Abstract
The quantitative analysis of molecular interactions is of high interest in medical research. Most methods for the investigation of ligand-receptor complexes deal with huge ensembles of biomolecules, but often neglect interactions with low affinity or small subpopulations with different binding properties. Single-molecule force spectroscopy offers fascinating possibilities for the quantitative analysis of ligand-receptor interactions in a wide affinity range and the sensitivity to detect point mutations. Furthermore, this technique allows one to address questions about the related binding energy landscape. In this article, we introduce single-molecule force spectroscopy with a focus on novel developments in both data analysis and theoretical models for the technique. We also demonstrate two examples of the capabilities of this method.
Original language | English (US) |
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Pages (from-to) | 657-666 |
Number of pages | 10 |
Journal | Nanomedicine |
Volume | 5 |
Issue number | 4 |
DOIs | |
State | Published - Jun 2010 |
Keywords
- Atomic force microscopy
- Force spectroscopy
- Ligandreceptor
- Single molecule
ASJC Scopus subject areas
- Bioengineering
- Medicine (miscellaneous)
- Biomedical Engineering
- General Materials Science