H-aggregation of azobenzene-substituted amphiphiles in vesicular membranes

Photochemical switching has been studied of double-tailed phosphate amphiphiles containing azobenzene units in both tails in aqueous vesicular dispersions and in mixed vesicular systems with 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC). Since the ease of switching depends on the strength of the b...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 20(2004), 4 vom: 17. Feb., Seite 1152-60
1. Verfasser: Kuiper, Johanna M (VerfasserIn)
Weitere Verfasser: Engberts, Jan B F N
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 Azo Compounds Escherichia coli Proteins Fluoresceins Ion Channels Lipid Bilayers Lipids Liposomes Membrane Lipids mehr... Membranes, Artificial MscL protein, E coli Phosphates Phosphatidylcholines Phospholipids Hydrogen 7YNJ3PO35Z 1,2-oleoylphosphatidylcholine EDS2L3ODLV azobenzene F0U1H6UG5C fluorexon V0YM2B16TS
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100 1 |a Kuiper, Johanna M  |e verfasserin  |4 aut 
245 1 0 |a H-aggregation of azobenzene-substituted amphiphiles in vesicular membranes 
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520 |a Photochemical switching has been studied of double-tailed phosphate amphiphiles containing azobenzene units in both tails in aqueous vesicular dispersions and in mixed vesicular systems with 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC). Since the ease of switching depends on the strength of the bilayer packing, particular emphasis has been placed on the occurrence of H-aggregation in the hydrophobic core of the vesicles. UV-vis spectrometry was employed to monitor H-aggregation and showed how this process depends on the ionic strength and on the mode of preparation of the vesicles. Two types of H-aggregates were observed in mixed DOPC vesicles with 5 mol % of azobenzene phosphate: one with lambda(max) at around 300 nm and one with lambda(max) at 305-320 nm. Those with lambda(max) at 300 nm could not be trans-cis photoisomerized, whereas those with lambda(max) at 305-320 nm are more loosely packed and can be photochemically switched. The permeability of the vesicular bilayers, as probed with leakage experiments using calcein as a fluorescent probe, was examined as another measure for the strength of bilayer packing. Leakage occurred only for DOPC vesicles containing more than 20 mol % of azobenzenephosphate, irradiated with UV light to induce trans-cis photoisomerization. We contend that detailed information on bilayer packing will be of crucial importance for fine-tuning the lateral pressure in vesicular membranes with the ultimate aim to steer the opening and closing of mechanosensitive protein channels of large conductance 
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650 7 |a Escherichia coli Proteins  |2 NLM 
650 7 |a Fluoresceins  |2 NLM 
650 7 |a Ion Channels  |2 NLM 
650 7 |a Lipid Bilayers  |2 NLM 
650 7 |a Lipids  |2 NLM 
650 7 |a Liposomes  |2 NLM 
650 7 |a Membrane Lipids  |2 NLM 
650 7 |a Membranes, Artificial  |2 NLM 
650 7 |a MscL protein, E coli  |2 NLM 
650 7 |a Phosphates  |2 NLM 
650 7 |a Phosphatidylcholines  |2 NLM 
650 7 |a Phospholipids  |2 NLM 
650 7 |a Hydrogen  |2 NLM 
650 7 |a 7YNJ3PO35Z  |2 NLM 
650 7 |a 1,2-oleoylphosphatidylcholine  |2 NLM 
650 7 |a EDS2L3ODLV  |2 NLM 
650 7 |a azobenzene  |2 NLM 
650 7 |a F0U1H6UG5C  |2 NLM 
650 7 |a fluorexon  |2 NLM 
650 7 |a V0YM2B16TS  |2 NLM 
700 1 |a Engberts, Jan B F N  |e verfasserin  |4 aut 
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