ArticleProceedings of the National Academy of Sciences of the United States of America2019
Heterogeneous and rate-dependent streptavidin-biotin unbinding revealed by high-speed force spectroscopy and atomistic simulations.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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51 citing papers in PubMed, 124 citations in OpenAlex.
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- Controlled and orthogonal partitioning of large particles into biomolecular condensates.Nature communications · 2025Article
- AFM reveals differential effects of acidification on LDL- and oxidized LDL-receptor interactions: biomechanical implications in atherogenesis.Cellular & molecular biology letters · 2025Article
- In silico analyses of molecular force sensors for mechanical characterization of biological systems.Biophysical journal · 2025Article
- Multistate kinetics of the syringe-like injection mechanism of Tc toxins.Science advances · 2025Article
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- Controlled and orthogonal partitioning of large particles into biomolecular condensates.bioRxiv : the preprint server for biology · 2024Article
- Mechanical Stability and Unfolding Pathways of Parallel Tetrameric G-Quadruplexes Probed by Pulling Simulations.Journal of chemical information and modeling · 2024Article
- Ebola Virus Glycoprotein Strongly Binds to Membranes in the Absence of Receptor Engagement.ACS infectious diseases · 2024Article
- A Biophysics Toolbox for Reliable Data Acquisition and Processing in Integrated Force-Confocal Fluorescence Microscopy.ACS photonics · 2024Article
- Statistical Study of Low-Intensity Single-Molecule Recognition Events Using DeepTipBiomimetics (Basel, Switzerland) · 2023Article
- Development of Single Molecule Techniques for Sensing and Manipulation of CRISPR and Polymerase Enzymes.Small (Weinheim an der Bergstrasse, Germany) · 2023Review
- Complexity of Guanine Quadruplex Unfolding Pathways Revealed by Atomistic Pulling Simulations.Journal of chemical information and modeling · 2023Article
- Combining DNA scaffolds and acoustic force spectroscopy to characterize individual protein bonds.Biophysical journal · 2023Article
- Anisotropic Friction in a Ligand-Protein Complex.Nano letters · 2023Article
- Interfacial Layer Breaker: A Violation of Stokes' Law in High-Speed Atomic Force Microscope Flows.Langmuir : the ACS journal of surfaces and colloids · 2023Article
- High-Yield Characterization of Single Molecule Interactions with DeepTipMolecules (Basel, Switzerland) · 2022Article
- Visualizing Intramolecular Dynamics of Membrane Proteins.International journal of molecular sciences · 2022Review
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Authors and funding
5 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Receptor-ligand interactions are essential for biological function and their binding strength is commonly explained in terms of static lock-and-key models based on molecular complementarity. However, detailed information on the full unbinding pathway is often lacking due, in part, to the static nature of atomic structures and ensemble averaging inherent to bulk biophysics approaches. Here we combine molecular dynamics and high-speed force spectroscopy on the streptavidin-biotin complex to determine the binding strength and unbinding pathways over the widest dynamic range. Experiment and simulation show excellent agreement at overlapping velocities and provided evidence of the unbinding mechanisms. During unbinding, biotin crosses multiple energy barriers and visits various intermediate states far from the binding pocket, while streptavidin undergoes transient induced fits, all varying with loading rate. This multistate process slows down the transition to the unbound state and favors rebinding, thus explaining the long lifetime of the complex. We provide an atomistic, dynamic picture of the unbinding process, replacing a simple two-state picture with one that involves many routes to the lock and rate-dependent induced-fit motions for intermediates, which might be relevant for other receptor-ligand bonds.
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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.