期刊
SMALL
卷 18, 期 10, 页码 -出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/smll.202106401
关键词
2D assembly; high-speed atomic force microscopy; Monte Carlo simulation; protein assembly; protein needle
类别
资金
- [JP20H01872]
- [21H01772]
- [JP18H05421]
- [JP18H05427]
- [21H00393]
- [20H04669]
The dynamic process of protein assembly is essential for highly ordered structures in biological systems. This study shows the control of the 2D assembly pattern of protein needles by regulating their tip-to-tip interactions. The findings provide a new strategy for constructing supramolecular protein architectures.
The dynamic process of formation of protein assemblies is essential to form highly ordered structures in biological systems. Advances in structural and synthetic biology have led to the construction of artificial protein assemblies. However, development of design strategies exploiting the anisotropic shape of building blocks of protein assemblies has not yet been achieved. Here, the 2D assembly pattern of protein needles (PNs) is controlled by regulating their tip-to-tip interactions. The PN is an anisotropic needle-shaped protein composed of beta-helix, foldon, and His-tag. Three different types of tip-modified PNs are designed by deleting the His-tag and foldon to change the protein-protein interactions. Observing their assembly by high-speed atomic force microscopy (HS-AFM) reveals that PN, His-tag deleted PN, and His-tag and foldon deleted PN form triangular lattices, the monomeric state with nematic order, and fiber assemblies, respectively, on a mica surface. Their assembly dynamics are observed by HS-AFM and analyzed by the theoretical models. Monte Carlo (MC) simulations indicate that the mica-PN interactions and the flexible and multipoint His-tag interactions cooperatively guide the formation of the triangular lattice. This work is expected to provide a new strategy for constructing supramolecular protein architectures by controlling directional interactions of anisotropic shaped proteins.
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