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Updated: Mar 9, 2026

Monitoring Protein Adsorption with Solid-state Nanopores

Monitoring Protein Adsorption with Solid-state Nanopores

Published on: December 2, 2011

Tiny protein detection using pressure through solid-state nanopores.

Ji Li¹, Rui Hu¹, Xiaoqing Li¹

¹State Key Laboratory for Mesoscopic Physics and Electron Microscopy Laboratory, School of Physics, Peking University, Beijing, P. R. China.

Electrophoresis

|January 11, 2017

Summary

This summary is machine-generated.

We introduce pressure to solid-state nanopore detection, enabling the sensing of tiny proteins (<6.5 kDa) with enhanced capture rates and temporal resolution for improved biomolecule analysis.

Keywords:

Nanopore Pressure Pretein Temporal resolution Translocation

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Published on: October 26, 2016

Area of Science:

Biophysics
Nanotechnology
Biochemistry

Background:

Solid-state nanopores are effective for protein detection.
Small proteins (<35 kDa) translocate too rapidly for standard detection.
Low temporal resolution limits current nanopore techniques.

Purpose of the Study:

To enhance the detection of small proteins using solid-state nanopores.
To improve the temporal resolution for detecting fast-translocating biomolecules.
To develop a method for studying tiny protein dynamics in ionic solutions.

Main Methods:

Introduction of pressure as a driving force in nanopore experiments.
Combined use of pressure-derived force and voltage bias for biomolecule manipulation.
Fine-tuning pressure and voltage to optimize capture rate and temporal resolution.
Modulating driving pressure and retard voltage to determine equilibrium ranges for protein movement.

Main Results:

Enabled detection of very tiny proteins (MW < 6.5 kDa).
Achieved a five-fold enhanced capture rate for Aprotinin compared to voltage-driven methods.
Improved temporal resolution for Aprotinin detection by reducing effective driving force.
Provided a method to locate equilibrium ranges for Bovine Serum Albumin (BSA) movement.

Conclusions:

Pressure-assisted nanopore sensing significantly enhances detection of small proteins.
This technique offers improved temporal resolution for studying fast molecular events.
The study provides a novel platform for analyzing small proteins and other minute biomolecules.