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

10 Citations (Scopus)

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 languageEnglish
Pages (from-to)1036 - 1038
Number of pages3
JournalBiosensors & Bioelectronics
Volume24
Issue number4
DOIs
Publication statusPublished - 2008
MoE publication typeA1 Journal article-refereed

Fingerprint

Artificial Receptors
Molecular recognition
Antibodies
Morphine
Monolayers
Immunoglobulin Fragments
Polymers
Immunoglobulin Fab Fragments
Sulfhydryl Compounds
Antigens
Surface Plasmon Resonance
Bovine Serum Albumin
Gold
Surface plasmon resonance
Self assembled monolayers

Keywords

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

Cite this

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title = "A comparative evaluation of molecular recognition by monolayers composed of synthetic receptors or oriented antibodies",
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.",
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A comparative evaluation of molecular recognition by monolayers composed of synthetic receptors or oriented antibodies. / Vikholm-Lundin, Inger (Corresponding Author); Pulli, Timo; Albers, Willem M.; Tappura, Kirsi.

In: Biosensors & Bioelectronics, Vol. 24, No. 4, 2008, p. 1036 - 1038.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - A comparative evaluation of molecular recognition by monolayers composed of synthetic receptors or oriented antibodies

AU - Vikholm-Lundin, Inger

AU - Pulli, Timo

AU - Albers, Willem M.

AU - Tappura, Kirsi

PY - 2008

Y1 - 2008

N2 - 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.

AB - 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.

KW - Immobilisation

KW - Antibody Fab' fragment

KW - Protein repellent polymer

KW - Immunoassay

KW - Surface plasmon resonance

KW - Imprinted self-assembled monolayer

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JO - Biosensors & Bioelectronics

JF - Biosensors & Bioelectronics

SN - 0956-5663

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