Microscopic visualization of alamethicin incorporation into model membrane monolayers

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31 Scopus citations


Lipid interactions and cooperative assembly properties are fundamental determinants for the action of antimicrobial membrane-active peptides. Here we analyze the interactions and aggregation properties of alamethicin, 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 detailed information 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 the structural consequences of alamethicin association at the air/water interface, with pure phospholipid films, and within mixed phospholipid/polydiacetylene (PDA) films. The analysis exposed the kinetic features and the interplay between the peptide aggregates and film constituents. In particular, the results demonstrate the use of phospholipio/PDA film assemblies for studying membrane-peptide association and interactions within two-dimensional films.

Original languageEnglish
Pages (from-to)11084-11091
Number of pages8
Issue number25
StatePublished - 7 Dec 2004

ASJC Scopus subject areas

  • General Materials Science
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Spectroscopy
  • Electrochemistry


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