Cargando…
Reconsideration of Dynamic Force Spectroscopy Analysis of Streptavidin-Biotin Interactions
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)...
Autores principales: | , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Molecular Diversity Preservation International (MDPI)
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2885099/ https://www.ncbi.nlm.nih.gov/pubmed/20559507 http://dx.doi.org/10.3390/ijms11052134 |
_version_ | 1782182354696011776 |
---|---|
author | Taninaka, Atsushi Takeuchi, Osamu Shigekawa, Hidemi |
author_facet | Taninaka, Atsushi Takeuchi, Osamu Shigekawa, Hidemi |
author_sort | Taninaka, Atsushi |
collection | PubMed |
description | 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. |
format | Text |
id | pubmed-2885099 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Molecular Diversity Preservation International (MDPI) |
record_format | MEDLINE/PubMed |
spelling | pubmed-28850992010-06-17 Reconsideration of Dynamic Force Spectroscopy Analysis of Streptavidin-Biotin Interactions Taninaka, Atsushi Takeuchi, Osamu Shigekawa, Hidemi Int J Mol Sci Article 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. Molecular Diversity Preservation International (MDPI) 2010-05-13 /pmc/articles/PMC2885099/ /pubmed/20559507 http://dx.doi.org/10.3390/ijms11052134 Text en © 2010 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Taninaka, Atsushi Takeuchi, Osamu Shigekawa, Hidemi Reconsideration of Dynamic Force Spectroscopy Analysis of Streptavidin-Biotin Interactions |
title | Reconsideration of Dynamic Force Spectroscopy Analysis of Streptavidin-Biotin Interactions |
title_full | Reconsideration of Dynamic Force Spectroscopy Analysis of Streptavidin-Biotin Interactions |
title_fullStr | Reconsideration of Dynamic Force Spectroscopy Analysis of Streptavidin-Biotin Interactions |
title_full_unstemmed | Reconsideration of Dynamic Force Spectroscopy Analysis of Streptavidin-Biotin Interactions |
title_short | Reconsideration of Dynamic Force Spectroscopy Analysis of Streptavidin-Biotin Interactions |
title_sort | reconsideration of dynamic force spectroscopy analysis of streptavidin-biotin interactions |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2885099/ https://www.ncbi.nlm.nih.gov/pubmed/20559507 http://dx.doi.org/10.3390/ijms11052134 |
work_keys_str_mv | AT taninakaatsushi reconsiderationofdynamicforcespectroscopyanalysisofstreptavidinbiotininteractions AT takeuchiosamu reconsiderationofdynamicforcespectroscopyanalysisofstreptavidinbiotininteractions AT shigekawahidemi reconsiderationofdynamicforcespectroscopyanalysisofstreptavidinbiotininteractions |