Single-molecule force spectroscopy: a method for quantitative analysis of ligand-receptor interactions.
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.
Fuhrmann
Alexander
A
Department of Physics, Arizona State University, Tempe, AZ 85287-1504, USA.
Ros
Robert
R
D000937:Antigen-Antibody Reactions; D008024:Ligands; D018625:Microscopy, Atomic Force; D011956:Receptors, Cell Surface / Q000378:metabolism; D013057:Spectrum Analysis / Q000379:methods*
D008024:Ligands; D011956:Receptors, Cell Surface