Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 11, Issue 5, Pages 2134-2151Publisher
MDPI
DOI: 10.3390/ijms11052134
Keywords
dynamic force spectroscopy; atomic force microscopy; site-selective analysis; streptavidin-biotin interaction
Funding
- Ministry of Education, Culture, Sports, Science, and Technology of Japan
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available