Surface behaviour and peptide-lipid interactions of the antibiotic peptides, Maculatin and Citropin

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dc.contributor.authorAmbroggio, E.
dc.contributor.authorSeparovic, F.
dc.contributor.authorBowie, J.
dc.contributor.authorFidelio, G.
dc.date.issued2004
dc.descriptionCopyright © 2004 Elsevier B.V. All rights reserved.
dc.description.abstractSurface 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.
dc.description.statementofresponsibilityErnesto E. Ambroggio, Frances Separovic, John Bowie and Gerardo D. Fidelio
dc.description.urihttp://www.elsevier.com/wps/find/journaldescription.cws_home/601272/description#description
dc.identifier.citationBiochimica et Biophysica Acta - Biomembranes, 2004; 1664(1):31-37
dc.identifier.doi10.1016/j.bbamem.2004.03.013
dc.identifier.issn0005-2736
dc.identifier.issn1878-2434
dc.identifier.urihttp://hdl.handle.net/2440/17966
dc.language.isoen
dc.publisherElsevier Science BV
dc.source.urihttps://doi.org/10.1016/j.bbamem.2004.03.013
dc.subjectLipids
dc.subjectPhosphatidylcholines
dc.subjectPhosphatidylglycerols
dc.subjectPeptides
dc.subjectAntimicrobial Cationic Peptides
dc.subjectAmphibian Proteins
dc.subjectAnti-Infective Agents
dc.subjectMagnetic Resonance Spectroscopy
dc.subjectKinetics
dc.subjectAdsorption
dc.subjectHydrogen-Ion Concentration
dc.subjectThermodynamics
dc.titleSurface behaviour and peptide-lipid interactions of the antibiotic peptides, Maculatin and Citropin
dc.typeJournal article
pubs.publication-statusPublished

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