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Updated: May 27, 2026

Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms
Published on: April 17, 2017
Effect of antibody modifications on its biomolecular binding as determined by surface plasmon resonance
1Centre for Bioanalytical Sciences, National Centre for Sensor Research, Dublin City University, Dublin 9, Ireland. sandeep.vashist@yahoo.com
Abstract:
A surface plasmon resonance (SPR)-based procedure was developed to determine the effect of antibody modifications on its biomolecular binding behavior. Mouse immunoglobulin G (IgG) was immobilized on a protein A-functionalized gold-coated SPR chip. Goat anti-mouse IgG and its various commercially available modifications (i.e., conjugated with atto 550, atto 647, tetramethylrhodamine isothiocyanate [TRITC], horseradish peroxidase [HRP], or biotin) were employed in exactly the same concentration for the detection of mouse IgG. The various modifications of goat anti-mouse IgG decreased its biomolecular binding to mouse IgG in the order of unmodified>HRP-labeled>atto 550-labeled>biotinylated>TRITC-labeled>atto 647-labeled.
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