Lactoferrin-derived antimicrobial peptide induces a micellar cubic phase in a model membrane system |
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Authors: | Bastos Margarida Silva Tânia Teixeira Vitor Nazmi Kamran Bolscher Jan G M Funari Sérgio S Uhríková Daniela |
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Affiliation: | †Centro de Investigação em Química (UP), Department of Chemistry and Biochemistry, Faculty of Sciences, University of Porto, Porto, Portugal;‡Academic Centre Dentistry Amsterdam, Department of Oral Biochemistry, Amsterdam, The Netherlands;§Hamburger Synchrotronstrahlungslabor (HASYLAB), Deutsches Elektronen-Synchrotron, Hamburg, Germany;¶Faculty of Pharmacy, Comenius University, Bratislava, Slovak Republic |
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Abstract: | The observation of a micellar cubic phase is reported for a mixture of an antimicrobial peptide from the Lactoferrin family, LFampin 265-284, and a model membrane system of dimyristoylphosphatidylcholine/dimyristoylphosphatidylglycerol (3:1), as derived from small-angle x-ray diffraction (SAXD) measurements. The system shows remarkable thermotropic polymorphism: the peptide disrupts the lipid bilayer, forming a cubic phase of the space group Pm3n (t < 28°C), and as the temperature increases it shows a complex phase behavior (not fully clarified by SAXD). The onset, volume fraction of each phase, and phase parameters are seen to vary with peptide/lipid ratio and temperature. The obtained SAXD data represent the first experimental evidence, to our knowledge, of a micellar cubic phase in the context of antimicrobial peptide/membrane interaction. We propose that the micellization of the membrane according to the carpet model, for long proposed as a possible mechanism of action, can go through the formation of a cubic micellar phase. |
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