Programmable biofilm-based materials from engineered curli nanofibres

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Programmable biofilm-based materials from engineered curli nanofibres

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Title: Programmable biofilm-based materials from engineered curli nanofibres
Author: Nguyen, Peter Q; Botyanszki, Zsofia; Tay, Pei Kun Richie; Joshi, Neel S.

Note: Order does not necessarily reflect citation order of authors.

Citation: Nguyen, Peter Q., Zsofia Botyanszki, Pei Kun R. Tay, and Neel S. Joshi. 2014. “Programmable Biofilm-Based Materials from Engineered Curli Nanofibres.” Nature Communications 5 (September 17): 4945. doi:10.1038/ncomms5945.
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Abstract: The significant role of biofilms in pathogenicity has spurred research into preventing their formation and promoting their disruption, resulting in overlooked opportunities to develop biofilms as a synthetic biological platform for self-assembling functional materials. Here we present Biofilm-Integrated Nanofiber Display (BIND) as a strategy for the molecular programming of the bacterial extracellular matrix material by genetically appending peptide domains to the amyloid protein ​CsgA, the dominant proteinaceous component in Escherichia coli biofilms. These engineered ​CsgA fusion proteins are successfully secreted and extracellularly self-assemble into amyloid nanofibre networks that retain the functions of the displayed peptide domains. We show the use of BIND to confer diverse artificial functions to the biofilm matrix, such as nanoparticle biotemplating, substrate adhesion, covalent immobilization of proteins or a combination thereof. BIND is a versatile nanobiotechnological platform for developing robust materials with programmable functions, demonstrating the potential of utilizing biofilms as large-scale designable biomaterials.
Published Version: doi:10.1038/ncomms5945
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:14350457
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