ArticleAnalytical chemistry2014
Analysis of protein interactions with picomolar binding affinity by fluorescence-detected sedimentation velocity.
Article in Analytical chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- Analytical Ultracentrifugation in Aotearoa: A Brief History of the Technique and its Place Among Other Tools Used to Investigate Biomolecular Interactions.Journal of the Royal Society of New Zealand · 2026Review
- Analysis of Giant-Shell CdSe/CdS Quantum Dots via Analytical Ultracentrifugation Combined with Spectrally Resolved Photoluminescence.Small methods · 2026Article
- Analytical Ultracentrifugation for Studying the Oligomeric State and Protein-Protein Interactions of Membrane Transporters.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Article
- Molecularly Imprinted Polymer Sensor Empowered by Bound States in the Continuum for Selective Trace-Detection of TGF-beta.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Development of an advanced multiwavelength emission detector for the analytical ultracentrifuge.Nanoscale advances · 2024Article
- Soluble Frizzled-related proteins promote exosome-mediated Wnt re-secretion.Communications biology · 2024Article
- An automated interface for sedimentation velocity analysis in SEDFIT.PLoS computational biology · 2023Article
- On the utility of microfluidic systems to study protein interactions: advantages, challenges, and applications.European biophysics journal : EBJ · 2023Review
- An automated interface for sedimentation velocity analysis in SEDFIT.bioRxiv : the preprint server for biology · 2023Article
- Biophysical Approaches for the Characterization of Protein-Metabolite Interactions.Methods in molecular biology (Clifton, N.J.) · 2023Review
- Label-free methods for opticalPhysical chemistry chemical physics : PCCP · 2021Review
- Multi-wavelength analytical ultracentrifugation as a tool to characterise protein-DNA interactions in solution.European biophysics journal : EBJ · 2020Article
- Analytical Ultracentrifugation (AUC): An Overview of the Application of Fluorescence and Absorbance AUC to the Study of Biological Macromolecules.Current protocols in molecular biology · 2020Article
- Quantitative Analysis of Protein Self-Association by Sedimentation Velocity.Current protocols in protein science · 2020Article
- The structure of the extracellular domains of human interleukin 11α receptor reveals mechanisms of cytokine engagement.The Journal of biological chemistry · 2020Article
- In Vitro Analytical Approaches to Study Plant Ligand-Receptor Interactions.Plant physiology · 2020Review
- Efficient data acquisition with three-channel centerpieces in sedimentation velocity.Analytical biochemistry · 2019Article
- Nucleic acid-induced dimerization of HIV-1 Gag protein.The Journal of biological chemistry · 2019Article
- Solution-Based Determination of Dissociation Constants for the Binding of Aβ42 to Antibodies.ChemistryOpen · 2019Article
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3 authors.
Funding
Abstract
The study of high-affinity protein interactions with equilibrium dissociation constants (KD) in the picomolar range is of significant interest in many fields, but the characterization of stoichiometry and free energy of such high-affinity binding can be far from trivial. Analytical ultracentrifugation has long been considered a gold standard in the study of protein interactions but is typically applied to systems with micromolar KD. Here we present a new approach for the study of high-affinity interactions using fluorescence detected sedimentation velocity analytical ultracentrifugation (FDS-SV). Taking full advantage of the large data sets in FDS-SV by direct boundary modeling with sedimentation coefficient distributions c(s), we demonstrate detection and hydrodynamic resolution of protein complexes at low picomolar concentrations. We show how this permits the characterization of the antibody-antigen interactions with low picomolar binding constants, 2 orders of magnitude lower than previously achieved. The strongly size-dependent separation and quantitation by concentration, size, and shape of free and complex species in free solution by FDS-SV has significant potential for studying high-affinity multistep and multicomponent protein assemblies.
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