Free-standing films of fluorinated surfactants as 2D matrices for organizing detergent-solubilized membrane proteins

The possibility of organizing detergent-solubilized membrane proteins in a plane within the core of Newton black films (NBFs) formed from fluorinated surfactants has been investigated. Fluorinated surfactants have the interesting characteristics of being poorly miscible with detergents and highly su...

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Bibliographische Detailangaben
Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 23(2007), 8 vom: 10. Apr., Seite 4303-9
1. Verfasser: Petkova, Vera (VerfasserIn)
Weitere Verfasser: Benattar, Jean-Jacques, Zoonens, Manuela, Zito, Francesca, Popot, Jean-Luc, Polidori, Ange, Jasseron, Sylvain, Pucci, Bernard
Format: Aufsatz
Sprache:English
Veröffentlicht: 2007
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Bacterial Outer Membrane Proteins Detergents Lipoproteins Membrane Proteins Micelles Proteins Surface-Active Agents OMPA outer membrane proteins mehr... 149024-69-1 polyhistidine 26062-48-6 Fluorine 284SYP0193 Histidine 4QD397987E Nickel 7OV03QG267
Beschreibung
Zusammenfassung:The possibility of organizing detergent-solubilized membrane proteins in a plane within the core of Newton black films (NBFs) formed from fluorinated surfactants has been investigated. Fluorinated surfactants have the interesting characteristics of being poorly miscible with detergents and highly surface-active. As a result, when a membrane protein-the transmembrane domain of OmpA (tOmpA)-solubilized by the nonionic detergent C8E4 (tetraethylene glycol monooctyl ether) was injected under a monolayer of fluorinated surfactant, C8E4 and tOmpA/C8E4 complexes remained confined to the subphase. Vertical, macroscopic NBFs were drawn, and their structure was investigated by means of X-ray reflectivity. Depending on experimental conditions, the protein was shown to organize into either one or two monolayers stabilized by two monolayers of fluorinated surfactant. Two different mechanisms of protein insertion were investigated: (i) attachment of polyhistidine-tagged tOmpA/C8E4 complexes to nickel-bearing polar groups born by a fluorinated surfactant and (ii) spontaneous diffusion into the surfactant films. Possible applications are discussed
Beschreibung:Date Completed 27.06.2007
Date Revised 21.11.2013
published: Print-Electronic
Citation Status MEDLINE
ISSN:1520-5827