A comparative evaluation of molecular recognition by monolayers composed of synthetic receptors or oriented antibodies

Inger Vikholm-Lundin (Corresponding Author), Timo Pulli, Willem M. Albers, Kirsi Tappura

Research output: Contribution to journalArticleScientificpeer-review

11 Citations (Scopus)


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 languageEnglish
Pages (from-to)1036 - 1038
Number of pages3
JournalBiosensors & Bioelectronics
Issue number4
Publication statusPublished - 2008
MoE publication typeA1 Journal article-refereed



  • Immobilisation
  • Antibody Fab' fragment
  • Protein repellent polymer
  • Immunoassay
  • Surface plasmon resonance
  • Imprinted self-assembled monolayer

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