Journal article
Amyloid fibrils nucleated and organized by DNA origami constructions
A Udomprasert, MN Bongiovanni, R Sha, WB Sherman, T Wang, PS Arora, JW Canary, SL Gras, NC Seeman
Nature Nanotechnology | Published : 2014
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 2-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 ..
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Awarded by National Science Foundation
Funding Acknowledgements
This research was supported by the following grants to N.C.S.: grant no. GM-29554 from the National Institute of General Medical Sciences, grants nos CMMI-1120890 and CCF-1117210 from the National Science Foundation, MURI W911NF-11-1-0024 from the Army Research Office, and grants nos N000141110729 and N000140911118 from the Office of Naval Research. M.N.B. was supported by an Australian Nanotechnology Network Overseas Travel Fellowship, a Melbourne Abroad Travelling Scholarship and the Bio21 Institute. S.L.G. and M.N.B. were supported by the Particulate Fluids Processing Centre and S.L.G. by the ARC Dairy Innovation Hub. Part of this research was carried out at the Macromolecular Crystallography beamline at the Australian Synchrotron, Victoria, Australia. Research was carried out in part at the Center for Functional Nanomaterials, Brookhaven National Laboratory, which is supported by the US Department of Energy, Office of Basic Energy Sciences (contract no. DE-AC02-98CH10886).