There is growing research, industrial, and commercial interest in the study of membrane proteins in general, and more specifically in immobilizing membrane proteins to various biosensor surfaces.
Surface plasmon resonance (SPR) is a direct label-free technique that provides real-time data on the affinity, specificity, and kinetics of biomolecular interactions.
Membrane proteins are typically analyzed in biosensors after incorporation into liposomes or lipoparticles (virus-like particles).
The memLAYER products used in this study are based on the proprietary DNA tether enhanced liposome immobilization (TELI) technology from Layerlab AB (Göteborg, Sweden). The memLAYER technology can be used in various applications, including the transport of molecules over cell membrane that is mediated via membrane proteins such as aquaporins and melittin, activity of membrane proteins such as GPCR and clotting factors, and passive diffusion of small uncharged molecules over liposome membrane.
Why is determining lipid specificity and affinity important?
High-affinity interactions between peripheral proteins regulate lipid signalling from the cellular membrane. Using techniques like surface plasmon resonance (SPR) to accurately determine lipid specificity and membrane affinity is important for establishing how the membrane interface signals throughout a cell. There are a few biochemical and biophysical experiments used to determine the specificity and affinity of lipids in the field, but SPR has become a key label-free technique for this type of analysis.
Liposome sensor chips are used to capture user-prepared liposomes. They are composed of covalently attached lipophilic groups. Lipid vesicles, or liposomes, mimic biological membranes and can be a convenient way to study membrane systems.
Yes, this means that you can study transmembrane proteins using liposome sensor chips by reconstituting your protein into the liposome and directly capturing the liposome using the liposome sensor chips!
Membrane protein-protein interactions
Peripheral protein-protein interactions
Hydrophobic sensor chips are used to immobilize lipid molecules into a monolayer on the sensor surface. Hydrophobic sensor chips are coated with a hydrophobic layer of long-chain alkane molecules, which means that partially solubilized lipids will self-assemble to the surface creating a monolayer with the hydrophilic groups positioned away from the surface.
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