Force Measurement Enabling Precise Analysis by Dynamic Force Spectroscopy
Dynamic force spectroscopy (DFS) makes it possible to investigate specific interactions between two molecules such as ligand-receptor pairs at the single-molecule level. In the DFS method based on the Bell-Evans model, the unbinding force applied to a molecular bond is increased at a constant rate,...
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| Format: | Article |
| Language: | English |
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MDPI AG
2011-12-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | http://www.mdpi.com/1422-0067/13/1/453/ |
| _version_ | 1811257624439554048 |
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| author | Hidemi Shigekawa Osamu Takeuchi Yuuichi Hirano Atsushi Taninaka |
| author_facet | Hidemi Shigekawa Osamu Takeuchi Yuuichi Hirano Atsushi Taninaka |
| author_sort | Hidemi Shigekawa |
| collection | DOAJ |
| description | Dynamic force spectroscopy (DFS) makes it possible to investigate specific interactions between two molecules such as ligand-receptor pairs at the single-molecule level. In the DFS method based on the Bell-Evans model, the unbinding force applied to a molecular bond is increased at a constant rate, and the force required to rupture the molecular bond is measured. By analyzing the relationship between the modal rupture force and the logarithm of the loading rate, microscopic potential barrier landscapes and the lifetimes of bonds can be obtained. However, the results obtained, for example, in the case of streptavidin/biotin complexes, have differed among previous studies and some results have been inconsistent with theoretical predictions. In this study, using an atomic force microscopy technique that enables the precise analysis of molecular interactions on the basis of DFS, we investigated the effect of the sampling rate on DFS analysis. The shape of rupture force histograms, for example, was significantly deformed at a sampling rate of 1 kHz in comparison with that of histograms obtained at 100 kHz, indicating the fundamental importance of ensuring suitable experimental conditions for further advances in the DFS method. |
| first_indexed | 2024-04-12T18:00:25Z |
| format | Article |
| id | doaj.art-4b4636c2f19140fcb0062bdcc9caa2d6 |
| institution | Directory Open Access Journal |
| issn | 1422-0067 |
| language | English |
| last_indexed | 2024-04-12T18:00:25Z |
| publishDate | 2011-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-4b4636c2f19140fcb0062bdcc9caa2d62022-12-22T03:22:11ZengMDPI AGInternational Journal of Molecular Sciences1422-00672011-12-0113145346510.3390/ijms13010453Force Measurement Enabling Precise Analysis by Dynamic Force SpectroscopyHidemi ShigekawaOsamu TakeuchiYuuichi HiranoAtsushi TaninakaDynamic force spectroscopy (DFS) makes it possible to investigate specific interactions between two molecules such as ligand-receptor pairs at the single-molecule level. In the DFS method based on the Bell-Evans model, the unbinding force applied to a molecular bond is increased at a constant rate, and the force required to rupture the molecular bond is measured. By analyzing the relationship between the modal rupture force and the logarithm of the loading rate, microscopic potential barrier landscapes and the lifetimes of bonds can be obtained. However, the results obtained, for example, in the case of streptavidin/biotin complexes, have differed among previous studies and some results have been inconsistent with theoretical predictions. In this study, using an atomic force microscopy technique that enables the precise analysis of molecular interactions on the basis of DFS, we investigated the effect of the sampling rate on DFS analysis. The shape of rupture force histograms, for example, was significantly deformed at a sampling rate of 1 kHz in comparison with that of histograms obtained at 100 kHz, indicating the fundamental importance of ensuring suitable experimental conditions for further advances in the DFS method.http://www.mdpi.com/1422-0067/13/1/453/dynamic force spectroscopyatomic force microscopypotential landscapefunctional moleculesmolecular recognition |
| spellingShingle | Hidemi Shigekawa Osamu Takeuchi Yuuichi Hirano Atsushi Taninaka Force Measurement Enabling Precise Analysis by Dynamic Force Spectroscopy International Journal of Molecular Sciences dynamic force spectroscopy atomic force microscopy potential landscape functional molecules molecular recognition |
| title | Force Measurement Enabling Precise Analysis by Dynamic Force Spectroscopy |
| title_full | Force Measurement Enabling Precise Analysis by Dynamic Force Spectroscopy |
| title_fullStr | Force Measurement Enabling Precise Analysis by Dynamic Force Spectroscopy |
| title_full_unstemmed | Force Measurement Enabling Precise Analysis by Dynamic Force Spectroscopy |
| title_short | Force Measurement Enabling Precise Analysis by Dynamic Force Spectroscopy |
| title_sort | force measurement enabling precise analysis by dynamic force spectroscopy |
| topic | dynamic force spectroscopy atomic force microscopy potential landscape functional molecules molecular recognition |
| url | http://www.mdpi.com/1422-0067/13/1/453/ |
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