Abstract
| - Lipid interactions and cooperative assembly properties are fundamental determinants for the action ofantimicrobial membrane-active peptides. Here we analyze the interactions and aggregation properties ofalamethicin, an antimicrobial pore-forming peptide, with films formed at the air/water interface. Surface-area/pressure isotherms, Brewster angle microscopy, and fluorescence-confocal microscopy provided detailedinformation on the morphologies and structural properties of the peptide and its effect on the film components.The pressure−area analysis and microscopy experiments facilitated unprecedented visualization of thestructural consequences of alamethicin association at the air/water interface, with pure phospholipidfilms, and within mixed phospholipid/polydiacetylene (PDA) films. The analysis exposed the kinetic featuresand the interplay between the peptide aggregates and film constituents. In particular, the results demonstratethe use of phospholipid/PDA film assemblies for studying membrane−peptide association and interactionswithin two-dimensional films.
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