Maltose-Based Fluorinated Surfactants for Membrane-Protein Extraction and Stabilization

Two new surfactants, F5OM and F5DM, were designed as partially fluorinated analogues of n-dodecyl-β-D-maltoside (DDM). The micellization properties and the morphologies of the aggregates formed by the two surfactants in water and phosphate buffer were evaluated by NMR spectroscopy, surface tension m...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 37(2021), 6 vom: 16. Feb., Seite 2111-2122
1. Verfasser: Wehbie, Moheddine (VerfasserIn)
Weitere Verfasser: Onyia, Kenechi Kanayo, Mahler, Florian, Le Roy, Aline, Deletraz, Anais, Bouchemal, Ilham, Vargas, Carolyn, Babalola, Jonathan Oyebamiji, Breyton, Cécile, Ebel, Christine, Keller, Sandro, Durand, Grégory
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2021
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Membrane Proteins Micelles Surface-Active Agents Maltose 69-79-4
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520 |a Two new surfactants, F5OM and F5DM, were designed as partially fluorinated analogues of n-dodecyl-β-D-maltoside (DDM). The micellization properties and the morphologies of the aggregates formed by the two surfactants in water and phosphate buffer were evaluated by NMR spectroscopy, surface tension measurement, isothermal titration calorimetry, dynamic light scattering, small-angle X-ray scattering, and analytical ultracentrifugation. As expected, the critical micellar concentration (cmc) was found to decrease with chain length of the fluorinated tail from 2.1-2.5 mM for F5OM to 0.3-0.5 mM for F5DM, and micellization was mainly entropy-driven at 25 °C. Close to their respective cmc, the micelle sizes were similar for both surfactants, that is, 7 and 13 nm for F5OM and F5DM, respectively, and both increased with concentration forming 4 nm diameter rods with maximum dimensions of 50 and 70 nm, respectively, at a surfactant concentration of ∼30 mM. The surfactants were found to readily solubilize lipid vesicles and extract membrane proteins directly from Escherichia coli membranes. They were found more efficient than the commercial fluorinated detergent F6H2OM over a broad range of concentrations (1-10 mM) and even better than DDM at low concentrations (1-5 mM). When transferred into the two new surfactants, the thermal stability of the proteins bacteriorhodopsin (bR) and FhuA was higher than in the presence of their solubilization detergents and similar to that in DDM; furthermore, bR was stable over several months. The membrane enzymes SpNOX and BmrA were not as active as in DDM micelles but similarly active as in F6OM. Together, these findings indicate both extracting and stabilizing properties of the new maltose-based fluorinated surfactants, making them promising tools in MP applications 
650 4 |a Journal Article 
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650 4 |a Research Support, U.S. Gov't, Non-P.H.S. 
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700 1 |a Onyia, Kenechi Kanayo  |e verfasserin  |4 aut 
700 1 |a Mahler, Florian  |e verfasserin  |4 aut 
700 1 |a Le Roy, Aline  |e verfasserin  |4 aut 
700 1 |a Deletraz, Anais  |e verfasserin  |4 aut 
700 1 |a Bouchemal, Ilham  |e verfasserin  |4 aut 
700 1 |a Vargas, Carolyn  |e verfasserin  |4 aut 
700 1 |a Babalola, Jonathan Oyebamiji  |e verfasserin  |4 aut 
700 1 |a Breyton, Cécile  |e verfasserin  |4 aut 
700 1 |a Ebel, Christine  |e verfasserin  |4 aut 
700 1 |a Keller, Sandro  |e verfasserin  |4 aut 
700 1 |a Durand, Grégory  |e verfasserin  |4 aut 
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