and mildly cationic anti-microbial peptides from amphibian skin.
Genetically encoded cationic anti-microbial peptides (AMPs) are essential components of the ancient and non-specific innate immune system, which is the principal defence mechanism of all species of life, with the primary role to kill infectious microorganisms. Amphibian skin is one of the richest natural sources of such molecules, which are produced by holocrine-type dermal glands and released upon stimulation. This review highlights the attractive and unique structural/functional properties of temporins and bombinins H, two families of short and mildly cationic peptides, isolated from the skin of frogs belonging to Rana and Bombina genera, respectively. Beside improving our knowledge on the role of AMPs in the regulation of the innate immunity, the biological significance of the existence of multiple forms of a prototypic peptide sequence within the same organism and the implication of short peptides in the endotoxin neutralization, these two classes of AMPs can be also considered as valid candidates for the design of novel anti-infective and anti-sepsis drugs.
Mangoni
Maria Luisa
ML
Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche A. Rossi Fanelli, II Facoltà di Medicina e Chirurgia, Sapienza Università di Roma, Azienda Ospedaliera S. Andrea - Roma, Italy. marialuisa.mangoni@uniroma1.it
Marcellini
H G Ludovica
HG
Simmaco
Maurizio
M
D000595:Amino Acid Sequence; D000818:Animals; D000890:Anti-Infective Agents / Q000737:chemistry / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology* / Q000502:physiology*; D001001:Anura / Q000235:genetics / Q000502:physiology*; D004357:Drug Synergism; D006090:Gram-Negative Bacteria / Q000187:drug effects; D006094:Gram-Positive Bacteria / Q000187:drug effects; D007891:Leishmania / Q000187:drug effects / Q000648:ultrastructure; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology* / Q000502:physiology*; D011898:Ranidae / Q000235:genetics / Q000502:physiology; D012879:Skin Physiological Phenomena
D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D011506:Proteins; C510197:bombinin H2; C104501:temporin