Linker lipids were embedded in a phosphatidylcholine monolayer matrix prepared at the air–water interface. The covalent coupling of antibody fragments, non-specific adsorption of bovine serum albumin and specific binding of antibodies was monitored in situ with a 10-MHz quartz crystal microbalance. The attachment of antibody fragments and the activity of the layers was also showed with standardized radioimmunoassay. The results demonstrate that the coupling of Fab′-fragments to linker lipids in a monolayer matrix is a promising approach to achieve a highly oriented layer of antibody fragments with a high density of binding sites on the sensor surface for immunological measurements.
Vikholm, I., Albers, M., Välimäki, H., & Helle, H. (1998). In situ Quartz crystal microbalance monitoring of Fab'-fragment binding to linker lipids in a phoshatidylcholine monolayer matrix: Application to immunosensors. Thin Solid Films, 327-329, 643-646. https://doi.org/10.1016/S0040-6090(98)00731-7