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 0.1 ng/ml have been measured with surface plasmon resonance.
- Antibody Fab' fragment
- Protein repellent polymer
- Surface plasmon resonance
- Imprinted self-assembled monolayer
Vikholm-Lundin, I., Pulli, T., Albers, W. M., & Tappura, K. (2008). A comparative evaluation of molecular recognition by monolayers composed of synthetic receptors or oriented antibodies. Biosensors & Bioelectronics, 24(4), 1036 - 1038. https://doi.org/10.1016/j.bios.2008.06.049