title: Short native antimicrobial peptides and engineered ultrashort lipopeptides: similarities and differences in cell specificities and modes of action.
abstract: Due to the rapid emergence of resistant microbes to the currently available antibiotics, cationic antimicrobial peptides have attracted considerable interest as a possible new generation of anti-infective compounds. However, low cost development for therapeutic or industrial purposes requires, among other properties, that the peptides will be small and with simple structure. Therefore, considerable research has been devoted to optimizing peptide length combined with a simple design. This review focuses on the similarities and differences in the mode of action and target cell specificity of two families of small peptides: the naturally occurring temporins from the skin of amphibia and the engineered ultrashort lipopeptides. We will also discuss the finding that acylation of cationic peptides results in molecules with a more potent spectrum of activity and a higher resistance to proteolytic degradation. Conjugation of fatty acids to linear native peptide sequences is a powerful strategy to engineer novel successful anti-infective drugs.
authors.affiliation: Istituto Pasteur-Fondazione Cenci Bolognetti, La Sapienza University of Rome, 00185, Rome, Italy, marialuisa.mangoni@uniroma1.it
authors.forename: Maria Luisa
authors.initials: ML
authors.lastname: Mangoni
authors.forename: Yechiel
authors.initials: Y
authors.lastname: Shai
mesh_terms: D000215:Acylation; D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000494:pharmacology*; D002462:Cell Membrane / Q000737:chemistry / Q000187:drug effects; D002463:Cell Membrane Permeability; D015195:Drug Design; D005227:Fatty Acids / Q000737:chemistry; D006801:Humans; D055666:Lipopeptides / Q000737:chemistry* / Q000494:pharmacology*; D008563:Membrane Lipids / Q000737:chemistry; D008969:Molecular Sequence Data; D015202:Protein Engineering; D011506:Proteins / Q000737:chemistry / Q000494:pharmacology
chemical_list: D023181:Antimicrobial Cationic Peptides; D005227:Fatty Acids; D055666:Lipopeptides; D008563:Membrane Lipids; D011506:Proteins; C104501:temporin