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Updated: Feb 6, 2026
08:51
Monitoring Protein Adsorption with Solid-state Nanopores
Published on: December 2, 2011
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Protein Motion and Configurations in a Form-Fitting Nanopore: Avidin in ClyA
Bo Lu1, Chris Stokes2, Monifa Fahie3
1Department of Physics, Harvard University, Cambridge, Massachusetts.
Biophysical Journal
|August 21, 2018
Summary
We reveal avidin protein dynamics within a cytolysin A nanopore using electrical signals. A stable avidin configuration was identified for reliable trapping, useful for biotinylated protein studies.
Area of Science:
- Biophysics
- Nanotechnology
- Molecular Biology
Background:
- Understanding protein dynamics at the single-molecule level is crucial for advancing molecular biology and nanotechnology.
- Avidin-biotin interactions are widely used in biochemical assays and diagnostics.
- Nanopores offer a unique platform for probing single-molecule behavior.
Purpose of the Study:
- To investigate the molecular dynamics and conformational states of avidin protein trapped in a voltage-biased cytolysin A nanopore.
- To develop and apply a novel analysis method for single-molecule electrical conductance data.
- To identify stable configurations of avidin within the nanopore for potential applications in protein sensing.
Main Methods:
- Time-resolved single-molecule electrical conductance measurements.
- Utilizing a voltage-biased cytolysin A nanopore system.
- Development of a new data analysis method for visualizing molecular-scale processes.
Main Results:
- Avidin exhibits rich conductance spectra within the nanopore, indicating transient and stable configurations.
- A reliable, long-lasting, low-noise avidin configuration was identified and characterized.
- The system demonstrated sensitivity to biotin attachment to avidin captured in the pore.
Conclusions:
- The cytolysin A nanopore system provides detailed insights into avidin molecular dynamics.
- A stable avidin trapping configuration can be achieved, with potential for controlled protein manipulation.
- This approach may enable single-molecule studies of biotinylated proteins using avidin as a transporter.
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