Single-molecule force spectroscopy: a method for quantitative analysis of ligand-receptor interactions
Single-molecule force spectroscopy: a method for quantitative analysis of ligand-receptor interactions
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DOI：
10.2217/nnm.10.26
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发表时间：
2010-06-01
期刊：
影响因子：
5.5
通讯作者：
Ros, Robert
中科院分区：
文献类型：
--
作者：
Fuhrmann, Alexander;Ros, Robert
分子相互作用的定量分析在医学研究中具有重要意义。大多数研究配体受体复合体的方法都涉及大量的生物分子，但往往忽略了与低亲和力或具有不同结合性质的小亚群之间的相互作用。单分子力谱为在广泛的亲和力范围内定量分析配体受体相互作用和检测点突变的灵敏度提供了迷人的可能性。此外，这项技术使人们能够解决有关结合能格局的问题。在这篇文章中，我们介绍了单分子力谱，重点介绍了该技术在数据分析和理论模型方面的新发展。我们还演示了该方法的两个功能示例。
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.