Micellar and biochemical properties of a propyl-ended fluorinated surfactant designed for membrane–protein study

[Display omitted] Our goal is to design optimised fluorinated surfactants for handling membrane proteins in solution. We report herein the self-assembling and biochemical properties of a new hemifluorinated surfactant (H3F6H3DigluM) with a branched diglucosylated polar head group and an apolar tail...

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Bibliographic Details
Published in:Journal of colloid and interface science 2015-05, Vol.445, p.127-136
Main Authors: Abla, Maher, Unger, Sebastian, Keller, Sandro, Bonneté, Françoise, Ebel, Christine, Pucci, Bernard, Breyton, Cécile, Durand, Grégory
Format: Article
Language:English
Subjects:
Bacteriorhodopsin
Biochemistry
Biochemistry, Molecular Biology
Fluorinated surfactants
Fluorination
Fluorocarbons - chemistry
Glucosides - chemistry
Halogenation
Hydrophobicity
Life Sciences
Light scattering
Membrane proteins
Membrane Proteins - chemistry
Membranes
Micelles
Protein Stability
Proteins
Solutions
Structural Biology
Surface Tension
Surface-Active Agents - chemistry
Surfactants
Thermodynamics
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Summary:[Display omitted] Our goal is to design optimised fluorinated surfactants for handling membrane proteins in solution. We report herein the self-assembling and biochemical properties of a new hemifluorinated surfactant (H3F6H3DigluM) with a branched diglucosylated polar head group and an apolar tail consisting of a perfluorohexane core decorated with a hydrogenated propyl tip. For the sake of comparison, its fluorinated analogue without propyl tip (F6H3DigluM) was also studied. Isothermal titration calorimetry and surface tension showed that the addition of a propyl tip has a significant effect on the overall hydrophobicity of the surfactant, in contrast to the behaviour described when adding an ethyl tip to a fluorinated surfactant. From dynamic light scattering, analytical ultracentrifugation and small-angle X-ray scattering, both H3F6H3DigluM and F6H3DigluM self-assemble into small globular micelles of 5–7nm in diameter and have aggregation numbers of 62±8 and 46±2, respectively. Finally, H3F6H3DigluM was found to be the best fluorinated surfactant developed in our group to stabilise the model membrane protein bacteriorhodopsin (bR) in aqueous solution. This study demonstrates the suitability of this new propyl-ended fluorinated surfactant for biochemical and structural applications and confirms the superiority of hemifluorinated chains over fluorinated ones.
ISSN:0021-9797
1095-7103
DOI:10.1016/j.jcis.2014.12.066