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Monitoring Protein Adsorption with Solid-state Nanopores
Published on: December 2, 2011
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Single antibody-antigen interactions monitored via transient ionic current recording using nanopore sensors
Yi-Lun Ying1, Ru-Jia Yu1, Yong-Xu Hu1
1Key Laboratory for Advanced Materials, Shanghai Key Laboratory of Functional Materials Chemistry & School of Chemistry & Molecular Engineering, East China University of Science and Technology, 130 Meilong Road, Shanghai, 200237, P. R. China. ytlong@ecust.edu.cn.
Chemical Communications (Cambridge, England)
|July 20, 2017
Summary
This study monitored single alpha-fetoprotein (AFP) and antibody interactions using nanopore sensors. This method accurately determined antibody binding affinity at the single-molecule level without labeling.
Area of Science:
- Biophysics
- Immunology
- Nanotechnology
Background:
- Protein-protein interactions are crucial for antibody affinity assessment.
- Accurate measurement of binding kinetics is essential for diagnostic development.
Purpose of the Study:
- To monitor single alpha-fetoprotein (AFP) and antibody interactions.
- To determine the dissociation constant of AFP-antibody interactions at the single-molecule level.
- To evaluate antibody binding affinity without labeling.
Main Methods:
- Utilized antibody-functionalized nanopore sensors.
- Employed transient ionic current recording for interaction monitoring.
- Performed kinetic evaluation at the single-molecule level.
Main Results:
- Successfully monitored single AFP-antibody interactions.
- Determined the dissociation constant for the interaction.
- Demonstrated label-free kinetic analysis of antigen-antibody binding.
Conclusions:
- Nanopore sensors provide a powerful tool for single-molecule kinetic analysis of protein-protein interactions.
- This method offers new insights into antibody binding affinity.
- The technique has potential applications in developing advanced immunoassays for diagnostics.
