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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)...

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Detalles Bibliográficos
Autores principales: Taninaka, Atsushi, Takeuchi, Osamu, Shigekawa, Hidemi
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
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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.
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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
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