title: Membrane interaction and antibacterial properties of two mildly cationic peptide diastereomers, bombinins H2 and H4, isolated from Bombina skin.
abstract: Bombinins H are mildly cationic antimicrobial peptides isolated from the skin of the anuran genus Bombina, the fire-bellied toad. Some members of this peptide family coexist in skin secretions as diastereomers in which a single D: -amino acid (alloisoleucine or leucine) is incorporated as a result of the post-translational modification of the respective gene-encoded L-amino acid. Here we report on the antimicrobial properties and membrane interactions of bombinins H2 and H4. The latter differs from H2 by the presence of a D-alloisoleucine at the second N-terminal position. Specifically, we have evaluated the antimicrobial activity of H2 and H4 against a large panel of reference and clinical isolates of Gram-negative and Gram-positive bacteria; performed membrane permeation assays on both intact cells and model membranes (lipid monolayers and liposomes) mimicking the composition of the plasma membrane of Gram-negative/positive bacteria; used biochemical tools, such as trypsin-encapsulated liposomes and capillary electrophoresis, to monitor the peptides' ability to translocate through the membrane of liposomes mimicking Escherichia coli inner membrane. The results revealed interesting relationships between the presence of a single D: -amino acid in the sequence of an antimicrobial peptide and its target microbial cell selectivity/membrane-perturbing activity.
authors.affiliation: Dipartimento di Scienze e Tecnologie Biomediche, Università de L'Aquila, 67010 L'Aquila, Italy.
authors.forename: Cristina
authors.initials: C
authors.lastname: Coccia
authors.forename: Andrea C
authors.initials: AC
authors.lastname: Rinaldi
authors.forename: Vincenzo
authors.initials: V
authors.lastname: Luca
authors.forename: Donatella
authors.initials: D
authors.lastname: Barra
authors.forename: Argante
authors.initials: A
authors.lastname: Bozzi
authors.forename: Antonio
authors.initials: A
authors.lastname: Di Giulio
authors.forename: Enno C I
authors.initials: EC
authors.lastname: Veerman
authors.forename: Maria Luisa
authors.initials: ML
authors.lastname: Mangoni
mesh_terms: D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D001001:Anura / Q000378:metabolism*; D002463:Cell Membrane Permeability / Q000187:drug effects; D006090:Gram-Negative Bacteria / Q000145:classification / Q000187:drug effects / Q000378:metabolism; D006094:Gram-Positive Bacteria / Q000145:classification / Q000187:drug effects / Q000378:metabolism; D007532:Isoleucine / Q000737:chemistry / Q000494:pharmacology; D007930:Leucine / Q000737:chemistry / Q000494:pharmacology; D008081:Liposomes / Q000737:chemistry / Q000378:metabolism; D012867:Skin / Q000378:metabolism*; D013237:Stereoisomerism; D013997:Time Factors
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D008081:Liposomes; C510197:bombinin H2; D007532:Isoleucine; D007930:Leucine