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231226s2023 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.2c03146
|2 doi
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|a eng
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|a Kikuchi, Kosuke
|e verfasserin
|4 aut
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|a Design of a Hierarchical Assembly at a Solid-Liquid Interface Using an Asymmetric Protein Needle
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|c 2023
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 15.02.2023
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|a Date Revised 15.03.2023
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a 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 His-tag. 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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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Proteins
|2 NLM
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|a Date, Koki
|e verfasserin
|4 aut
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|a Ueno, Takafumi
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 39(2023), 6 vom: 14. Feb., Seite 2389-2397
|w (DE-627)NLM098181009
|x 1520-5827
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|g volume:39
|g year:2023
|g number:6
|g day:14
|g month:02
|g pages:2389-2397
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|u http://dx.doi.org/10.1021/acs.langmuir.2c03146
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