ArticleAngewandte Chemie (International ed. in English)2020
Quantitative Assessment of Tip Effects in Single-Molecule High-Speed Atomic Force Microscopy Using DNA Origami Substrates.
Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Toward high-density streptavidin arrays on DNA origami nanostructures.RSC advances · 2025Article
- Rapid assembly of highly ordered DNA origami lattices at mica surfaces.Discover nano · 2025Article
- Nanomechanical characterization of soft nanomaterial using atomic force microscopy.Materials today. Bio · 2025Review
- Radiation and DNA Origami Nanotechnology: Probing Structural Integrity at the Nanoscale.Chemphyschem : a European journal of chemical physics and physical chemistry · 2025Review
- Linker Engineering of Ligand-Decorated DNA Origami Nanostructures Affects Biological Activity.Small (Weinheim an der Bergstrasse, Germany) · 2022Article
- Salting-Out of DNA Origami Nanostructures by Ammonium Sulfate.International journal of molecular sciences · 2022Article
- Atomic force microscopy-A tool for structural and translational DNA research.APL bioengineering · 2021Review
- Magnesium-Free Immobilization of DNA Origami Nanostructures at Mica Surfaces for Atomic Force Microscopy.Molecules (Basel, Switzerland) · 2021Article
- Adsorption of SARS-CoV-2 Spike Protein S1 at Oxide Surfaces Studied by High-Speed Atomic Force Microscopy.Advanced nanobiomed research · 2021Article
- Quantitative Assessment of Tip Effects in Single-Molecule High-Speed Atomic Force Microscopy Using DNA Origami Substrates.Angewandte Chemie (International ed. in English) · 2020Article
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4 authors.
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Abstract
High-speed atomic force microscopy (HS-AFM) is widely employed in the investigation of dynamic biomolecular processes at a single-molecule level. However, it remains an open and somewhat controversial question, how these processes are affected by the rapidly scanned AFM tip. While tip effects are commonly believed to be of minor importance in strongly binding systems, weaker interactions may significantly be disturbed. Herein, we quantitatively assess the role of tip effects in a strongly binding system using a DNA origami-based single-molecule assay. Despite its femtomolar dissociation constant, we find that HS-AFM imaging can disrupt monodentate binding of streptavidin (SAv) to biotin (Bt) even under gentle scanning conditions. To a lesser extent, this is also observed for the much stronger bidentate SAv-Bt complex. The presented DNA origami-based assay can be universally employed to quantify tip effects in strongly and weakly binding systems and to optimize the experimental settings for their reliable HS-AFM imaging.
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