ArticleScientific reports2016
A Rough Energy Landscape to Describe Surface-Linked Antibody and Antigen Bond Formation.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- Binding of Soluble Ligands to Membrane Receptors: A Molecular Dynamics Simulation Study.The journal of physical chemistry. B · 2025Article
- Combining DNA scaffolds and acoustic force spectroscopy to characterize individual protein bonds.Biophysical journal · 2023Article
- Is There a Need for a More Precise Description of Biomolecule Interactions to Understand Cell Function?Current issues in molecular biology · 2022Review
- Interplay of receptor-ligand binding and lipid domain formation during cell adhesion.Frontiers in molecular biosciences · 2022Review
- Interplay Between Receptor-Ligand Binding and Lipid Domain Formation Depends on the Mobility of Ligands in Cell-Substrate Adhesion.Frontiers in molecular biosciences · 2021Article
- Membrane Organization and Physical Regulation of Lymphocyte Antigen Receptors: A Biophysicist's Perspective.The Journal of membrane biology · 2019Review
- TCR-pMHC kinetics under force in a cell-free system show no intrinsic catch bond, but a minimal encounter duration before binding.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Nanobody-CD16 Catch Bond Reveals NK Cell Mechanosensitivity.Biophysical journal · 2019Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antibodies and B cell receptors often bind their antigen at cell-cell interface while both molecular species are surface-bound, which impacts bond kinetics and function. Despite the description of complex energy landscapes for dissociation kinetics which may also result in significantly different association kinetics, surface-bound molecule (2D) association kinetics usually remain described by an on-rate due to crossing of a single free energy barrier, and few experimental works have measured association kinetics under conditions implying force and two-dimensional relative ligand-receptor motion. We use a new laminar flow chamber to measure 2D bond formation with systematic variation of the distribution of encounter durations between antigen and antibody, in a range from 0.1 to 10 ms. Under physiologically relevant forces, 2D association is 100-fold slower than 3D association as studied by surface plasmon resonance assays. Supported by brownian dynamics simulations, our results show that a minimal encounter duration is required for 2D association; an energy landscape featuring a rough initial part might be a reasonable way of accounting for this. By systematically varying the temperature of our experiments, we evaluate roughness at 2k
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Registered trials
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.