Bombinins H are mildly cationic antimicrobial peptides isolated from the skin of the anuran genus Bombina. Some members of this peptide family coexist in skin secretions as diastereomers in which a single L-amino acid is post-translational modified to produce the respective D-amino acid. We have evaluated the antimicrobial activity of H2 and H4 (the latter containing a D-alloisoleucine at the second N-terminal position) against a large panel of Gram-negative and Gram-positive bacteria; performed membrane permeation assays on both intact cells and model membranes mimicking the composition of the plasmamembrane of Gram-negative/positive bacteria; used biochemical tools to monitor the peptides’ ability to translocate through the membrane of liposomes mimicking Escherichia coli inner membrane. The results highlight that the presence of a single D-amino acid in the sequence of an antimicrobial peptide is decisive to determine its target microbial cell selectivity and its membrane perturbing activity.

Membrane interaction and antimicrobial features of two peptide diastereomers from Bombina skin / Luca, Vincenzo; C., Coccia; Rinaldi, A. C.; Mangoni, Maria Luisa. - In: THE FEBS JOURNAL. - ISSN 1742-4658. - 278:(2011), pp. 169-169. (Intervento presentato al convegno 36th FEBS Congress, Biochemistry for Tomorrows Medicine tenutosi a Lingotto Conference Center, Torino, Italy nel June 25-30, 2011) [10.1111/j.1742-4658.2011.08137.x].

Membrane interaction and antimicrobial features of two peptide diastereomers from Bombina skin.

LUCA, VINCENZO;MANGONI, Maria Luisa
2011

Abstract

Bombinins H are mildly cationic antimicrobial peptides isolated from the skin of the anuran genus Bombina. Some members of this peptide family coexist in skin secretions as diastereomers in which a single L-amino acid is post-translational modified to produce the respective D-amino acid. We have evaluated the antimicrobial activity of H2 and H4 (the latter containing a D-alloisoleucine at the second N-terminal position) against a large panel of Gram-negative and Gram-positive bacteria; performed membrane permeation assays on both intact cells and model membranes mimicking the composition of the plasmamembrane of Gram-negative/positive bacteria; used biochemical tools to monitor the peptides’ ability to translocate through the membrane of liposomes mimicking Escherichia coli inner membrane. The results highlight that the presence of a single D-amino acid in the sequence of an antimicrobial peptide is decisive to determine its target microbial cell selectivity and its membrane perturbing activity.
2011
36th FEBS Congress, Biochemistry for Tomorrows Medicine
04 Pubblicazione in atti di convegno::04c Atto di convegno in rivista
Membrane interaction and antimicrobial features of two peptide diastereomers from Bombina skin / Luca, Vincenzo; C., Coccia; Rinaldi, A. C.; Mangoni, Maria Luisa. - In: THE FEBS JOURNAL. - ISSN 1742-4658. - 278:(2011), pp. 169-169. (Intervento presentato al convegno 36th FEBS Congress, Biochemistry for Tomorrows Medicine tenutosi a Lingotto Conference Center, Torino, Italy nel June 25-30, 2011) [10.1111/j.1742-4658.2011.08137.x].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/540245
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