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Chen YT, Jamison AC, Lee TR, et al. Quantitatively Resolving Ligand-Receptor Bonds on Cell Surfaces Using Force-Induced Remnant Magnetization Spectroscopy. ACS Cent Sci. 2016;2(2):75-9doi: 10.1021/acscentsci.5b00325.
Chen, Y. T., Jamison, A. C., Lee, T. R., & Xu, S. (2016). Quantitatively Resolving Ligand-Receptor Bonds on Cell Surfaces Using Force-Induced Remnant Magnetization Spectroscopy. ACS central science, 2(2), 75-9. https://doi.org/10.1021/acscentsci.5b00325
Chen, Yi-Ting, et al. "Quantitatively Resolving Ligand-Receptor Bonds on Cell Surfaces Using Force-Induced Remnant Magnetization Spectroscopy." ACS central science vol. 2,2 (2016): 75-9. doi: https://doi.org/10.1021/acscentsci.5b00325
Chen YT, Jamison AC, Lee TR, Xu S. Quantitatively Resolving Ligand-Receptor Bonds on Cell Surfaces Using Force-Induced Remnant Magnetization Spectroscopy. ACS Cent Sci. 2016 Feb 24;2(2):75-9. doi: 10.1021/acscentsci.5b00325. Epub 2016 Feb 05. PMID: 27163031; PMCID: PMC4827459.
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ACS Cent Sci. 2016 Feb 24;2(2):75-9. doi: 10.1021/acscentsci.5b00325. Epub 2016 Feb 05.

Quantitatively Resolving Ligand-Receptor Bonds on Cell Surfaces Using Force-Induced Remnant Magnetization Spectroscopy.

ACS central science

Yi-Ting Chen, Andrew C Jamison, T Randall Lee, Shoujun Xu

Affiliations

  1. Department of Chemistry, University of Houston , Houston, Texas 77204, United States.

PMID: 27163031 PMCID: PMC4827459 DOI: 10.1021/acscentsci.5b00325

Abstract

Molecule-specific noncovalent bonding on cell surfaces is the foundation for cellular recognition and functioning. A major challenge in probing these bonds is to resolve the specific bonds quantitatively and efficiently from the nonspecific interactions in a complex environment. Using force-induced remnant magnetization spectroscopy (FIRMS), we were able to resolve quantitatively three different interactions for magnetic beads bearing anti-CD4 antibodies with CD4(+) T cell surfaces based upon their binding forces. The binding force of the CD4 antibody-antigen bonds was determined to be 75 ± 3 pN. For comparison, the same bonds were also studied on a functionalized substrate surface, and the binding force was determined to be 90 ± 6 pN. The 15 pN difference revealed by high-resolution FIRMS illustrates the significant impact of the bonding environment. Because the force difference was unaffected by the cell number or the receptor density on the substrate, we attributed it to the possible conformational or local environmental differences of the CD4 antigens between the cell surface and substrate surface. Our results show that the high force resolution and detection efficiency afforded by FIRMS are valuable for studying protein-protein interactions on cell surfaces.

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