New Detergent‐Like Polymerizable Monomers for membrane protein extraction

CALIXAR announces the publication of a new article from its joint research laboratory CHEM2STAB in the European Journal of Organic Chemistry.

This work conducted by chemists from Avignon University, biophysicists from TU Technische Universität Kaiserslautern  and biochemists from CALIXAR highlights the synthesis of three monomers which are allowed to solubilize phospholipid vesicles and to extract a broad range of membrane proteins.

Three monomers with a maltose polar head, an alkyl hydrogenated chain, and an acrylamide‐based polymerizable moiety were synthesized. The self‐assembly properties in aqueous solutions of these monomers were studied by means of isothermal titration calorimetry (ITC), surface tension (SFT) measurements, and dynamic light scattering (DLS), which indicated the formation of small micellar aggregates of about 6 nm diameter. The critical micellar concentration (CMC) was found to depend on the length of the alkyl chain and on the nature of the polymerizable moiety, ranging from 0.35 mM to ~10 mM. The monomers were found to solubilize phospholipid vesicles and to extract a broad range of proteins from Escherichia coli membranes. Finally, the extraction of two membrane proteins, namely, the full‐length, wild‐type human G‐protein‐coupled receptor (GPCR) adenosine receptor (A 2A R) and the bacterial transporter AcrB was demonstrated.

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