Dynamic Behavior of Cargo Proteins Regulated by Linker Peptides on a Protein Needle Scaffold

Nguyễn, Quốc Nhật; Kikuchi, K.; Kojima, Mariko; Ueno, Takafumi

doi:10.1246/cl.210599

Cited by 2 publications

(1 citation statement)

References 34 publications

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“…HS-AFM measurements were performed in the tapping mode using NanoExplore (RIBM) as described previously. ,, A small cantilever (BL-AC10DS, Olympus) with a spring constant of ∼0.2 N m –1 , a mechanical resonant frequency of 0.40–0.45 MHz, and a quality factor of ∼2 was used. An amorphous carbon tip was fabricated on the original cantilever tip by electron beam deposition (EBD), followed by sharpening by plasma etching.…”

Section: Methodsmentioning

confidence: 99%

Design of a Hierarchical Assembly at a Solid–Liquid Interface Using an Asymmetric Protein Needle

2023

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Design and control of processes for a hierarchical assembly of proteins remain challenging because it requires consideration of design principles with atomic-level accuracy. Previous studies have adopted symmetry-based strategies to minimize the complexity of protein−protein interactions and this has placed constraints on the structures of the resulting protein assemblies. In the present work, we used an anisotropic-shaped protein needle, gene product 5 (gp5) from bacteriophage T4 with a C-terminal hexahistidine-tag (His-tag) (gp5_CHis), to construct a hierarchical assembly with two distinct protein−protein interaction sites. High-speed atomic force microscopy (HS-AFM) measurements reveal that it forms unique tetrameric clusters through its N-terminal head on a mica surface. The clusters further self-assemble into a monolayer through the C-terminal Histag. The HS-AFM images and displacement analyses show that the monolayer is a network-like structure rather than a crystalline lattice. Our results expand the toolbox for constructing hierarchical protein assemblies based on structural anisotropy.

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Section: Methodsmentioning

confidence: 99%

Design of a Hierarchical Assembly at a Solid–Liquid Interface Using an Asymmetric Protein Needle

2023

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A Protein Needle Facilitates Encapsulation of Target Proteins via In-Cell Protein Crystallization

et al. 2023

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We have established a new method for encapsulating superfold green fluorescent protein (sfGFP) into polyhedra crystal (PhC) with high efficiency using a protein needle (PN). H1-sfGFP-PN, in which PN is fused to the C-terminus of H1-sfGFP, exhibits a 55-fold increase in encapsulation of sfGFP relative to H1-sfGFP with the improvement provided by the synergistic effects of the H1-helix, PN, and the His-tag at the C-terminus of PN. This method is expected to provide useful materials based on encapsulation of various functional proteins.

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Dynamic Behavior of Cargo Proteins Regulated by Linker Peptides on a Protein Needle Scaffold

Cited by 2 publications

References 34 publications

Design of a Hierarchical Assembly at a Solid–Liquid Interface Using an Asymmetric Protein Needle

Design of a Hierarchical Assembly at a Solid–Liquid Interface Using an Asymmetric Protein Needle

A Protein Needle Facilitates Encapsulation of Target Proteins via In-Cell Protein Crystallization

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