ArticleBeilstein journal of nanotechnology2015
Probing fibronectin-antibody interactions using AFM force spectroscopy and lateral force microscopy.
Article in Beilstein journal of nanotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Atomic Force Microscopy Based Single Molecule Recognition: Deciphering Biological Interactions at the Nanoscale.Journal of molecular recognition : JMR · 2026Review
- Specific Binding of Novel SPION-Based System Bearing Anti-N-Cadherin Antibodies to Prostate Tumor Cells.International journal of nanomedicine · 2021Article
- Distinct Binding Interactions of αBiophysical journal · 2019Article
- Advanced atomic force microscopy techniques III.Beilstein journal of nanotechnology · 2016Article
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Authors and funding
5 authors.
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Abstract
The first experiment showing the effects of specific interaction forces using lateral force microscopy (LFM) was demonstrated for lectin-carbohydrate interactions some years ago. Such measurements are possible under the assumption that specific forces strongly dominate over the non-specific ones. However, obtaining quantitative results requires the complex and tedious calibration of a torsional force. Here, a new and relatively simple method for the calibration of the torsional force is presented. The proposed calibration method is validated through the measurement of the interaction forces between human fibronectin and its monoclonal antibody. The results obtained using LFM and AFM-based classical force spectroscopies showed similar unbinding forces recorded at similar loading rates. Our studies verify that the proposed lateral force calibration method can be applied to study single molecule interactions.
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