ArticleScientific reports2026
Interferometric scattering microscopy supports real-time mass-resolved label-free single-molecule immunoassay.
Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Interferometric scattering microscopy supports real-time mass-resolved label-free single-molecule immunoassay.Scientific reports · 2026Article
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Authors and funding
6 authors.
Funding
Abstract
Protein-protein interactions govern the biomolecular logic of immunity, signalling, and disease. Elementary rates of association, dissociation, and inhibition underpin our understanding of life processes and remain a limiting factor at the frontier of therapeutic discovery. Yet existing assays infer these processes indirectly through ensemble-averaged signals or labels that obscure native dynamics. Here, we introduce a label-free, real-time, mass-resolved single-molecule immunoassay based on interferometric scattering microscopy (iSCAT) that directly observes individual protein-protein binding events in complex biological samples. By detecting light scattered from single proteins as they bind to an antibody-functionalized surface, we resolve discrete antibody-antigen interactions with single-molecule sensitivity and molecular-weight discrimination. Using IgM as a model system, we demonstrate real-time detection of individual binding events, with measured association rates that scale linearly with concentration over three orders of magnitude. Direct counts of IgM binding events in human serum yield quantitative concentrations that agree with bulk measurements obtained by enzyme-linked immunosorbent assay (ELISA). Spatially resolved tracking of individual binding and unbinding events captures the elementary dissociation rate constant, [Formula: see text], from the distribution of single-molecule dwell times. This bioaffinity iSCAT platform unifies molecular specificity, label-free detection, real-time kinetics, and mass-resolved single-molecule sensitivity, to offer a general framework for quantitative, single-molecule immunoassay.
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