Asymmetric distribution of phosphatidyl serine in supported phospholipid bilayers on titanium dioxide

Supported phospholipid bilayers (SPBs) are useful for studying cell adhesion, cell-cell interactions, protein-lipid interactions, protein crystallization, and applications in biosensor and biomaterial areas. We have recently reported that SPBs could be formed on titanium dioxide, an important biomat...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 22(2006), 8 vom: 11. Apr., Seite 3467-73
1. Verfasser: Rossetti, Fernanda F (VerfasserIn)
Weitere Verfasser: Textor, Marcus, Reviakine, Ilya
Format: Aufsatz
Sprache:English
Veröffentlicht: 2006
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Lipid Bilayers Phosphatidylcholines Phosphatidylserines Phospholipids titanium dioxide 15FIX9V2JP Silicon Dioxide 7631-86-9 mehr... Titanium D1JT611TNE 1,2-oleoylphosphatidylcholine EDS2L3ODLV Calcium SY7Q814VUP
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100 1 |a Rossetti, Fernanda F  |e verfasserin  |4 aut 
245 1 0 |a Asymmetric distribution of phosphatidyl serine in supported phospholipid bilayers on titanium dioxide 
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500 |a Date Revised 16.11.2017 
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520 |a Supported phospholipid bilayers (SPBs) are useful for studying cell adhesion, cell-cell interactions, protein-lipid interactions, protein crystallization, and applications in biosensor and biomaterial areas. We have recently reported that SPBs could be formed on titanium dioxide, an important biomaterial, from vesicles containing anionic phospholipid phosphatidyl serine (PS) in the presence of calcium. Here, we show that the mobility of the fluorescently labeled PS present in these bilayers is severely restricted, whereas that of the zwitterionic phosphatidyl choline is not affected. Removal of calcium alleviated the restriction on the mobility of PS. Both components were found to be mobile in SPBs of identical compositions prepared in the presence of calcium on silica. To explain these results, we propose that, on TiO2, PS is trapped in the proximal leaflet of the bilayers. This proposal is supported by the results of protein adsorption experiments carried out on bilayers containing various amounts of PS prepared on silica and titania 
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700 1 |a Textor, Marcus  |e verfasserin  |4 aut 
700 1 |a Reviakine, Ilya  |e verfasserin  |4 aut 
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