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

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.