title: Amyloid fibrils nucleated and organized by DNA origami constructions.
abstract: Amyloid fibrils are ordered, insoluble protein aggregates that are associated with neurodegenerative conditions such as Alzheimer's disease. The fibrils have a common rod-like core structure, formed from an elongated stack of β-strands, and have a rigidity similar to that of silk (Young's modulus of 0.2-14 GPa). They also exhibit high thermal and chemical stability and can be assembled in vitro from short synthetic non-disease-related peptides. As a result, they are of significant interest in the development of self-assembled materials for bionanotechnology applications. Synthetic DNA molecules have previously been used to form intricate structures and organize other materials such as metal nanoparticles and could in principle be used to nucleate and organize amyloid fibrils. Here, we show that DNA origami nanotubes can sheathe amyloid fibrils formed within them. The fibrils are built by modifying the synthetic peptide fragment corresponding to residues 105-115 of the amyloidogenic protein transthyretin and a DNA origami construct is used to form 20-helix DNA nanotubes with sufficient space for the fibrils inside. Once formed, the fibril-filled nanotubes can be organized onto predefined two-dimensional platforms via DNA-DNA hybridization interactions.
authors.affiliation: Department of Chemistry, New York University, New York, New York 10003, USA.
authors.forename: Anuttara
authors.initials: A
authors.lastname: Udomprasert
authors.affiliation: 1] Department of Chemical and Biomolecular Engineering, The University of Melbourne, Parkville, Victoria 3010, Australia [2] Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, Victoria 3010, Australia.
authors.forename: Marie N
authors.initials: MN
authors.lastname: Bongiovanni
authors.affiliation: Department of Chemistry, New York University, New York, New York 10003, USA.
authors.forename: Ruojie
authors.initials: R
authors.lastname: Sha
authors.affiliation: Bard High School Early College-Queens, 30-20 Thomson Avenue, Queens, New York 11101, USA.
authors.forename: William B
authors.initials: WB
authors.lastname: Sherman
authors.affiliation: Department of Chemistry, New York University, New York, New York 10003, USA.
authors.forename: Tong
authors.initials: T
authors.lastname: Wang
authors.affiliation: Department of Chemistry, New York University, New York, New York 10003, USA.
authors.forename: Paramjit S
authors.initials: PS
authors.lastname: Arora
authors.affiliation: Department of Chemistry, New York University, New York, New York 10003, USA.
authors.forename: James W
authors.initials: JW
authors.lastname: Canary
authors.affiliation: 1] Department of Chemical and Biomolecular Engineering, The University of Melbourne, Parkville, Victoria 3010, Australia [2] Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, Victoria 3010, Australia.
authors.forename: Sally L
authors.initials: SL
authors.lastname: Gras
authors.affiliation: Department of Chemistry, New York University, New York, New York 10003, USA.
authors.forename: Nadrian C
authors.initials: NC
authors.lastname: Seeman
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D004247:DNA / Q000737:chemistry*; D006801:Humans; D053768:Metal Nanoparticles / Q000737:chemistry*; D043942:Nanotubes / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D010957:Plasmids; D011228:Prealbumin / Q000737:chemistry*; D017433:Protein Structure, Secondary; D047011:Silk / Q000737:chemistry
chemical_list: D000682:Amyloid; D010455:Peptides; D011228:Prealbumin; D047011:Silk; D004247:DNA