ArticleJournal of biological physics2011
Imaging and determining friction forces of specific interactions between human IgG and rat anti-human IgG.
Article in Journal of biological physics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Electric Field-Driven Modulation of Nanomechanical Interactions Between Tyrosine Kinase Inhibitors and Human Serum Albumin: Insights from AFM-Based Force Spectroscopy.Molecules (Basel, Switzerland) · 2025Article
- Applying the Atomic Force Microscopy Technique in Medical Sciences-A Narrative Review.Biomedicines · 2024Review
- Review
- Friction Determination by Atomic Force Microscopy in Field of Biochemical Science.Micromachines · 2018Review
- Immunoassays based on surface-enhanced fluorescence using gap-plasmon-tunable Ag bilayer nanoparticle films.Journal of fluorescence · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Covalently immobilized rat anti-human immunoglobulin (IgG) monolayers on thiol-modified gold substrates and human IgG linked with the tips were fabricated using the self-assembled monolayer method, and interactions between these systems were studied by friction force microscopy (FFM). In addition to observation of distinct nanostructures of protein monolayers due to recognition events, FFM also quantified the friction force due to protein-protein-specific interactions. The average friction force due to interactions between the antigen functionalized tip and the antibody monolayer was determined as 200-250 pN, significantly greater than that between either the bare tip and the antibody monolayer (0-50 pN), or the blocked antigen tip and the antibody monolayer (50-100 pN), indicative of antigen/antibody-specific interactions. These results, taken together, suggest that FFM is not only capable of tracking recognition events, but also quantifying the friction force due to specific interactions between biological molecules, such as antigen and antibody.
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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.