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Maltose-Based Fluorinated Surfactants for Membrane-Protein Extraction and Stabilization.
Moheddine Wehbie1, Kenechi Kanayo Onyia2,3, Florian Mahler2
1Institut des Biomolécules Max Mousseron (UMR 5247 UM-CNRS-ENSCM) & Avignon University, Equipe Chimie Bioorganique et Systèmes amphiphiles, 301 rue Baruch de Spinoza, 84916 cedex 9 Avignon, France.
Langmuir : the ACS Journal of Surfaces and Colloids
|February 4, 2021
Summary
New fluorinated surfactants, F5OM and F5DM, effectively solubilize membrane proteins and enhance their stability. These novel maltose-based compounds show promise for membrane protein applications.
Area of Science:
- Biochemistry
- Materials Science
- Physical Chemistry
Background:
- Partially fluorinated analogues of n-dodecyl-β-D-maltoside (DDM) were designed.
- Understanding surfactant properties is crucial for membrane protein (MP) applications.
Purpose of the Study:
- To evaluate the micellization properties and aggregate morphologies of F5OM and F5DM.
- To assess the efficacy of these new surfactants in solubilizing and stabilizing membrane proteins.
Main Methods:
- NMR spectroscopy, surface tension measurement, isothermal titration calorimetry.
- Dynamic light scattering, small-angle X-ray scattering, analytical ultracentrifugation.
- Solubilization and stability assays with membrane proteins from E. coli.
Main Results:
- Critical micellar concentration (cmc) decreased with fluorinated tail length (F5OM: 2.1-2.5 mM, F5DM: 0.3-0.5 mM).
- Micelles formed rods (4 nm diameter) with increasing dimensions at higher concentrations.
- F5OM and F5DM showed superior solubilization efficiency compared to F6H2OM and DDM at low concentrations.
- Proteins bacteriorhodopsin (bR) and FhuA exhibited enhanced thermal stability in the new surfactants.
Conclusions:
- F5OM and F5DM possess effective membrane protein extracting and stabilizing properties.
- These novel maltose-based fluorinated surfactants are promising tools for membrane protein research and applications.
