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Dissociation constant measurement using combination tapered fiber-optic biosensor (CTFOB) dip-probes
1Department of Physics, University of Alabama at Birmingham, Birmingham, AL 35294.
Proceedings of Spie--The International Society for Optical Engineering
|September 28, 2011
Summary
This study introduces a new method using a fiber-optic biosensor to measure antibody-antigen binding strength. The novel approach accurately determined the dissociation constant for human Interleukin-6 (IL-6) and its antibody.
Area of Science:
- Biomedical Engineering
- Immunotechnology
- Analytical Chemistry
Background:
- Accurate measurement of antibody-antigen interactions is crucial for diagnostics and therapeutics.
- Existing methods for determining dissociation constants can be complex or require specialized equipment.
Purpose of the Study:
- To develop and validate a novel, sensitive method for measuring antibody-antigen dissociation constants (kD).
- To utilize a fiber-optic biosensor for real-time analysis of biomolecular interactions.
Main Methods:
- Employed an evanescent wave-based combination tapered fiber-optic biosensor (CTFOB) dip-probe.
- Utilized a sandwich immunoassay to generate a fluorescence signal proportional to antigen-antibody binding.
- Measured the dissociation constant for human Interleukin-6 (IL-6) and anti-IL-6 antibodies using a portable CCD spectrometer.
Main Results:
- Successfully measured the dissociation constant (kD) for the interaction between human Interleukin-6 (IL-6) and anti-IL-6 antibodies.
- The measured dissociation constant was determined to be 588 ±19 pM at room temperature.
Conclusions:
- The developed CTFOB method provides a sensitive and accurate approach for quantifying antibody-antigen binding affinity.
- This technique holds promise for applications in diagnostics, drug development, and understanding immune responses.
