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Guanghua Zhao
China Agricultural University
Corresponding Author
ORCiD: https://orcid.org/0000-0001-8587-9680
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Although various artificial protein nanoarchitectures have been constructed, controlling conversion between protein assemblies with different dimensions has largely been unexplored. Here, we describe a simple, effective approach to regulate conversion between 0D protein nanomaterials and their 1D or 2D analogues by adjusting the geometric arrangement of dimeric protein building blocks. Thermotoga maritima ferritin (TmFtn) naturally occurs as a dimeric protein, twelve of which interact with each other in a head-to-side manner to generate 0D 24-meric protein nanocage in the presence of Ca2+. 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 conversion of the inherent salt-mediated 0D protein nanocage into 1D or 2D nanomaterials in response to multiple external stimuli. Thus, one kind of dimeric protein building block can generate three protein materials with different dimensions in a manner that highly resembles natural pentamer building blocks from viral capsids that form different protein assemblies.
Keywords
protein nanomaterials, protein assemblies
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There is NO Competing Interest.
This is a list of supplementary files associated with this preprint. Click to download.
- sourcedata.xlsx
Supplementary Figure 2, Supplementary Figure 5, Supplementary Figure 13 Supplementary Figure 6,
- SupportingInformation.docx
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See the published version of this preprint at Nature Communications.
This is a preprint, a preliminary version of a manuscript that has not completed peer review at a journal. Research Square does not conduct peer review prior to posting preprints. The posting of a preprint on this server should not be interpreted as an endorsement of its validity or suitability for dissemination as established information or for guiding clinical practice.
Learn more about In Review
Article
Guanghua Zhao
China Agricultural University
Corresponding Author
ORCiD: https://orcid.org/0000-0001-8587-9680
Badges
Prescreen
This manuscript passed our Prescreen assessment
Complete author information
Appropriate declaration statements
Potential risks to human health
Prescreen
Peer Review Timeline
CURRENT STATUS: Published
View the published article at Nature Communications.
Version 1
Posted 11 Feb, 2021
Metrics
Comments: 0
PDF Downloads: ...
HTML Views: ...
License:
This work is licensed under a CC BY 4.0 License. Read Full License
View the published article at Nature Communications.
Although various artificial protein nanoarchitectures have been constructed, controlling conversion between protein assemblies with different dimensions has largely been unexplored. Here, we describe a simple, effective approach to regulate conversion between 0D protein nanomaterials and their 1D or 2D analogues by adjusting the geometric arrangement of dimeric protein building blocks. Thermotoga maritima ferritin (TmFtn) naturally occurs as a dimeric protein, twelve of which interact with each other in a head-to-side manner to generate 0D 24-meric protein nanocage in the presence of Ca2+. 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 conversion of the inherent salt-mediated 0D protein nanocage into 1D or 2D nanomaterials in response to multiple external stimuli. Thus, one kind of dimeric protein building block can generate three protein materials with different dimensions in a manner that highly resembles natural pentamer building blocks from viral capsids that form different protein assemblies.
Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
Figure 6
Figure 7
Figure 8
There is NO Competing Interest.
This is a list of supplementary files associated with this preprint. Click to download.
- sourcedata.xlsx
Supplementary Figure 2, Supplementary Figure 5, Supplementary Figure 13 Supplementary Figure 6,
- SupportingInformation.docx
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