Protein tethered lipid bilayer: an alternative mimic of the biological membrane (Mini Review).

An overview is given about results obtained so far with an alternative concept of solid-supported tethered lipid bilayers for the functional incorporation of membrane proteins. The incorporated protein itself acts as the tethering molecule resulting in a versatile system where the protein determines the characteristics of submembraneous space. This architecture is achieved through a metal chelating surface, onto which histidine-tagged (his-tagged) membrane proteins are able to bind in a reversible manner. The tethered bilayer membrane is generated by substitution of protein bound detergent molecules with lipids using in situ dialysis or adsorption. Histidine-tagged cytochrome c oxidase is used as a model protein in this study. However, the system should be applicable to all recombinant membrane proteins bearing a terminal his tag. The system is particularly designed, among other surface-analytical techniques, for a combined application of electrochemical and vibrational spectroscopy measurements.