We demonstrate feasibility of biophysical characterization of the peripheral cannabinoid receptor CB2 produced by heterologous expression in E. coli membranes. Recombinant receptor was purified by affinity chromatography, and NMR diffusion experiments performed on CB2 solubilized in dodecylphosphocholine (DPC) micelles. Circular dichroism spectroscopy indicated high α-helical content (49 %) of CB2.
Keywords: Cannabinoid receptor CB2, dodecylphosphocholine micelles, circular dichroism spectroscopy, 1H NMR, ligand binding
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