Lactoferrin-derived antimicrobial peptide induces a micellar cubic phase in a model membrane system

M. Bastos, T. Silva, V. Teixeira, K. Nazmi, J.G.M. Bolscher, S.S. Funari, D. Uhríková

Research output: Contribution to JournalArticleAcademicpeer-review

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.

Original languageEnglish
Pages (from-to)L20-L22
JournalBiophysical Journal
Volume101
Issue number3
DOIs
Publication statusPublished - 2011

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