Book of Abstracts: Albany 2011

category image Albany 2011
Conversation 17
June 14-18 2011
©Adenine Press (2010)

Amyloid Fibrils Captured inside Twenty-Helix DNA Nanotubes

Amyloid fibrils are ordered and insoluble protein aggregates that were originally found associated with neurodegenerative diseases such as Alzheimer’s disease. They share a common core structure, an elongated stack of β-strands, perpendicular to the fibril axis (1). These molecules have rod-like structures with a very high persistence length and also exhibit high thermal and chemical stability (2). Short synthetic non-disease-related peptides can induce fibril in vitro (3). There are increasing observations on how these fibrils form providing more opportunities to design novel functionalized motifs (2,4). They offer great potential as self-assembling materials for nanotechnology and bionanotechnology (5). However, they require the development of new methods to manipulate fibrils into organized arrangements.

DNA nanotubes with a cylindrical structure can be used as sheaths around rod-like molecules in biological systems and nanotechnology (6). In this work, we take advantage of the powerful features of DNA to form nanotubes to capture amyloid fibrils formed from a short peptide fragment of protein transthyretin (TTR105-115). The scaffolded DNA origami method is used to form DNA nanotubes, using M13mp18 as a scaffold strand with more than 170 staple strands, designed to have enough space for capturing the fibrils inside. We expect to be able to organize these bio-inspired materials onto predefined surfaces via DNA-DNA interactions. We report the results of sheathing experiments that are evaluated by atomic force microscopy.


  1. J. F. Smith, T. P. Knowles, C. M. Dobson, C. E. MacPhee and M. E. Welland, Proc. Natl. Acad. Sci. 103, 15806-15811 (2006).
  2. C. E. MacPhee and C. M. Dobson, J. Am. Chem. Soc. 122, 12707-12713 (2000).
  3. C. M. Dobson, Trends Biochem. Sci. 24, 329-332 (1999).
  4. S. L. Gras, A. K. Tickler, A. M. Squires, G. L. Devlin, M. A. Horton, C. M. Dobson, and C. E. MacPhee, Biomaterials 29, 1553-1562 (2008).
  5. S. L. Gras, Aust. J. Chem. 60, 333-342 (2007).
  6. A. Kuzuya, R. Wang, R. Sha, N. C. Seeman, Nano Lett. 7, 1757-1763 (2007).

Anuttara Udomprasert 1
Marie Bongiovanni2, 3
Ruojie Sha1
William B. Sherman4
Monica Menzenski1
Paramjit Arora1
James W. Canary1
Sally L. Gras2, 3
and Nadrian C. Seeman1

1 Department of Chemistry
New York University
New York NY 10003, USA
2 Department of Chemical and Biomolecular Engineering
The University of Melbourne
Parkville VIC 3010, Australia
3 The Bio21 Molecular Science and Biotechnology Institute
The University of Melbourne
Parkville VIC 3010, Australia
4 Brookhaven National Laboratory
Upton NY11973, USA

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