Interaction of gramicidin derivatives with phospholipid monolayers
Copyright 2004 American Chemical Society
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 20(2004), 21 vom: 12. Okt., Seite 9291-8 |
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| Weitere Verfasser: | , , , |
| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2004
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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 Metals, Heavy Phosphatidylglycerols Phospholipids Water 059QF0KO0R Gramicidin 1405-97-6 1,2-Dipalmitoylphosphatidylcholine mehr... |
| Zusammenfassung: | Copyright 2004 American Chemical Society A study of the interaction of gramicidin A (gA), tert-butyloxycarbonyl-gramicidin (g-BOC), and desformyl gramicidin (g-des) with dioleoyl phosphatidylcholine (DOPC) and DOPC/phosphatidylserine (PS) mixed monolayers on a mercury electrode is reported in this paper. Experiments were carried out in electrolytes KCl (0.1 mol dm(-3)) and Mg(NO3)2 (0.05 mol dm(-3)). The channel-forming properties of the gramicidins were studied by following the reduction of Tl(I) to Tl(Hg). The frequency dependence of the complex impedance of coated electrode surfaces in the presence and absence of the gramicidins was estimated between 65,000 and 0.1 Hz at potentials of -0.4 V versus Ag/AgCl with 3.5 mol dm(-3) KCl. Epifluorescence microscopy was used to qualitatively correlate the interaction of the gramicidin peptides with dipalmitoyl phosphatidylcholine (DPPC) and dipalmitoyl phosphatidylglycerol (DPPG) at the air-water interface. gA was shown to form Tl+ conducting channels in a DOPC monolayer, while g-BOC and g-des did not. In DOPC-30% PS (DOPC-0.3PS) layers, there is a marked increase in channel activity of all three gramicidin derivatives. None of the peptides facilitate the permeability of the DOPC-0.3PS layer to Cd2+. All three peptides interact with the layer as shown by capacitance-potential curves and impedance spectroscopy indicated by penetration of the peptide into the dielectric, an increase in surface "roughness", and an increased significance of low-frequency relaxations. The order of interaction is gA > g-des > g-BOC. The epifluorescence study of DPPC and DPPG layers at the air-water interface shows a selective action of the different gramicidins |
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| Beschreibung: | Date Completed 25.04.2006 Date Revised 21.11.2013 published: Print Citation Status MEDLINE |
| ISSN: | 1520-5827 |