ArticleMethods in enzymology2016
Cell-Binding Assays for Determining the Affinity of Protein-Protein Interactions: Technologies and Considerations.
Article in Methods in enzymology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
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- Deep Prior Framework: integrating functional specificity with general plausibility for targeted protein evolution.Briefings in bioinformatics · 2026Article
- Real-Time Binding Kinetics of Small Molecules to CA IX in Live Suspension Cells Using SPR Microscopy.ACS medicinal chemistry letters · 2026Article
- Advancements in Targeted Radiopharmaceuticals: Innovations in Diagnosis and Therapy for Enhanced Cancer Management.Chembiochem : a European journal of chemical biology · 2026Review
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- Probing the Dynamic Strength of Biomolecular Interactions with Single-Cell Centrifugation.ACS central science · 2025Article
- Engineering affinity-matured variants of an anti-polysialic acid monoclonal antibody with superior cytotoxicity-mediating potency.Cell chemical biology · 2025Article
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- Nanomechanical characterization of soft nanomaterial using atomic force microscopy.Materials today. Bio · 2025Review
- High-Throughput Centrifuge Force Microscopy Reveals Dynamic Immune-Cell Avidity at the Single-Cell Level.bioRxiv : the preprint server for biology · 2025Article
- Combination of Autodisplay and Dynamic Pharmacophore Modeling Reveals New Insights into Cyclic Nucleotide Binding in Hyperpolarization-Activated and Cyclic Nucleotide-Gated Ion Channel 4 (HCN4).ACS pharmacology & translational science · 2024Article
- Binding affinity between coronavirus spike protein and human ACE2 receptor.Computational and structural biotechnology journal · 2024Review
- BiSim Tool: a binding simulation tool to aid and simplify ligand-binding assay design and development.Bioanalysis · 2024Article
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- Identification of a potent PCNA-p15-interaction inhibitor by autodisplay-based peptide library screening.Microbial biotechnology · 2024Article
- Efficient evolution of human antibodies from general protein language models.Nature biotechnology · 2024Article
Corrections and comments
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2 authors.
Funding
Abstract
Determining the equilibrium-binding affinity (Kd) of two interacting proteins is essential not only for the biochemical study of protein signaling and function but also for the engineering of improved protein and enzyme variants. One common technique for measuring protein-binding affinities uses flow cytometry to analyze ligand binding to proteins presented on the surface of a cell. However, cell-binding assays require specific considerations to accurately quantify the binding affinity of a protein-protein interaction. Here we will cover the basic assumptions in designing a cell-based binding assay, including the relevant equations and theory behind determining binding affinities. Further, two major considerations in measuring binding affinities-time to equilibrium and ligand depletion-will be discussed. As these conditions have the potential to greatly alter the Kd, methods through which to avoid or minimize them will be provided. We then outline detailed protocols for performing direct- and competitive-binding assays against proteins displayed on the surface of yeast or mammalian cells that can be used to derive accurate Kd values. Finally, a comparison of cell-based binding assays to other types of binding assays will be presented.
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