Collaborative Innovation Center of Advanced Microstructures, National Laboratory of Solid State Microstructure, Department of Physics, Nanjing University, Nanjing, 210093, P. R. China.
Collaborative Innovation Center of Atmospheric Environment and Equipment Technology, Jiangsu Key Laboratory of Atmospheric Environment Monitoring and Pollution Control, School of Environmental Science and Engineering, Nanjing University of Information Science & Technology, Nanjing, Jiangsu, 210044, P. R. China.
Chemistry. 2018 Jul 2;24(37):9224-9228. doi: 10.1002/chem.201801730. Epub 2018 May 29.
Hydrophobins have raised lots of interest as powerful surface adhesives. However, it remains largely unexplored how their strong and versatile surface adhesion is linked to their unique amphiphilic structural features. Here, we develop an AFM-based single-molecule force spectroscopy assay to quantitatively measure the binding strength of hydrophobin to various types of surfaces both in isolation and in preformed protein films. We find that individual class II hydrophobins (HFBI) bind strongly to hydrophobic surfaces but weakly to hydrophilic ones. After self-assembly into protein films, they show much stronger binding strength to both surfaces due to the cooperativity of different interactions at nanoscale. Such self-assembly enhanced surface binding may serve as a general design principle for synthetic bioactive adhesives.
水蛋白作为一种强大的表面黏附剂引起了广泛关注。然而，它们独特的两亲性结构特征如何与其强大且多功能的表面黏附力相关联，在很大程度上仍未得到探索。在这里，我们开发了一种基于原子力显微镜的单分子力谱测定法，以定量测量水蛋白与各种类型表面的结合强度，包括在单独状态和预先形成的蛋白质膜中。我们发现，单个 II 类水蛋白（HFBI）强烈结合疏水性表面，但弱结合亲水性表面。在自组装成蛋白质膜后，由于纳米尺度上不同相互作用的协同作用，它们对两种表面的结合强度都大大增强。这种自组装增强的表面结合可能成为合成生物活性黏附剂的一般设计原则。
