ArticleBiophysical journal2008
Extending Bell's model: how force transducer stiffness alters measured unbinding forces and kinetics of molecular complexes.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
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- Combining DNA scaffolds and acoustic force spectroscopy to characterize individual protein bonds.Biophysical journal · 2023Article
- In silico and in vitro study of the adhesion dynamics of erythrophagocytosis in sickle cell disease.Biophysical journal · 2023Article
- Catch bond-inspired hydrogels with repeatable and loading rate-sensitive specific adhesion.Bioactive materials · 2023Article
- Bell-Evans model and steered molecular dynamics in uncovering the dissociation kinetics of ligands targeting G-protein-coupled receptors.Scientific reports · 2022Article
- Elasticity-associated rebinding rate of molecular bonds between soft elastic media.Biophysical journal · 2022Article
- Molecular Recognition of Proteins through Quantitative Force Maps at Single Molecule Level.Biomolecules · 2022Article
- Streptavidin/biotin: Tethering geometry defines unbinding mechanics.Science advances · 2020Article
- 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
- Quantifying Shear-Induced Deformation and Detachment of Individual Adherent Sickle Red Blood Cells.Biophysical journal · 2019Article
- How Do We Know when Single-Molecule Force Spectroscopy Really Tests Single Bonds?Biophysical journal · 2018Review
- A nanoscale perspective on the effects of transverse microprestress on drying creep of nanoporous solids.Proceedings. Mathematical, physical, and engineering sciences · 2018Article
- Molecular mechanism of DNA association with single-stranded DNA binding protein.Nucleic acids research · 2017Article
- Nonlinear Actin Deformations Lead to Network Stiffening, Yielding, and Nonuniform Stress Propagation.Biophysical journal · 2017Article
- The mechano-sensing role of the unique SH3 insertion in plakin domains revealed by Molecular Dynamics simulations.Scientific reports · 2017Article
- Transient effects of drying creep in nanoporous solids: understanding the effects of nanoscale energy barriers.Proceedings. Mathematical, physical, and engineering sciences · 2016Article
- Ranking of Molecular Biomarker Interaction with Targeted DNA Nucleobases via Full Atomistic Molecular Dynamics.Scientific reports · 2016Article
- Epithelial-mesenchymal transition enhances nanoscale actin filament dynamics of ovarian cancer cells.The journal of physical chemistry. B · 2013Article
- A force-activated trip switch triggers rapid dissociation of a colicin from its immunity protein.PLoS biology · 2013Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Forced unbinding of complementary macromolecules such as ligand-receptor complexes can reveal energetic and kinetic details governing physiological processes ranging from cellular adhesion to drug metabolism. Although molecular-level experiments have enabled sampling of individual ligand-receptor complex dissociation events, disparities in measured unbinding force F(R) among these methods lead to marked variation in inferred binding energetics and kinetics at equilibrium. These discrepancies are documented for even the ubiquitous ligand-receptor pair, biotin-streptavidin. We investigated these disparities and examined atomic-level unbinding trajectories via steered molecular dynamics simulations, as well as via molecular force spectroscopy experiments on biotin-streptavidin. In addition to the well-known loading rate dependence of F(R) predicted by Bell's model, we find that experimentally accessible parameters such as the effective stiffness of the force transducer k can significantly perturb the energy landscape and the apparent unbinding force of the complex for sufficiently stiff force transducers. Additionally, at least 20% variation in unbinding force can be attributed to minute differences in initial atomic positions among energetically and structurally comparable complexes. For force transducers typical of molecular force spectroscopy experiments and atomistic simulations, this energy barrier perturbation results in extrapolated energetic and kinetic parameters of the complex that depend strongly on k. We present a model that explicitly includes the effect of k on apparent unbinding force of the ligand-receptor complex, and demonstrate that this correction enables prediction of unbinding distances and dissociation rates that are decoupled from the stiffness of actual or simulated molecular linkers.
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