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Updated: Dec 8, 2025

Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms

Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms

Published on: April 17, 2017

Single injection microarray-based biosensor kinetics.

Ganeshram Krishnamoorthy¹, Edwin T Carlen¹, J Bianca Beusink¹

¹BIOS Lab-on-a-Chip Group, MESA+ Institute for Nanotechnology, University of Twente, P.O. Box 217, 7500, AE Enschede, The Netherlands. g.krishnamoorthy@utwente.nl.

Analytical Methods : Advancing Methods and Applications

|September 17, 2020

Summary

This summary is machine-generated.

A new surface plasmon resonance biosensor method estimates biomolecular binding affinity using a single analyte injection across multiple ligand densities. This approach simplifies affinity estimation, saving time and resources for various applications.

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Published on: September 23, 2013

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Published on: September 23, 2013

Area of Science:

Biochemistry
Analytical Chemistry
Biosensing Technology

Background:

Surface plasmon resonance (SPR) biosensors are crucial for measuring biomolecular interaction kinetics.
Traditional affinity estimation involves serial analyte injections and surface regeneration, which can be resource-intensive and damage sensitive samples.

Purpose of the Study:

To develop and validate an alternative method for estimating binding affinity using SPR.
To reduce the number of analyte injections and eliminate regeneration steps required for affinity determination.

Main Methods:

A novel approach using a single analyte concentration injected over a microarray of varying ligand densities.
Data analysis based on fitting sensorgram responses to appropriate model equations.
Demonstration with two specific biomolecular interactions: beta2 microglobulin/anti-beta2 microglobulin and human IgG/anti-human IgG Fab fragments.

Main Results:

The single analyte injection method yielded binding affinity constants (KD) comparable to the conventional method.
For beta2 microglobulin (β2M), KD was 1.52 ± 0.22 nM versus 1.48 ± 0.28 nM.
For human IgG (hIgG), KD was 12.5 ± 0.6 nM versus 12.6 ± 0.2 nM.

Conclusions:

The single analyte injection method provides accurate binding affinity measurements.
This simplified method is advantageous for applications with limited analyte, fragile ligands, or when analyzing multiple interactions simultaneously.