title: Surface behaviour and peptide-lipid interactions of the antibiotic peptides, Maculatin and Citropin.
abstract: Surface behaviour of Maculatin 1.1 and Citropin 1.1 antibiotic peptides have been studied using the Langmuir monolayer technique in order to understand the peptide-membrane interaction proposed as critical for cellular lysis. Both peptides have a spontaneous adsorption at the air-water interface, reaching surface potentials similar to those obtained by direct spreading. Collapse pressures (Pi(c), stability to lateral compression), molecular areas at maximal packing and surface potentials (DeltaV) obtained from compression isotherms of both pure peptide monolayers are characteristic of peptides adopting mainly alpha-helical structure at the interface. The stability of Maculatin monolayers depended on the subphase and increased when pH was raised. In an alkaline environment, Maculatin exhibits a molecular reorganization showing a reproducible discontinuity in the Pi-A compression isotherm. Both peptides in lipid films with the zwitterionic palmitoyl-oleoyl-phosphatidylcholine (POPC) showed an immiscible behaviour at all lipid-peptide proportions studied. By contrast, in films with the anionic palmitoyl-oleoyl-phosphatidylglycerol (POPG), the peptides showed miscible behaviour when the peptides represented less than 50% of total surface area. Additional penetration experiments also demonstrated that both peptides better interact with POPG compared with POPC monolayers. This lipid preference is discussed as a possible explanation of their antibiotic properties.
authors.affiliation: CIQUIBIC-CONICET-Departamento de Química Biológica, Facultad de Ciencias Químicas, Haya de la Torre y Medina Allende, Ciudad Universitaria, AP 4, Casilla de Correo 61, Córdoba (CP 5000), Argentina.
authors.forename: Ernesto E
authors.initials: EE
authors.lastname: Ambroggio
authors.forename: Frances
authors.initials: F
authors.lastname: Separovic
authors.forename: John
authors.initials: J
authors.lastname: Bowie
authors.forename: Gerardo D
authors.initials: GD
authors.lastname: Fidelio
mesh_terms: D000327:Adsorption; D029845:Amphibian Proteins / Q000737:chemistry*; D000890:Anti-Infective Agents / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008055:Lipids / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides / Q000737:chemistry*; D010713:Phosphatidylcholines / Q000737:chemistry; D010715:Phosphatidylglycerols / Q000737:chemistry; D013816:Thermodynamics
chemical_list: D029845:Amphibian Proteins; D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D008055:Lipids; D010455:Peptides; D010713:Phosphatidylcholines; D010715:Phosphatidylglycerols; C121829:citropin 1.1 protein, Litoria; C113499:maculatin-1.1 protein, Litoria; C060037:1-palmitoyl-2-oleoylglycero-3-phosphoglycerol; C028694:1-palmitoyl-2-oleoylphosphatidylcholine