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.
Department of Physics, Arizona State University, Tempe, AZ 85287-1504, USA.
Alexander
A
Fuhrmann
Robert
R
Ros
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