Microarrays are tools for screening the binding interactions of biomolecules. In the usual design, different biomolecules are printed by fluidic dispensing from a robotic spotter into designated positions (spots), hundreds of microns in diameter, to form a spatially indexed array of probe or capture molecules. The array is covered with an analyte solution containing a target biomolecule which can potentially bind to one or more of the capture molecules in the array. After allowing binding to proceed, the surface is washed and analyzed to identify the conjugation of targets, usually by labeling the targets with a fluorophore whose signature fluorescence is detected at the positions where the printed molecules have bound targets. As the size of the array spots is of the order of hundreds of microns in diameter, a chip with an active area of 1 cm x 1 cm and thousands of elements can screen a very large number of interactions with a very small volume of target analyte (approximately 1 ml to cover the active area). The high throughput, high capacity nature of the microarray tool has brought it to pre-eminence in clinical diagnostics, and drug discovery efforts. The above current approach to microarraying is not suitable for the display of cell membrane receptors (e.g. membrane protein receptors) because these biomolecules require their native membrane lipid environment in order to retain their binding capacity. This problem is very important to drug discovery efforts which usually target membrane receptors to achieve their therapeutic effect, and in which the screening of lead compounds with membrane receptors is essential in designing molecules which bind strongly and with great specificity to the receptor. At present drug discovery research cannot take advantage of the high throughput nature of microarrays, since active membrane receptor molecules cannot simply be spotted onto the surface. Our approach for implementing a membrane receptor microarray is to use liposomes to host the membrane receptor probes in order to retain their binding activity, and then array the liposomes onto a surface to display the receptors. Individual, intact phospholipid bilayer liposomes, which are on the order of 1 micron in diameter, are positioned in microwells etched in a regular array on a silicon oxide substrate. The diameter of the wells is on the order of the liposome diameter, so only one liposome is located in each well. The background of the silicon oxide surface is functionalized with a PEG oligomer using the contact printing of a PEG silane to present a surface that resists the adsorption of proteins, lipid material, and liposomes. The interiors of the wells are functionalized with an aminosilane to facilitate the conjugation of biotin, which is then bound to Neutravidin. The avidin-coated well interiors bind the liposomes whose surfaces contain biotinylated lipids. The specific binding of the liposomes to the surface using the biotin-avidin linkage, together with the resistant nature of the background and the physical confinement of the wells, allows the liposomes to remain intact and to not unravel, rupture, and fuse onto the surface. We demonstrate this intact arraying using confocal laser scanning microscopy of fluorophores specifically tagging the microwells, the lipid bilayer, and the aqueous interior of the liposome. The utilization of this format for receptor display as a biosensor is also demonstrated by using the liposome array to display GM1 ganglioside receptors which bind cholera toxin subunit B (CTx-B). GM1 was incorporated in the lipid bilayer of liposomes and these receptor liposomes were arrayed onto chemically functionalized substrates. Demonstration of the ability of the receptors to bind exclusively to cholera toxin is shown by fluorescent labeling of the target toxin and the probe ganglioside.