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Design of a Hierarchical Assembly at a Solid-Liquid Interface Using an Asymmetric Protein Needle
Kosuke Kikuchi1, Koki Date1, Takafumi Ueno1,2
1School of Life Science and Technology, Tokyo Institute of Technology, 4259-B-55, Nagatsuta-cho, Midori-ku, Yokohama 226-8501, Japan.
Langmuir : the ACS Journal of Surfaces and Colloids
|February 3, 2023
Summary
Researchers engineered hierarchical protein assemblies using anisotropic gene product 5 (gp5) protein needles. This novel approach bypasses symmetry constraints, enabling complex structures through distinct interaction sites.
Area of Science:
- Protein engineering
- Biophysics
- Materials science
Background:
- Hierarchical protein assembly design is complex, requiring atomic precision.
- Symmetry-based strategies limit resulting protein assembly structures.
Purpose of the Study:
- To construct a hierarchical protein assembly using anisotropic protein needles.
- To explore novel protein-protein interaction strategies beyond symmetry.
Main Methods:
- Utilized anisotropic gene product 5 (gp5) protein from bacteriophage T4 with a C-terminal hexahistidine-tag (His-tag).
- Employed high-speed atomic force microscopy (HS-AFM) for real-time surface imaging and analysis.
Main Results:
- gp5_CHis formed tetrameric clusters via its N-terminal head on mica.
- These clusters self-assembled into a network-like monolayer via the C-terminal His-tag.
- HS-AFM confirmed a non-crystalline, network structure.
Conclusions:
- Structural anisotropy provides a new paradigm for hierarchical protein assembly.
- This method expands the available tools for designing complex protein structures.
