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Synthesis and Characterization of Supramolecular Colloids
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Hybrid Double-Chain Maltose-Based Detergents: Synthesis and Colloidal and Biochemical Evaluation
Christophe Bonnet1,2, Pierre Guillet1,2, Sébastien Igonet2,3
1Equipe Chimie Bioorganique et Systèmes Amphiphiles , Institut des Biomolécules Max Mousseron (UMR 5247 UM-CNRS-ENSCM) & Avignon University , 301 rue Baruch de Spinoza , 84916 Avignon cedex 9 , France.
The Journal of Organic Chemistry
|August 16, 2019
Summary
New hybrid surfactants with maltose heads show potential for membrane protein extraction and stabilization. These novel compounds effectively solubilize receptors like adenosine A2A receptor and bacterial transporters, with one derivative offering significant thermostabilization.
Area of Science:
- Biochemistry
- Materials Science
- Supramolecular Chemistry
Background:
- Developing novel surfactants is crucial for membrane protein research.
- Hybrid surfactants offer unique properties combining different chain characteristics.
- Maltose-based surfactants are of interest due to their biocompatibility.
Purpose of the Study:
- To synthesize and characterize novel hybrid double-chain surfactants with maltose headgroups.
- To investigate the self-assembly behavior and water solubility of these surfactants.
- To evaluate their efficacy in solubilizing and stabilizing membrane proteins.
Main Methods:
- Synthesis of four hybrid double-chain surfactants with varying chain lengths.
- Dynamic light scattering and transmission electron microscopy for aggregate analysis.
- Solubilization assays using GPCR adenosine A2A receptor and AcrB transporter.
- Thermostabilization studies using differential scanning calorimetry.
Main Results:
- Synthesized surfactants exhibited low water solubility but formed aggregates in water.
- Mixed micelles were formed with n-dodecylmaltoside (DDM), improving solubility.
- Efficient extraction of A2A receptor (40-70%) and AcrB (60-90%) was achieved.
- Three hybrids demonstrated significant protein thermostabilization, with one showing a ~7 °C increase for A2A receptor.
Conclusions:
- Hybrid surfactants can form aggregates and mixed micelles with DDM.
- These novel surfactants are effective in extracting and stabilizing membrane proteins.
- The derivative with a C12-hydrogenated and C4F9-fluorinated chain is a promising additive for protein studies.
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