Spider-silk inspired polymeric networks by harnessing the mechanical potential of β-sheets through network guided assembly.
- Publisher:
- NATURE PUBLISHING GROUP
- Publication Type:
- Journal Article
- Citation:
- Nature communications, 2020, 11, (1)
- Issue Date:
- 2020-04-02
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Field | Value | Language |
---|---|---|
dc.contributor.author | Chan, NJ-A | |
dc.contributor.author | Gu, D | |
dc.contributor.author | Tan, S | |
dc.contributor.author |
Fu, Q https://orcid.org/0000-0002-4012-330X |
|
dc.contributor.author | Pattison, TG | |
dc.contributor.author | O'Connor, AJ | |
dc.contributor.author | Qiao, GG | |
dc.date.accessioned | 2021-03-11T01:36:39Z | |
dc.date.available | 2020-02-24 | |
dc.date.available | 2021-03-11T01:36:39Z | |
dc.date.issued | 2020-04-02 | |
dc.identifier.citation | Nature communications, 2020, 11, (1) | |
dc.identifier.issn | 2041-1723 | |
dc.identifier.issn | 2041-1723 | |
dc.identifier.uri | http://hdl.handle.net/10453/147025 | |
dc.description.abstract | The high toughness of natural spider-silk is attributed to their unique β-sheet secondary structures. However, the preparation of mechanically strong β-sheet rich materials remains a significant challenge due to challenges involved in processing the polymers/proteins, and managing the assembly of the hydrophobic residues. Inspired by spider-silk, our approach effectively utilizes the superior mechanical toughness and stability afforded by localised β-sheet domains within an amorphous network. Using a grafting-from polymerisation approach within an amorphous hydrophilic network allows for spatially controlled growth of poly(valine) and poly(valine-r-glycine) as β-sheet forming polypeptides via N-carboxyanhydride ring opening polymerisation. The resulting continuous β-sheet nanocrystal network exhibits improved compressive strength and stiffness over the initial network lacking β-sheets of up to 30 MPa (300 times greater than the initial network) and 6 MPa (100 times greater than the initial network) respectively. The network demonstrates improved resistance to strong acid, base and protein denaturants over 28 days. | |
dc.format | Electronic | |
dc.language | eng | |
dc.publisher | NATURE PUBLISHING GROUP | |
dc.relation.ispartof | Nature communications | |
dc.relation.isbasedon | 10.1038/s41467-020-15312-x | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.subject.mesh | Animals | |
dc.subject.mesh | Biomechanical Phenomena | |
dc.subject.mesh | Hydrophobic and Hydrophilic Interactions | |
dc.subject.mesh | Polymers | |
dc.subject.mesh | Protein Conformation, beta-Strand | |
dc.subject.mesh | Silk | |
dc.subject.mesh | Spiders | |
dc.subject.mesh | Animals | |
dc.subject.mesh | Spiders | |
dc.subject.mesh | Polymers | |
dc.subject.mesh | Silk | |
dc.subject.mesh | Hydrophobic and Hydrophilic Interactions | |
dc.subject.mesh | Biomechanical Phenomena | |
dc.subject.mesh | Protein Conformation, beta-Strand | |
dc.subject.mesh | Animals | |
dc.subject.mesh | Biomechanical Phenomena | |
dc.subject.mesh | Hydrophobic and Hydrophilic Interactions | |
dc.subject.mesh | Polymers | |
dc.subject.mesh | Protein Conformation, beta-Strand | |
dc.subject.mesh | Silk | |
dc.subject.mesh | Spiders | |
dc.title | Spider-silk inspired polymeric networks by harnessing the mechanical potential of β-sheets through network guided assembly. | |
dc.type | Journal Article | |
utslib.citation.volume | 11 | |
utslib.location.activity | England | |
pubs.organisational-group | /University of Technology Sydney | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Engineering and Information Technology | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Engineering and Information Technology/School of Civil and Environmental Engineering | |
pubs.organisational-group | /University of Technology Sydney/Strength - CTWW - Centre for Technology in Water and Wastewater Treatment | |
utslib.copyright.status | open_access | * |
pubs.consider-herdc | false | |
dc.date.updated | 2021-03-11T01:36:29Z | |
pubs.issue | 1 | |
pubs.publication-status | Published | |
pubs.volume | 11 | |
utslib.citation.issue | 1 |
Abstract:
The high toughness of natural spider-silk is attributed to their unique β-sheet secondary structures. However, the preparation of mechanically strong β-sheet rich materials remains a significant challenge due to challenges involved in processing the polymers/proteins, and managing the assembly of the hydrophobic residues. Inspired by spider-silk, our approach effectively utilizes the superior mechanical toughness and stability afforded by localised β-sheet domains within an amorphous network. Using a grafting-from polymerisation approach within an amorphous hydrophilic network allows for spatially controlled growth of poly(valine) and poly(valine-r-glycine) as β-sheet forming polypeptides via N-carboxyanhydride ring opening polymerisation. The resulting continuous β-sheet nanocrystal network exhibits improved compressive strength and stiffness over the initial network lacking β-sheets of up to 30 MPa (300 times greater than the initial network) and 6 MPa (100 times greater than the initial network) respectively. The network demonstrates improved resistance to strong acid, base and protein denaturants over 28 days.
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