ArticleBiophysical journal2005
The solution to the streptavidin-biotin paradox: the influence of history on the strength of single molecular bonds.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- Kinetic study of membrane protein interactions: from three to two dimensions.Scientific reports · 2024Article
- Membrane Tubulation with a Biomembrane Force Probe.Membranes · 2023Article
- Biomembrane force probe (BFP): Design, advancements, and recent applications to live-cell mechanobiology.Exploration (Beijing, China) · 2023Review
- New Label-Free Biosensing for the Evaluation of the AX-024 Inhibitor: Case Study for the Development of New Drugs in Autoimmune Diseases.Sensors (Basel, Switzerland) · 2022Article
- Mechanotransduction as a major driver of cell behaviour: mechanisms, and relevance to cell organization and future research.Open biology · 2021Review
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- 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
- Detection of streptavidin-biotin intermediate metastable states at the single-molecule level using high temporal-resolution atomic force microscopy.RSC advances · 2019Article
- Direction Matters: Monovalent Streptavidin/Biotin Complex under Load.Nano letters · 2019Article
- Heterogeneous and rate-dependent streptavidin-biotin unbinding revealed by high-speed force spectroscopy and atomistic simulations.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Keratocytes Generate High Integrin Tension at the Trailing Edge to Mediate Rear De-adhesion during Rapid Cell Migration.iScience · 2018Article
- How Do We Know when Single-Molecule Force Spectroscopy Really Tests Single Bonds?Biophysical journal · 2018Review
- Dissection of structural dynamics of chromatin fibers by single-molecule magnetic tweezers.Biophysics reports · 2018Article
- Micropipette force probe to quantify single-cell force generation: application to T-cell activation.Molecular biology of the cell · 2017Article
- BFPTool: a software tool for analysis of Biomembrane Force Probe experiments.BMC biophysics · 2017Article
- Characterizing cell adhesion by using micropipette aspiration.Biophysical journal · 2015Article
- pH-dependent deformations of the energy landscape of avidin-like proteins investigated by single molecule force spectroscopy.Molecules (Basel, Switzerland) · 2014Article
- Integrin-generated forces lead to streptavidin-biotin unbinding in cellular adhesions.Biophysical journal · 2014Article
- Atomic force microscopy reveals a role for endothelial cell ICAM-1 expression in bladder cancer cell adherence.PloS one · 2014Article
- Biophysical description of multiple events contributing blood leukocyte arrest on endothelium.Frontiers in immunology · 2013Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the past few years, many studies have attempted to measure the strength of a single molecular bond. In general, these experiments consisted in pulling on the bond and measuring the force necessary to dissociate the molecules. However, seemingly contradictory experimental results led to draw the intriguing conclusion that the strength of the bond could depend on the experiment even if the pulling conditions are similar: this paradox was first observed on the widely used streptavidin-biotin bond. Here, by doing supplementary measurements and by reanalyzing the controversial experimental results using Kramers' theory, we show that they can be conciliated. This allows us to show that the strength of a bond is very sensitive to the history of its formation, which is the key to the paradox.
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