Immunoreactivity of adsorbed anti human chorionic gonadotropin studied with an optical waveguide interferometric sensor

Rene Heideman, R.P.H. Kooyman, Jan Greve

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Abstract

A study on the immunoreactivity of adsorbed αhCG molecules as a function of substrate hydrophobicity and protein coverage is presented. The experiments were performed with a planar waveguide interferometrical immunosensor. The substrate hydrophobicity and the antibody density were found to be of major importance for the immunoreactivity of the adsorbed antibodies. A combination of a hydrophobic (contact angle ≥80°) substrate and only a fraction (≈0·3) of a monolayer of antibodies gives the highest immunoreactivity. However, the immunoreaction affinity constant of the active antibodies is found to be essentially independent of the substrate hydrophobicity. The experimental results indicate that the orientation and not the conformation of the active antibodies on the substrate is dependent on the substrate hydrophobicity.
Original languageUndefined
Pages (from-to)33-43
Number of pages11
JournalBiosensors and bioelectronics
Volume9
Issue number1
DOIs
Publication statusPublished - 1994

Keywords

  • Coverage
  • adsorbed antibodies
  • interferometer
  • immunoreactivity
  • METIS-129463
  • hydrophobicity
  • IR-24662
  • Immunosensor
  • planar waveguides

Cite this

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title = "Immunoreactivity of adsorbed anti human chorionic gonadotropin studied with an optical waveguide interferometric sensor",
abstract = "A study on the immunoreactivity of adsorbed αhCG molecules as a function of substrate hydrophobicity and protein coverage is presented. The experiments were performed with a planar waveguide interferometrical immunosensor. The substrate hydrophobicity and the antibody density were found to be of major importance for the immunoreactivity of the adsorbed antibodies. A combination of a hydrophobic (contact angle ≥80°) substrate and only a fraction (≈0·3) of a monolayer of antibodies gives the highest immunoreactivity. However, the immunoreaction affinity constant of the active antibodies is found to be essentially independent of the substrate hydrophobicity. The experimental results indicate that the orientation and not the conformation of the active antibodies on the substrate is dependent on the substrate hydrophobicity.",
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author = "Rene Heideman and R.P.H. Kooyman and Jan Greve",
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Immunoreactivity of adsorbed anti human chorionic gonadotropin studied with an optical waveguide interferometric sensor. / Heideman, Rene; Kooyman, R.P.H.; Greve, Jan.

In: Biosensors and bioelectronics, Vol. 9, No. 1, 1994, p. 33-43.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Immunoreactivity of adsorbed anti human chorionic gonadotropin studied with an optical waveguide interferometric sensor

AU - Heideman, Rene

AU - Kooyman, R.P.H.

AU - Greve, Jan

PY - 1994

Y1 - 1994

N2 - A study on the immunoreactivity of adsorbed αhCG molecules as a function of substrate hydrophobicity and protein coverage is presented. The experiments were performed with a planar waveguide interferometrical immunosensor. The substrate hydrophobicity and the antibody density were found to be of major importance for the immunoreactivity of the adsorbed antibodies. A combination of a hydrophobic (contact angle ≥80°) substrate and only a fraction (≈0·3) of a monolayer of antibodies gives the highest immunoreactivity. However, the immunoreaction affinity constant of the active antibodies is found to be essentially independent of the substrate hydrophobicity. The experimental results indicate that the orientation and not the conformation of the active antibodies on the substrate is dependent on the substrate hydrophobicity.

AB - A study on the immunoreactivity of adsorbed αhCG molecules as a function of substrate hydrophobicity and protein coverage is presented. The experiments were performed with a planar waveguide interferometrical immunosensor. The substrate hydrophobicity and the antibody density were found to be of major importance for the immunoreactivity of the adsorbed antibodies. A combination of a hydrophobic (contact angle ≥80°) substrate and only a fraction (≈0·3) of a monolayer of antibodies gives the highest immunoreactivity. However, the immunoreaction affinity constant of the active antibodies is found to be essentially independent of the substrate hydrophobicity. The experimental results indicate that the orientation and not the conformation of the active antibodies on the substrate is dependent on the substrate hydrophobicity.

KW - Coverage

KW - adsorbed antibodies

KW - interferometer

KW - immunoreactivity

KW - METIS-129463

KW - hydrophobicity

KW - IR-24662

KW - Immunosensor

KW - planar waveguides

U2 - 10.1016/0956-5663(94)80013-8

DO - 10.1016/0956-5663(94)80013-8

M3 - Article

VL - 9

SP - 33

EP - 43

JO - Biosensors and bioelectronics

JF - Biosensors and bioelectronics

SN - 0956-5663

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