ArticleBiophysical journal2007
Affinity-matured recombinant antibody fragments analyzed by single-molecule force spectroscopy.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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Who cites it
31 citing papers in PubMed, 85 citations in OpenAlex.
- AFM-Based Single-Molecule Force Spectroscopy of PEG-Anti-PEG Antibody Interactions.ACS applied bio materials · 2026Article
- Advances in ligand-based surface engineering strategies for fine-tuning T cell mechanotransduction toward efficient immunotherapy.Biophysical journal · 2025Review
- Expression, Sarkosyl Solubilization, DNase Activity, Purification, and SPR Binding Affinity of Recombinant Diphtheria Toxoid (rCRM197EK) Expressed in Escherichia coli BL21(DE3).Molecular biotechnology · 2025Article
- Mechanical control of antigen detection and discrimination by T and B cell receptors.Biophysical journal · 2024Review
- Immune cells use active tugging forces to distinguish affinity and accelerate evolution.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Interaction of miR-155 with Human Serum Albumin: An Atomic Force Spectroscopy, Fluorescence, FRET, and Computational Modelling Evidence.International journal of molecular sciences · 2022Article
- Digital holography-based 3D particle localization for single-molecule tweezer techniques.Biophysical journal · 2022Article
- Long-term imaging of individual mRNA molecules in living cells.Cell reports methods · 2022Article
- The CAR T-Cell Mechanoimmunology at a Glance.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020Review
- Kin discrimination in social yeast is mediated by cell surface receptors of the Flo11 adhesin family.eLife · 2020Article
- Probing Ligand-Receptor Interaction in Living Cells Using Force Measurements With Optical Tweezers.Frontiers in bioengineering and biotechnology · 2020Article
- Removal of a Conserved Disulfide Bond Does Not Compromise Mechanical Stability of a VHH Antibody Complex.Nano letters · 2019Article
- Engineering switchable and programmable universal CARs for CAR T therapy.Journal of hematology & oncology · 2019Review
- Nanobody-CD16 Catch Bond Reveals NK Cell Mechanosensitivity.Biophysical journal · 2019Article
- Investigating single molecule adhesion by atomic force spectroscopy.Journal of visualized experiments : JoVE · 2015Article
- Ultrastable cellulosome-adhesion complex tightens under load.Nature communications · 2014Article
- Atomic force microscopy with sub-picoNewton force stability for biological applications.Methods (San Diego, Calif.) · 2013Review
- A force-activated trip switch triggers rapid dissociation of a colicin from its immunity protein.PLoS biology · 2013Article
- Single-molecule dissection of the high-affinity cohesin-dockerin complex.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Exploring the energy profile of human IgG/rat anti-human IgG interactions by dynamic force spectroscopy.The protein journal · 2012Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
For many applications, antibodies need to be engineered toward maximum affinity. Strategies are in demand to especially optimize this process toward slower dissociation rates, which correlate with the (un)binding forces. Using single-molecule force spectroscopy, we have characterized three variants of a recombinant antibody single-chain Fv fragment. These variants were taken from different steps of an affinity maturation process. Therefore, they are closely related and differ from each other by a few mutations only. The dissociation rates determined with the atomic force microscope differ by one order of magnitude and agree well with the values obtained from surface plasmon resonance measurements. However, the effective potential width of the binding complexes, which was derived from the dynamic force spectroscopy measurements, was found to be the same for the different mutants. The large potential width of 0.9 nm indicates that both the binding pocket and the peptide deform significantly during the unbinding process.
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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.