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 0.1 ng/ml have been measured with surface plasmon resonance.
| Original language | English |
|---|---|
| Pages (from-to) | 1036-1038 |
| Journal | Biosensors & Bioelectronics |
| Volume | 24 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 2008 |
| MoE publication type | A1 Journal article-refereed |
Keywords
- Immobilisation
- Antibody Fab' fragment
- Protein repellent polymer
- Immunoassay
- Surface plasmon resonance
- Imprinted self-assembled monolayer