Premium
Protein Self‐Assembly Driven by De Novo Coiled Coils and Constructing Ag Nanoparticle‐Protein Assembly Composite with High Catalytic Activity
Author(s) -
Qiao Shanpeng,
Wang Ruidi,
Yan Tengfei,
Li Xiumei,
Zhao Linlu,
Zhang Xin,
Fan Xiaotong,
Wang Tingting,
Liu Yao,
Hou Chunxi,
Luo Quan,
Xu Jiayu,
Liu Junqiu
Publication year - 2018
Publication title -
particle and particle systems characterization
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.877
H-Index - 56
eISSN - 1521-4117
pISSN - 0934-0866
DOI - 10.1002/ppsc.201700436
Subject(s) - antiparallel (mathematics) , coiled coil , linker , nanoparticle , biomaterial , composite number , nanotechnology , materials science , protein engineering , surface modification , self assembly , streptavidin , chemistry , chemical engineering , biochemistry , enzyme , engineering , biotin , computer science , composite material , quantum mechanics , magnetic field , operating system , physics
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.