ArticleAngewandte Chemie (International ed. in English)2020
Quantifying Protein-Protein Interactions by Molecular Counting with Mass Photometry.
Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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Who cites it
84 citing papers in PubMed.
- Immunoglobulin binding protein (BiP) forms two types of dimers.Protein science : a publication of the Protein Society · 2026Article
- Reconstitution of antiviral Dicer activity in vitro reveals distinct contributions of RDE-4 dsRNA-binding motifs.RNA (New York, N.Y.) · 2026Article
- A metabolite-bridged complex between SerRS and SIRT2 couples NAD⁺ metabolism to translation control.Nature communications · 2026Article
- Best practice mass photometry: a guide to optimal single-molecule mass measurement.Nature protocols · 2026Review
- Structural basis for the mechanism and stability of the EEPD1 5' endonuclease.The Journal of biological chemistry · 2026Article
- Biophysical Sensing Tools in Drug Discovery: Integrating Kinetics, Thermodynamics, Cellular Target Engagement and Structure.Sensors (Basel, Switzerland) · 2026Review
- Distinct transport cycle and lipid regulation of a MgResearch square · 2026Article
- Site-Specific Glycan Conjugation Improves Stability and Efficacy of an Antibody-Drug Conjugates Bearing DXd as a Cytotoxic Payload.ACS omega · 2026Article
- The filamentous ultrastructure of the PopZ condensate is required for its cellular function.Nature structural & molecular biology · 2026Article
- Deep Learning-Based Event Classification of Mass Photometry Data for Optimal Mass Measurement at the Single-Molecule Level.ACS nano · 2026Article
- Reconstitution of antiviral Dicer activity in vitro reveals distinct contributions of RDE-4 dsRNA-binding motifs.bioRxiv : the preprint server for biology · 2025Article
- Cooperativity inInternational journal of molecular sciences · 2025Article
- Quantitative analysis of inhibitor-induced assembly disruption in human UDP-GlcNAc 2-epimerase using mass photometry.Protein science : a publication of the Protein Society · 2025Article
- Engineering Protein-Peptide Interfaces via Combinatorial Mutagenesis and Mass Photometric Screening.Biomolecules · 2025Article
- NIPBL and STAG1 enable loop extrusion by providing differential DNA-cohesin affinity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Cryo-EM led analysis of open and closed conformations of Chagas vaccine candidate TcPOP.Nature communications · 2025Article
- Characterization of intact mRNA-based therapeutics by charge detection mass spectrometry and mass photometry.Molecular therapy. Methods & clinical development · 2025Article
- Enhanced Interferometric Imaging by Rotating Coherent Scattering Microscopy.ACS photonics · 2025Article
- Unexpected enzymatic function of an ancient nucleic acid-binding fold.Nucleic acids research · 2025Article
- Biolayer interferometry for measuring the kinetics of protein-protein interactions and nanobody binding.Nature protocols · 2025Review
24 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interactions between biomolecules control the processes of life in health and their malfunction in disease, making their characterization and quantification essential. Immobilization- and label-free analytical techniques are desirable because of their simplicity and minimal invasiveness, but they struggle with quantifying tight interactions. Here, we show that mass photometry can accurately count, distinguish by molecular mass, and thereby reveal the relative abundances of different unlabelled biomolecules and their complexes in mixtures at the single-molecule level. These measurements determine binding affinities over four orders of magnitude at equilibrium for both simple and complex stoichiometries within minutes, as well as the associated kinetics. These results introduce mass photometry as a rapid, simple and label-free method for studying sub-micromolar binding affinities, with potential for extension towards a universal approach for characterizing complex biomolecular interactions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.