Sparsely tethered bilayer lipid membranes formed by self-assembly of bicelles: Spectroelectrochemical characterization and incorporation of transmembrane protein.

Many biochemical processes related to proper homeostasis take place in cell membranes. The key molecules involved in these processes are proteins, including transmembrane proteins. These macromolecules still challenge the understanding of their function within the membrane. Biomimetic models that mimic the properties of the cell membrane can help understand their functionality. Unfortunately, preserving the native protein structure in such systems is problematic. A possible solution to this problem involves the use of bicelles. Their unique properties make integrating bicelles with transmembrane proteins manageable while preserving their native structure. Hitherto, bicelles have not been used as precursors for protein-hosting lipid membranes deposited on solid substrates like pre-modified gold. Here, we demonstrated that bicelles can be self-assembled to form sparsely tethered bilayer lipid membranes and the properties of the resulting membrane satisfy the conditions suitable for transmembrane protein insertion. We showed that the incorporation of α-hemolysin toxin in the lipid membrane leads to a decrease in membrane resistance due to pore formation. Simultaneously, the insertion of the protein causes a drop in the capacitance of the membrane-modified electrode, which can be explained by the dehydration of the polar region of the lipid bilayer and the loss of water from the submembrane region.