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|a pubmed24n0515.xml
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|a (DE-627)NLM154552003
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|a (NLM)15803690
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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1 |
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|a Kuiper, Johanna M
|e verfasserin
|4 aut
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|a H-aggregation of azobenzene-substituted amphiphiles in vesicular membranes
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|c 2004
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|a Text
|b txt
|2 rdacontent
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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|a Band
|b nc
|2 rdacarrier
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|a Date Completed 26.01.2006
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|a Date Revised 26.10.2019
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|a published: Print
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|a Citation Status MEDLINE
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|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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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Azo Compounds
|2 NLM
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|a Escherichia coli Proteins
|2 NLM
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|a Fluoresceins
|2 NLM
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|a Ion Channels
|2 NLM
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|a Lipid Bilayers
|2 NLM
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|a Lipids
|2 NLM
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|a Liposomes
|2 NLM
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|a Membrane Lipids
|2 NLM
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|a Membranes, Artificial
|2 NLM
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|a MscL protein, E coli
|2 NLM
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|a Phosphates
|2 NLM
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|a Phosphatidylcholines
|2 NLM
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|a Phospholipids
|2 NLM
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|a Hydrogen
|2 NLM
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|a 7YNJ3PO35Z
|2 NLM
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|a 1,2-oleoylphosphatidylcholine
|2 NLM
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|a EDS2L3ODLV
|2 NLM
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|a azobenzene
|2 NLM
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|a F0U1H6UG5C
|2 NLM
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|a fluorexon
|2 NLM
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|a V0YM2B16TS
|2 NLM
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1 |
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|a Engberts, Jan B F N
|e verfasserin
|4 aut
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773 |
0 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 20(2004), 4 vom: 17. Feb., Seite 1152-60
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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773 |
1 |
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|g volume:20
|g year:2004
|g number:4
|g day:17
|g month:02
|g pages:1152-60
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|a GBV_USEFLAG_A
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|a SYSFLAG_A
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|a GBV_NLM
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|a GBV_ILN_22
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|a GBV_ILN_350
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|a GBV_ILN_721
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|a AR
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|d 20
|j 2004
|e 4
|b 17
|c 02
|h 1152-60
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