ArticleBiophysical journal2009
Biomolecule association rates do not provide a complete description of bond formation.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Is There a Need for a More Precise Description of Biomolecule Interactions to Understand Cell Function?Current issues in molecular biology · 2022Review
- Mechanotransduction as a major driver of cell behaviour: mechanisms, and relevance to cell organization and future research.Open biology · 2021Review
- 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
- A general model of focal adhesion orientation dynamics in response to static and cyclic stretch.Communications biology · 2018Article
- A Rough Energy Landscape to Describe Surface-Linked Antibody and Antigen Bond Formation.Scientific reports · 2016Article
- Transport regulation of two-dimensional receptor-ligand association.Biophysical journal · 2015Article
- Cell surface topography is a regulator of molecular interactions during chemokine-induced neutrophil spreading.Biophysical journal · 2014Article
- Biophysical description of multiple events contributing blood leukocyte arrest on endothelium.Frontiers in immunology · 2013Article
- Functional interaction of CD154 protein with α5β1 integrin is totally independent from its binding to αIIbβ3 integrin and CD40 molecules.The Journal of biological chemistry · 2012Article
- Kinetics and mechanics of two-dimensional interactions between T cell receptors and different activating ligands.Biophysical journal · 2012Article
- Membrane dynamics shape TCR-generated signaling.Frontiers in immunology · 2012Article
- Article
- Minimal encounter time and separation determine ligand-receptor binding in cell adhesion.Biophysical journal · 2011Article
- Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The efficiency of many cell-surface receptors is dependent on the rate of binding soluble or surface-attached ligands. Much effort was exerted to measure association rates between soluble molecules (three-dimensional k(on)) and, more recently, between surface-attached molecules (two-dimensional [2D] k(on)). According to a generally accepted assumption, the probability of bond formation between receptors and ligands is proportional to the first power of encounter duration. Here we provide new experimental evidence and review published data demonstrating that this simple assumption is not always warranted. Using as a model system the (2D) interaction between ICAM-1-coated surfaces and flowing microspheres coated with specific anti-ICAM-1 antibodies, we show that the probability of bond formation may scale as a power of encounter duration that is significantly higher than 1. Further, we show that experimental data may be accounted for by modeling ligand-receptor interaction as a displacement along a single path of a rough energy landscape. Under a wide range of conditions, the probability that an encounter of duration t resulted in bond formation varied as erfc[(t(0)/t)(1/2)], where t(0) was on the order of 10 ms. We conclude that the minimum contact time for bond formation may be a useful parameter to describe a ligand-receptor interaction, in addition to conventional association rates.
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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.