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Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance (SPR)

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Comparative Real-Time Kinetics of Ligand-Receptor Interactions Using Immobilization-Based Sensing Readouts.

Yazheng Wang^1,2, Yalun Wu^3,4, Lauren A Mayse^1,5

¹Department of Physics, Syracuse University, 201 Physics Building, Syracuse, New York, New York 13244, United States.

Analytical Chemistry

|July 9, 2026

Summary

This summary is machine-generated.

Quantitative analysis of early ligand-EGFR binding kinetics reveals complex interactions. Immobilization techniques influence results, and glycosylation significantly impacts receptor affinity.

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Real-time Monitoring of Ligand-receptor Interactions with Fluorescence Resonance Energy Transfer

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Published on: August 20, 2012

Area of Science:

Biochemistry
Molecular Biology
Cell Signaling

Background:

Receptor tyrosine kinase (RTK) and growth factor ligand interactions are vital for cellular communication.
Early kinetic events in these signaling pathways are not fully quantified.
Understanding ligand-receptor binding dynamics is crucial for deciphering cell signaling.

Purpose of the Study:

To quantitatively analyze the real-time binding kinetics of high-affinity ligands with epidermal growth factor receptor (EGFR) isoforms.
To investigate the influence of immobilization-based sensing techniques on kinetic and affinity measurements.
To determine the role of glycosylation in ligand-EGFR interactions.

Main Methods:

Employed biolayer interferometry (BLI) and surface plasmon resonance (SPR) for real-time binding kinetics analysis.
Utilized high-affinity ligands and the full extracellular domain of various EGFR isoforms.
Investigated interactions with both native and deglycosylated EGFR variants.

Main Results:

Both BLI and SPR revealed complex binding kinetics with fast and slow dissociation phases, indicating two binding substates in ligand-EGFR interactions.
Sensing technique choice significantly impacted kinetic parameters and relative ligand-EGFR interaction strengths.
Glycan side chains at N151 did not affect interactions, but extensive deglycosylation markedly reduced ligand binding affinity.

Conclusions:

Ligand-EGFR interactions exhibit complex kinetics, characterized by multiple binding substates.
Immobilization strategies critically influence the quantitative assessment of these interactions.
Post-translational modifications, specifically glycosylation, play a significant role in modulating ligand-receptor affinity.