title: Programmable biofilm-based materials from engineered curli nanofibres.
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.
authors.affiliation: 1] School of Engineering and Applied Sciences, Harvard University, Cambridge, Massachusetts 02138, USA [2] Wyss Institute for Biologically Inspired Engineering, Harvard University, Cambridge, Massachusetts 02138, USA.
authors.forename: Peter Q
authors.initials: PQ
authors.lastname: Nguyen
authors.affiliation: 1] Wyss Institute for Biologically Inspired Engineering, Harvard University, Cambridge, Massachusetts 02138, USA [2] Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
authors.forename: Zsofia
authors.initials: Z
authors.lastname: Botyanszki
authors.affiliation: 1] School of Engineering and Applied Sciences, Harvard University, Cambridge, Massachusetts 02138, USA [2] Wyss Institute for Biologically Inspired Engineering, Harvard University, Cambridge, Massachusetts 02138, USA.
authors.forename: Pei Kun R
authors.initials: PK
authors.lastname: Tay
authors.affiliation: 1] School of Engineering and Applied Sciences, Harvard University, Cambridge, Massachusetts 02138, USA [2] Wyss Institute for Biologically Inspired Engineering, Harvard University, Cambridge, Massachusetts 02138, USA.
authors.forename: Neel S
authors.initials: NS
authors.lastname: Joshi
mesh_terms: D000682:Amyloid / Q000737:chemistry; D001672:Biocompatible Materials / Q000737:chemistry*; D018441:Biofilms; D004797:Enzyme-Linked Immunosorbent Assay; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry; D007150:Immunohistochemistry; D008422:Materials Testing; D053768:Metal Nanoparticles / Q000737:chemistry; D008855:Microscopy, Electron, Scanning; D046529:Microscopy, Electron, Transmission; D009154:Mutation; D057139:Nanofibers / Q000737:chemistry*; D036103:Nanotechnology; D010455:Peptides / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D012834:Silver / Q000737:chemistry; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013193:Stainless Steel; D013379:Substrate Specificity
chemical_list: D000682:Amyloid; D001672:Biocompatible Materials; D029968:Escherichia coli Proteins; D010455:Peptides; D011993:Recombinant Fusion Proteins; C489688:csgA protein, E coli; D013193:Stainless Steel; D012834:Silver