ArticleAnalytical chemistry2023
Multiplexed Protein Detection and Parallel Binding Kinetics Analysis with Label-Free Digital Single-Molecule Counting.
Article in Analytical chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 5 citations in OpenAlex.
- Meta-amplified dark-field interferometric scattering microscopy.Nature communications · 2026Article
- In Situ and Label-Free Quantification of Membrane Protein-Ligand Interactions Using Optical Imaging Techniques: A Review.Biosensors · 2024Review
- Dielectric Surface-Based Biosensors for Enhanced Detection of Biomolecular Interactions: Advances and Applications.Biosensors · 2024Review
- Label-Free Optical Imaging of Nanoscale Single Entities.ACS sensors · 2024Review
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Multiplexed protein detection is critical for improving the drug and biomarker screening efficiency. Here, we show that multiplexed protein detection and parallel protein interaction analysis can be realized by evanescent scattering microscopy (ESM). ESM enables binding kinetics measurement with label-free digital single-molecule counting. We implemented an automatic single-molecule counting strategy with high temporal resolution to precisely determine the binding time, which improves the counting efficiency and accuracy. We show that digital single-molecule counting can recognize proteins with different molecular weights, thus making it possible to monitor the protein binding processes in the solution by real-time tracking of the numbers of free and bound proteins landing on the sensor surface. Furthermore, we show that this strategy can simultaneously analyze the kinetics of two different protein interaction processes on the surface and in the solution. This work may pave a way to investigate complicated protein interactions, such as the competition of biomarker-antibody binding in biofluids with biomarker-protein binding on the cellular membrane.
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