Duramycin-induced destabilization of a phosphatidylethanolamine monolayer at the air-water interface observed by vibrational sum-frequency generation spectroscopy
Duramycin is a small tetracyclic peptide which binds specifically to ethanolamine phospholipids (PE). In this study, we used lipid monolayers consisting of 1-palmitoyl-2-oleoyl phosphatidylethanolamine (POPE) and various phosphatidylcholines (PC) to investigate the effect of duramycin on the organiz...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 26(2010), 20 vom: 19. Okt., Seite 16055-62 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2010
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Amides Bacteriocins Peptides Phosphatidylethanolamines Water 059QF0KO0R duramycin 1391-36-2 mehr... |
| Zusammenfassung: | Duramycin is a small tetracyclic peptide which binds specifically to ethanolamine phospholipids (PE). In this study, we used lipid monolayers consisting of 1-palmitoyl-2-oleoyl phosphatidylethanolamine (POPE) and various phosphatidylcholines (PC) to investigate the effect of duramycin on the organization of lipids and its influence on surrounding water molecules, using vibrational sum-frequency generation spectroscopy in conjunction with surface pressure measurements and fluorescence microscopy. The results show that while duramycin has no effect on the PC lipid monolayers, it induces significant disorder of PE molecules and causes an increase of the PE monolayer surface pressure. Duramycin adopts a β-sheet conformation and is well-ordered at the air-water interface as well as after binding to PE. Our results are consistent with duramycin inserting into the PE monolayer via its hydrophobic end, exposing phenylalanine residues to the lipid. Binding of duramycin to PE broadens the hydrogen-bond distribution of lipid-bound water molecules, notably increasing the fraction of the less strongly hydrogen-bonded, possibly undercoordinated, water molecules. Fluorescence microscopy reveals that the interaction of duramycin with PE causes a change in the shape of the liquid-condensed domains of the PE monolayer from circular to horseshoe-like, indicating a reduction of line tension at the boundary of the two lipid phases. These results reveal that the first steps in the disruption of membrane integrity by duramycin consist of a reduction of the line tension, a decrease in the lipid order, and a weakening of the hydrogen bonding network of water around PE |
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| Beschreibung: | Date Completed 21.01.2011 Date Revised 21.11.2013 published: Print Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/la1028965 |