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Nanopore-Based Protein Deceleration and Sensing Using Graphene/Si3N4 Dual Membrane Cavity.
Yubin Cao1, Junzhou He1, Wei Si1
1Jiangsu Key Laboratory for Design and Manufacturing of Precision Medicine Equipment, School of Mechanical Engineering, Southeast University, Nanjing, China.
Advanced Science (Weinheim, Baden-Wurttemberg, Germany)
|June 11, 2026
Summary
Researchers developed a novel graphene/silicon nitride (Si3N4) dual membrane system to improve nanopore protein sequencing. This system effectively slows peptide translocation, enhancing accuracy and paving the way for high-throughput proteomics.
Area of Science:
- Nanotechnology
- Proteomics
- Biophysics
Background:
- Nanopore sequencing offers rapid, portable protein analysis but requires improved accuracy.
- Controlling protein translocation speed is crucial for effective nanopore sensing.
- Current methods face challenges in balancing speed, accuracy, and signal resolution.
Purpose of the Study:
- To enhance the accuracy and efficiency of single-molecule protein sequencing using nanopores.
- To investigate methods for controlling peptide translocation rates within nanopores.
- To develop a novel dual membrane cavity system for improved nanopore sensing.
Main Methods:
- Designed a graphene/silicon nitride (Si3N4) dual membrane cavity system.
- Utilized charge regulation and cavity structure engineering to modulate peptide translocation.
- Investigated the impact of a Si3N4 toroidal cavity on peptide residence time and signal resolution.
Main Results:
- The Si3N4 toroidal cavity significantly reduced peptide translocation rates.
- Physical steric hindrance and enhanced van der Waals adsorption were key mechanisms.
- Prolonged peptide residence time and maintained excellent signal resolution were achieved.
Conclusions:
- The developed dual membrane system offers a promising approach for high-resolution, high-throughput protein sequencing.
- Controlling translocation rates via cavity engineering is vital for advancing nanopore proteomics.
- This work addresses bandwidth limitations in single-molecule protein analysis.
