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An Optimized Protocol for Electrophoretic Mobility Shift Assay Using Infrared Fluorescent Dye-labeled Oligonucleotides
Published on: November 29, 2016
16.4K
Optical imaging of single-protein size, charge, mobility, and binding
Guangzhong Ma1, Zijian Wan1,2, Yunze Yang1
1Biodesign Center for Biosensors and Bioelectronics, Arizona State University, Tempe, AZ, 85287, USA.
Nature Communications
|September 22, 2020
Summary
This study introduces a novel method for analyzing single protein molecules, measuring size, charge, and mobility simultaneously. This breakthrough enables precise protein biomarker detection for biomedical research and diagnostics.
Area of Science:
- Biophysics
- Biochemistry
- Nanotechnology
Background:
- Protein analysis is crucial for biomedical research, disease diagnosis, and treatment.
- Current methods often require multiple techniques and cannot analyze single molecules comprehensively.
- Measuring protein size, charge, mobility, and antibody binding simultaneously at the single-molecule level remains a challenge.
Purpose of the Study:
- To develop a single technology capable of comprehensive protein analysis at the single-molecule level.
- To enable precision detection of protein biomarkers.
Main Methods:
- Tethering a single protein to a surface using a flexible polymer.
- Inducing protein oscillation with an electric field.
- Imaging oscillations using near-field optical imaging to determine protein properties.
Main Results:
- Successfully determined protein size, charge, and mobility using the developed method.
- Enabled measurement of antibody binding and protein conformation changes.
- Demonstrated comprehensive protein analysis at the single-molecule level.
Conclusions:
- The developed method offers a powerful new capability for detailed protein characterization.
- This technology facilitates precise protein biomarker detection, advancing biomedical research and diagnostics.
