Strong underwater adhesives made by self-assembling multi-protein nanofibres View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2014-10

AUTHORS

Chao Zhong, Thomas Gurry, Allen A. Cheng, Jordan Downey, Zhengtao Deng, Collin M. Stultz, Timothy K. Lu

ABSTRACT

Many natural underwater adhesives harness hierarchically assembled amyloid nanostructures to achieve strong and robust interfacial adhesion under dynamic and turbulent environments. Despite recent advances, our understanding of the molecular design, self-assembly and structure-function relationships of these natural amyloid fibres remains limited. Thus, designing biomimetic amyloid-based adhesives remains challenging. Here, we report strong and multi-functional underwater adhesives obtained from fusing mussel foot proteins (Mfps) of Mytilus galloprovincialis with CsgA proteins, the major subunit of Escherichia coli amyloid curli fibres. These hybrid molecular materials hierarchically self-assemble into higher-order structures, in which, according to molecular dynamics simulations, disordered adhesive Mfp domains are exposed on the exterior of amyloid cores formed by CsgA. Our fibres have an underwater adhesion energy approaching 20.9 mJ m(-2), which is 1.5 times greater than the maximum of bio-inspired and bio-derived protein-based underwater adhesives reported thus far. Moreover, they outperform Mfps or curli fibres taken on their own and exhibit better tolerance to auto-oxidation than Mfps at pH ≥ 7.0. More... »

PAGES

858-866

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nnano.2014.199

DOI

http://dx.doi.org/10.1038/nnano.2014.199

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1033392974

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/25240674


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