TY - JOUR
T1 - Optical imaging of single-protein size, charge, mobility, and binding
AU - Ma, Guangzhong
AU - Wan, Zijian
AU - Yang, Yunze
AU - Zhang, Pengfei
AU - Wang, Shaopeng
AU - Tao, Nongjian
N1 - Funding Information:
This paper is dedicated to the memory of N.T. (1963–2020). The present work was financially supported by Gordon and Betty Moore Foundation, and National Institute of Health (R44GM126720). We thank Dr. Dong-Kyun Seo and Shaojiang Chen at Arizona State University for their help with dynamic light scattering measurement, and Dr. Shuoxing Jiang and Xu Zhou for help with AFM.
Publisher Copyright:
© 2020, The Author(s).
PY - 2020/12/1
Y1 - 2020/12/1
N2 - Detection and identification of proteins are typically achieved by analyzing protein size, charge, mobility and binding to antibodies, which are critical for biomedical research and disease diagnosis and treatment. Despite the importance, measuring these quantities with one technology and at the single-molecule level has not been possible. Here we tether a protein to a surface with a flexible polymer, drive it into oscillation with an electric field, and image the oscillation with a near field optical imaging method, from which we determine the size, charge, and mobility of the protein. We also measure antibody binding and conformation changes in the protein. The work demonstrates a capability for comprehensive protein analysis and precision protein biomarker detection at the single molecule level.
AB - Detection and identification of proteins are typically achieved by analyzing protein size, charge, mobility and binding to antibodies, which are critical for biomedical research and disease diagnosis and treatment. Despite the importance, measuring these quantities with one technology and at the single-molecule level has not been possible. Here we tether a protein to a surface with a flexible polymer, drive it into oscillation with an electric field, and image the oscillation with a near field optical imaging method, from which we determine the size, charge, and mobility of the protein. We also measure antibody binding and conformation changes in the protein. The work demonstrates a capability for comprehensive protein analysis and precision protein biomarker detection at the single molecule level.
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U2 - 10.1038/s41467-020-18547-w
DO - 10.1038/s41467-020-18547-w
M3 - Article
C2 - 32958747
AN - SCOPUS:85091276247
SN - 2041-1723
VL - 11
JO - Nature communications
JF - Nature communications
IS - 1
M1 - 4768
ER -