ArticleInternational journal of molecular sciences2010
Reconsideration of dynamic force spectroscopy analysis of streptavidin-biotin interactions.
Article in International journal of molecular sciences, 2010. 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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10 citing papers in PubMed.
- AFM reveals differential effects of acidification on LDL- and oxidized LDL-receptor interactions: biomechanical implications in atherogenesis.Cellular & molecular biology letters · 2025Article
- Surface charge density measurement of a single protein molecule with a controlled orientation by AFM.Biophysical journal · 2021Article
- Probing Ligand-Receptor Interaction in Living Cells Using Force Measurements With Optical Tweezers.Frontiers in bioengineering and biotechnology · 2020Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- Detection of streptavidin-biotin intermediate metastable states at the single-molecule level using high temporal-resolution atomic force microscopy.RSC advances · 2019Article
- Direction Matters: Monovalent Streptavidin/Biotin Complex under Load.Nano letters · 2019Article
- How Do We Know when Single-Molecule Force Spectroscopy Really Tests Single Bonds?Biophysical journal · 2018Review
- Monodisperse measurement of the biotin-streptavidin interaction strength in a well-defined pulling geometry.PloS one · 2017Article
- A simple bioconjugate attachment protocol for use in single molecule force spectroscopy experiments based on mixed self-assembled monolayers.International journal of molecular sciences · 2012Article
- Force measurement enabling precise analysis by dynamic force spectroscopy.International journal of molecular sciences · 2012Article
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3 authors.
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Abstract
To understand and design molecular functions on the basis of molecular recognition processes, the microscopic probing of the energy landscapes of individual interactions in a molecular complex and their dependence on the surrounding conditions is of great importance. Dynamic force spectroscopy (DFS) is a technique that enables us to study the interaction between molecules at the single-molecule level. However, the obtained results differ among previous studies, which is considered to be caused by the differences in the measurement conditions. We have developed an atomic force microscopy technique that enables the precise analysis of molecular interactions on the basis of DFS. After verifying the performance of this technique, we carried out measurements to determine the landscapes of streptavidin-biotin interactions. The obtained results showed good agreement with theoretical predictions. Lifetimes were also well analyzed. Using a combination of cross-linkers and the atomic force microscope that we developed, site-selective measurement was carried out, and the steps involved in bonding due to microscopic interactions are discussed using the results obtained by site-selective analysis.
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