| Abstract
| - The covalent coupling of antibody fragments to linkers embedded ina monolayer matrix of phosphatidylcholine and cholesterol was examined at the air−water interfaceby the means of a quartz crystalmicrobalance, QCM. Two linkers that bind the free thiols of theFab‘ fragment were investigated. Thenonspecific binding of bovine serum albumin and the specific binding ofantigen were also monitored withthe QCM. Standardized radioimmunoassay was used to confirm theimmunoreaction and determinebinding parameters. The monolayer formation of the linker lipidsin the ternary system of phosphatidylcholine and cholesterol was, moreover, demonstrated by film balancestudies. The results demonstratethat the covalent coupling of Fab‘ fragments to linking groups embeddedin a phospholipid monolayermatrix is a promising approach to achieve a defined immobilization ofantibodies at the sensor surfacewith high antigen binding effeciency.
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