Protein interface redesign facilitates the transformation of nanocage building blocks to 1D and 2D nanomaterials
Xiaorong Zhang,
Yu Liu,
Bowen Zheng,
Jiachen Zang,
Chenyan Lv,
Tuo Zhang (),
Hongfei Wang and
Guanghua Zhao ()
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Xiaorong Zhang: Beijing Key Laboratory of Functional Food from Plant Resources
Yu Liu: Beijing Key Laboratory of Functional Food from Plant Resources
Bowen Zheng: Beijing Key Laboratory of Functional Food from Plant Resources
Jiachen Zang: Beijing Key Laboratory of Functional Food from Plant Resources
Chenyan Lv: Beijing Key Laboratory of Functional Food from Plant Resources
Tuo Zhang: Beijing Key Laboratory of Functional Food from Plant Resources
Hongfei Wang: Shanxi University
Guanghua Zhao: Beijing Key Laboratory of Functional Food from Plant Resources
Nature Communications, 2021, vol. 12, issue 1, 1-11
Abstract:
Abstract Although various artificial protein nanoarchitectures have been constructed, controlling the transformation between different protein assemblies has largely been unexplored. Here, we describe an approach to realize the self-assembly transformation of dimeric building blocks by adjusting their geometric arrangement. Thermotoga maritima ferritin (TmFtn) naturally occurs as a dimer; twelve of these dimers interact with each other in a head-to-side manner to generate 24-meric hollow protein nanocage in the presence of Ca2+ or PEG. By tuning two contiguous dimeric proteins to interact in a fully or partially side-by-side fashion through protein interface redesign, we can render the self-assembly transformation of such dimeric building blocks from the protein nanocage to filament, nanorod and nanoribbon in response to multiple external stimuli. We show similar dimeric protein building blocks can generate three kinds of protein materials in a manner that highly resembles natural pentamer building blocks from viral capsids that form different protein assemblies.
Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-25199-x
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DOI: 10.1038/s41467-021-25199-x
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