We acknowledge support from the Danish National Research Foundation, the Villum-Kann Rasmussen Foundation, the Danish Center for Scientific Computing, the Danish Natural Science Research Council, and the Danish Biotechnological Instrument Centre.
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Communication
Unique Identification of Supramolecular Structures in Amyloid Fibrils by Solid-State NMR Spectroscopy†
Article first published online: 7 JAN 2009
DOI: 10.1002/anie.200804198
Copyright © 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Nielsen, Jakob T., Bjerring, M., Jeppesen, Martin D., Pedersen, Ronnie O., Pedersen, Jan M., Hein, Kim L., Vosegaard, T., Skrydstrup, T., Otzen, Daniel E. and Nielsen, Niels C. (2009), Unique Identification of Supramolecular Structures in Amyloid Fibrils by Solid-State NMR Spectroscopy. Angew. Chem. Int. Ed., 48: 2118–2121. doi: 10.1002/anie.200804198
- †
Publication History
- Issue published online: 3 MAR 2009
- Article first published online: 7 JAN 2009
- Manuscript Revised: 31 OCT 2008
- Manuscript Received: 25 AUG 2008
Funded by
- Danish National Research Foundation
- Villum-Kann Rasmussen Foundation
- Danish Center for Scientific Computing
- Danish Natural Science Research Council
- Danish Biotechnological Instrument Centre
Keywords:
- amyloid fibrils;
- NMR spectroscopy;
- peptides;
- supramolecular chemistry
Abstract
The fibril structure formed by the amyloidogenic fragment SNNFGAILSS of the human islet amyloid polypeptide (hIAPP) is determined with 0.52 Å resolution. Symmetry information contained in the easily obtainable resonance assignments from solid-state NMR spectra (see picture), along with long-range constraints, can be applied to uniquely identify the supramolecular organization of fibrils.