Microscopic visualization of alamethicin incorporation into model membrane monolayers

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 interfac...

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Bibliographische Detailangaben
Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 20(2004), 25 vom: 07. Dez., Seite 11084-91
1. Verfasser: Volinsky, Roman (VerfasserIn)
Weitere Verfasser: Kolusheva, Sofiya, Berman, Amir, Jelinek, Raz
Format: Aufsatz
Sprache:English
Veröffentlicht: 2004
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Membranes, Artificial Phospholipids Polyacetylene Polymer Polymers Water 059QF0KO0R Polyynes 25067-58-7 mehr... Alamethicin 27061-78-5 polydiacetylene 27987-87-7 Acetylene OC7TV75O83
Beschreibung
Zusammenfassung: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 phospholipid/PDA film assemblies for studying membrane-peptide association and interactions within two-dimensional films
Beschreibung:Date Completed 30.05.2006
Date Revised 01.12.2018
published: Print
Citation Status MEDLINE
ISSN:1520-5827