Department of Physics and Astronomy, University of Sheffield, Sheffield, United Kingdom; Department of Infection, Immunity and Cardiovascular Disease, University of Sheffield, Sheffield, United Kingdom.
Department of Physics, Nanjing University, Nanjing, People's Republic of China.
Biophys J. 2019 Aug 20;117(4):688-695. doi: 10.1016/j.bpj.2019.07.002. Epub 2019 Jul 5.
Dynamic single-molecule force spectroscopy was performed to monitor the unbinding of fibronectin with the proteoglycans syndecan-4 (SDC4) and decorin and to compare this with the unbinding characteristics of αβ-integrin. A single energy barrier was sufficient to describe the unbinding of both SDC4 and decorin from fibronectin, whereas two barriers were observed for the dissociation of αβ-integrin from fibronectin. The outer (high-affinity) barriers in the interactions of fibronectin with αβ-integrin and SDC4 are characterized by larger barrier heights and widths and slower dissociation rates than those of the inner (low-affinity) barriers in the interactions of fibronectin with αβ-integrin and decorin. These results indicate that SDC4 and (ultimately) αβ-integrin have the ability to withstand deformation in their interactions with fibronectin, whereas the decorin-fibronectin interaction is considerably more brittle.
采用动态单分子力谱技术来监测纤连蛋白与蛋白聚糖 syndecan-4（SDC4）和decorin 的解联，并将其与 αβ-整联蛋白的解联特性进行比较。一个单一的能量势垒足以描述 SDC4 和 decorin 从纤连蛋白上的解联，而αβ-整联蛋白从纤连蛋白上的解离则观察到两个势垒。纤连蛋白与 αβ-整联蛋白和 SDC4 的相互作用的外（高亲和力）势垒的特征是具有更大的势垒高度和宽度，以及比纤连蛋白与 αβ-整联蛋白和 decorin 的相互作用的内（低亲和力）势垒的解离速率更慢。这些结果表明，SDC4 和（最终）αβ-整联蛋白具有在与纤连蛋白相互作用中承受变形的能力，而 decorin-纤连蛋白相互作用则相当脆弱。
