Department of Physics, Arizona State University, Tempe, AZ 85287-1504, USA.
Nanomedicine (Lond). 2010 Jun;5(4):657-66. doi: 10.2217/nnm.10.26.
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.
分子相互作用的定量分析在医学研究中具有重要意义。大多数用于研究配体-受体复合物的方法都涉及大量的生物分子集合，但往往忽略了与低亲和力或具有不同结合特性的小亚群的相互作用。单分子力谱技术为定量分析广泛亲和力范围内的配体-受体相互作用以及检测点突变提供了迷人的可能性。此外，该技术还可以解决与相关结合能景观有关的问题。本文重点介绍单分子力谱技术，包括该技术在数据分析和理论模型方面的新进展。我们还展示了该方法的两个应用实例。
