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Updated: Jul 7, 2026

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Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms
Published on: April 17, 2017
A concentration dependent study of acoustic plate mode immunosensor response using antigen/antibody systems with
1Angewandte Physikalische Chemie, Universität Heidelberg, 69120 Heidelberg, Germany. Reiner.Dahint@urz.uni-heidelberg
Summary
Acoustic plate mode sensors effectively monitor immunochemical reactions, achieving a detection limit of 0.5 microg/ml. This technology demonstrates high antibody activity, crucial for sensitive antigen concentration detection.
Area of Science:
- Biosensing
- Immunochemistry
- Surface Science
Background:
- Acoustic plate mode sensors offer label-free detection of biomolecular interactions.
- Monitoring immunochemical reactions requires sensitive and quantitative methods.
Purpose of the Study:
- To evaluate acoustic plate mode sensors for monitoring immunochemical reactions.
- To determine the sensor's detection limit and binding constants for antigen/antibody systems.
- To assess the activity of immobilized antibodies on the sensor surface.
Main Methods:
- Covalent immobilization of antibodies onto a gold-coated sensing surface using mercaptoethanol, aminosilane, and glutaraldehyde.
- Utilizing two distinct antigen/antibody model systems with varying binding affinities.
- Operating the sensor at approximately 150 MHz to measure binding events.
Main Results:
- A detection limit of approximately 0.5 microg/ml was achieved for both model systems.
- Binding constants were found to be approximately 1.10(8) 1/mole, comparable to homogeneous immunoassays.
- Approximately 70% of the immobilized antibodies were found to be active.
Conclusions:
- Acoustic plate mode sensors are suitable for quantitative monitoring of immunochemical reactions.
- The sensor demonstrates high sensitivity and reliable binding constant determination.
- The immobilization strategy results in a high percentage of active antibodies.
Related Concept Videos
Enzyme-Linked Immunosorbent Assay
In 1971, Peter Perlman and Eva Engvall developed an Enzyme-linked immunosorbent assay (ELISA or EIA). ELISA differs from western blot in that the assays are conducted in microtiter plates or in vivo rather than on an absorbent membrane.
There are many different types of ELISAs, but they all involve an antibody molecule whose constant region binds an enzyme, leaving the variable region free to bind its specific antigen. Enzyme-substrate reaction allows the antigen to be visualized or quantified.
There are many different types of ELISAs, but they all involve an antibody molecule whose constant region binds an enzyme, leaving the variable region free to bind its specific antigen. Enzyme-substrate reaction allows the antigen to be visualized or quantified.
Affinity and Avidity
Overview

