ArticleAnalytical biochemistry2020
Measuring the affinity of protein-protein interactions on a single-molecule level by mass photometry.
Article in Analytical biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Interferometric scattering microscopy supports real-time mass-resolved label-free single-molecule immunoassay.Scientific reports · 2026Article
- Molecule by Molecule Characterization of a Polymer Molecular Mass Distribution via Mass Photometry.Angewandte Chemie (International ed. in English) · 2026Article
- Deep Learning-Based Event Classification of Mass Photometry Data for Optimal Mass Measurement at the Single-Molecule Level.ACS nano · 2026Article
- Review
- Deciphering the dark side of histone ADP-ribosylation: what structural features of damaged nucleosome regulate the activities of PARP1 and PARP2.Nucleic acids research · 2025Article
- Engineering Protein-Peptide Interfaces via Combinatorial Mutagenesis and Mass Photometric Screening.Biomolecules · 2025Article
- High-Throughput Single-Particle Characterization of Aggregation Pathways and the Effects of Inhibitors for Large (Megadalton) Protein Oligomers.Analytical chemistry · 2024Article
- Heterogeneous distribution of kinesin-streptavidin complexes revealed by mass photometry.Soft matter · 2024Article
- Assembly of SARS-CoV-2 nucleocapsid protein with nucleic acid.Nucleic acids research · 2024Article
- Mono-UFMylation promotes misfolding-associated secretion of α-synuclein.Science advances · 2024Article
- Searching for EGF Fragments Recreating the Outer Sphere of the Growth Factor Involved in Receptor Interactions.International journal of molecular sciences · 2024Article
- Energy landscape of conformational changes for a single unmodified protein.Npj biosensing · 2024Article
- Assembly reactions of SARS-CoV-2 nucleocapsid protein with nucleic acid.bioRxiv : the preprint server for biology · 2023Article
- Mass photometry: A powerful tool for carbohydrates-proteins conjugation monitoring and glycoconjugates molecular mass determination.Glycoconjugate journal · 2023Article
- Identification of nurse shark VFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023Article
- Characterization of HZ0412a, a novel potent humanized anti-IL-6 receptor antibody that blocks IL-6R binding to gp130.Antibody therapeutics · 2023Article
- SAYSD1 senses UFMylated ribosome to safeguard co-translational protein translocation at the endoplasmic reticulum.Cell reports · 2023Article
- Elucidating the Stoichiometries of Host-Pathogen Protein Interactions with Mass Photometry.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Direct observation of the molecular mechanism underlying protein polymerization.Science advances · 2022Article
- The dimerization interface of initiator RctB governs chaperone and enhancer dependence of Vibrio cholerae chromosome 2 replication.Nucleic acids research · 2022Article
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2 authors.
Funding
Abstract
Measurements of biomolecular interactions are crucial to understand the mechanisms of the biological processes they facilitate. Bulk-based methods such as ITC and SPR provide important information on binding affinities, stoichiometry, and kinetics of interactions. However, the ensemble averaging approaches are not able to probe the intrinsic heterogeneity often displayed by biological systems. Interactions that involve cooperativity or result in the formation of multicomponent complexes pose additional experimental challenges. Single-molecule techniques have previously been applied to solve these problems. However, single-molecule experiments are often technically demanding and require labeling or immobilization of the molecules under study. A recently developed single-molecule method, mass photometry (MP), overcomes these limitations. Here we applied MP to measure the affinities of biomolecular interactions. We have demonstrated how MP allows the user to study multivalent complexes and quantify the affinities of different binding sites in a single measurement. Results obtained from this single-molecule technique have been validated by ITC and BLI. The quality and information content of the MP data, combined with simple and fast measurements and low sample consumption makes MP a new preferred method for measuring strong protein-protein interactions.
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