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Abstract: Recombinant anti-morphine Fab' fragments have been immobilised on gold by covalent attachment through the free thiol groups of the fragment. The antibody fragments were intercalated with a non-ionic hydrophilic polymer in order to suppress non-specific binding of interfering substances. The antibodies are oriented on the surface due to the thiol groups of the antibody and the layer shows a high response to antigen. Non-specific binding of bovine serum albumin is moreover very low because of the repellent polymer. Synthetic receptors composed of an imprinted self-assembled monolayer made from lipoates and the template, morphine, exhibit the same binding response to the antigen, morphine as the site-specific oriented antibody monolayer. A similar binding curve could be obtained as that for binding of morphine to an antibody Fab' fragment/polymer layer - indicating that synthetic receptors produced are comparable to those of antibody layers. Concentrations down to 0.1áng/ml have been measured with surface plasmon resonance
Template and target information: morphine
Author keywords: immobilisation, Antibody Fab' fragment, Protein repellent polymer, immunoassay, surface plasmon resonance, Imprinted self-assembled monolayer