Protein Self-Assembly Driven by De Novo Coiled Coils and Constructing Ag Nanoparticle-Protein Assembly Composite with High Catalytic Activity

Abstract Construction of protein self‐assembly has drawn more and more attention for understanding the natural wisdom and producing functional biomaterial. Current efforts focus on the novel driving force, dynamic control, and functionalization. In this study, protein assembly driven by de novo coiled coils is reported. By precisely designing coiled coil sequence, dimeric antiparallel coiled coils are successfully constructed and used as a linker to drive helical protein nanostructures. Furthermore, Ag nanoparticles (NPs) are subsequently biomineralized, endowing the protein assembly ability of p ‐nitrophenol hydrogenation. It is noteworthy that the Ag NPs‐protein assembly composite presents a 4.19 times higher activity than traditional hydrothermal synthesized Ag NPs because of the higher affinity with substrates. The composite also demonstrates good water stability and recyclability. This article provides a manipulative strategy to drive protein assembling and reveals the Ag‐protein assembly composite a potential biomaterial in the future.

摘要 蛋白质自组装的构建对于理解自然智慧和生产功能性生物材料越来越受到关注。目前的工作重点是新颖的驱动力、动态控制和功能化。在这项研究中，报道了由从头卷曲线圈驱动的蛋白质组装。通过精确设计卷曲线圈序列，成功构建了二聚体反平行卷曲线圈，并将其用作驱动螺旋蛋白质纳米结构的连接体。此外，银纳米颗粒（NP）随后被生物矿化，赋予对硝基苯酚氢化的蛋白质组装能力。值得注意的是，由于与底物的亲和力更高，Ag NPs-蛋白质组装复合物的活性比传统水热合成的Ag NPs高4.19倍。该复合材料还表现出良好的水稳定性和可回收性。本文提供了一种驱动蛋白质组装的操作策略，并揭示了银-蛋白质组装复合物是未来潜在的生物材料。