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Tracking single-molecule ferritin reassembly and disassembly using polymer-coated nanopores
Mahya Assadipapari1, Alireza Soleimanian2, Max Adam1
1Advanced Optics and Photonics Laboratory, Department of Engineering, School of Science and Technology, Nottingham Trent University, Nottingham, UK. cuifeng.ying@ntu.ac.uk.
Nanoscale
|December 16, 2025
Summary
Single-molecule analysis of ferritin reassembly and disassembly was achieved using polymer-coated nanopores. This method identified intermediate protein subunits, advancing nanomedicine applications.
Area of Science:
- Biochemistry
- Nanotechnology
- Materials Science
Background:
- Ferritin, an iron-storing protein, is a promising nanomedicine candidate due to its disassembly/reassembly properties for drug delivery.
- Monitoring these dynamic processes at the single-molecule level is crucial but challenging due to nanopore clogging.
Purpose of the Study:
- To develop a method for real-time, single-molecule monitoring of ferritin reassembly and disassembly.
- To characterize intermediate ferritin subunits and reaction dynamics.
Main Methods:
- Utilized polymer-coated solid-state nanopores for continuous, long-term ion current recording of ferritin fragment translocations.
- Applied individual event analysis to determine fragment volume and shape from translocation data.
Main Results:
- Achieved clog-free recording of ferritin fragment translocations for up to 1 hour.
- Identified intermediate ferritin subunits (4-, 6-, 8-, 10-, 12-, and 16-mers) using single translocation event analysis.
- Demonstrated that individual event analysis surpasses population-based analysis in discriminating subunits.
Conclusions:
- Polymer-coated nanopores enable real-time, single-molecule tracking of protein dynamics like ferritin reassembly and disassembly.
- This approach allows for the characterization of individual protein components within mixtures and their reaction kinetics.
- The developed method holds significant potential for advancing nanomedicine and protein analysis.
