The State Key Laboratory of Molecular Engineering of Polymers, Department of Macromolecular Science and Collaborative Innovation Center of Genetics and Development, Fudan University, Shanghai, 200433, China.
Center for Soft Condensed Matter Physics and Interdisciplinary Research, Soochow University, Suzhou, 215006, China.
Angew Chem Int Ed Engl. 2017 Aug 28;56(36):10691-10695. doi: 10.1002/anie.201703052. Epub 2017 Jun 7.
In nature, proteins self-assemble into various structures with different dimensions. To construct these nanostructures in laboratories, normally proteins with different symmetries are selected. However, most of these approaches are engineering-intensive and highly dependent on the accuracy of the protein design. Herein, we report that a simple native protein LecA assembles into one-dimensional nanoribbons and nanowires, two-dimensional nanosheets, and three-dimensional layered structures controlled mainly by small-molecule assembly-inducing ligands RnG (n=1, 2, 3, 4, 5) with varying numbers of ethylene oxide repeating units. To understand the formation mechanism of the different morphologies controlled by the small-molecule structure, molecular simulations were performed from microscopic and mesoscopic view, which presented a clear relationship between the molecular structure of the ligands and the assembled patterns. These results introduce an easy strategy to control the assembly structure and dimension, which could shed light on controlled protein assembly.
在自然界中，蛋白质会自组装成具有不同维度的各种结构。为了在实验室中构建这些纳米结构，通常会选择具有不同对称性的蛋白质。然而，这些方法大多需要进行复杂的工程设计，并且高度依赖于蛋白质设计的准确性。在此，我们报告称，一种简单的天然蛋白质 LecA 可以在小分子组装诱导配体 RnG（n=1、2、3、4、5）的控制下自组装成一维纳米带和纳米线、二维纳米片以及三维层状结构，其中 RnG 具有不同数量的氧化乙烯重复单元。为了理解小分子结构控制的不同形态的形成机制，我们从微观和介观的角度进行了分子模拟，揭示了配体的分子结构与组装模式之间的清晰关系。这些结果为控制蛋白质组装提供了一种简单的策略，可能会为控制蛋白质组装提供新的思路。
