Exploiting the ability of proteins to self-assemble into architectural templates may provide novel routes for the positioning of functional molecules in nanotechnology. Here we report the engineering of multicomponent protein templates composed of distinct monomers that assemble in repeating orders into a dynamic functional structure. This was achieved by redesigning the protein–protein interfaces of a molecular chaperone with helical sequences to create unique subunits that assemble through orthogonal coiled-coils into filaments up to several hundred nanometers in length. Subsequently, it was demonstrated that functional proteins could be fused to the subunits to achieve ordered alignment along filaments. Importantly, the multicomponent filaments had molecular chaperone activity and could prevent other proteins from thermal-induced aggregation, a potentially useful property for the scaffolding of enzymes. The design in this work is presented as proof-of-concept for the creation of modular templates that could potentially be used to position functional molecules, stabilize other proteins such as enzymes, and enable controlled assembly of nanostructures with unique topologies.

中文翻译：

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使用工程亚基界面组装多组分蛋白丝。

利用蛋白质自组装成建筑模板的能力可以为纳米技术中功能分子的定位提供新颖的途径。在这里，我们报告了由不同单体组成的多组分蛋白质模板的工程设计，这些单体以重复顺序组装成动态功能结构。这是通过重新设计分子伴侣具有螺旋序列的蛋白质-蛋白质界面以创建独特的亚基而实现的，这些亚基通过正交的卷曲线圈组装成长度达数百纳米的细丝。随后，证明了功能蛋白可以融合到亚基上，以实现沿着细丝的有序排列。重要的是，多组分长丝具有分子伴侣活性，可以阻止其他蛋白质热诱导聚集，可能对酶的支架有用。这项工作中的设计是概念验证，用于创建模块化模板，该模板可潜在地用于定位功能分子，稳定其他蛋白质（如酶）并实现具有独特拓扑结构的纳米结构的受控组装。