Journal
ACS SENSORS
Volume 6, Issue 3, Pages 1357-1366Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acssensors.0c02729
Keywords
surface plasmon resonance; plasmonic scattering imaging; single proteins; molecule interaction; binding kinetics
Funding
- National Institutes of Health [R01GM107165, R33CA235294]
- NSF program [NNCI-ECCS-1542160]
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Single-molecule-based measurement can distinguish specific and nonspecific binding processes by quantifying the mass and binding dynamics of individual-bound analyte molecules, providing a convenient solution for high-resolution imaging on widely used prism-coupled SPR systems.
Measuring molecular binding is critical for understanding molecular-scale biological processes and screening drugs. Label-free detection technologies, such as surface plasmon resonance (SPR), have been developed for analyzing analytes in their natural forms. However, the specificity of these methods is solely relying on surface chemistry and has often nonspecific binding issues when working with samples in complex media. Herein, we show that single-molecule-based measurement can distinct specific and nonspecific binding processes by quantifying the mass and binding dynamics of individual-bound analyte molecules, thus allowing the binding kinetic analysis in complex media such as serum. In addition, this single-molecule imaging is realized in a commonly used Kretschmann prism-coupled SPR system, thus providing a convenient solution to realize high-resolution imaging on widely used prism-coupled SPR systems.
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