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Hydrogen Bonding in Alzheimer’s Amyloid-β Fibrils Probed by 15N{17O} REAPDOR Solid-State NMR Spectroscopy

Authors


  • We acknowledge Dr. A. Kukol for preparation of Fmoc-Val(17O), Dr. S. Afonin for electrospray mass-spectrometry analysis of peptides, Dr. A. T. Petkova and Dr. R. Tycko for seeds of Aβ(11–25) (pH 2.4) fibrils, reagents and access to the peptide synthesizer at LCP, NIDDK, NIH, where Aβ(11–25) was synthesized, and I. Portman at the Electron Microscopy Facility, School of Life Sciences, University of Warwick (Wellcome Trust reference 055663/Z/98/Z) for technical support. This work was supported by the Foundation in memory of J.C. and Seth M. Kempe and the Alzheimer’s Foundation of Sweden (funds for a peptide synthesizer and HPLC at LTU, Sweden, reagents for synthesis of Aβ(16–22) and stipends for A.V.F.). The UK 850 MHz solid-state NMR Facility used in this research was funded by EPSRC and BBSRC, as well as the University of Warwick including partial funding through Birmingham Science City Advanced Materials Project 1 and 2 supported by Advantage West Midlands (AWM) and the European Regional Development Fund (ERDF).

Abstract

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Nach selektiver Markierung mit 17O und 15N wurden mithilfe von 15N{17O}-REAPDOR-NMR-Spektroskopie intermolekulare C[DOUBLE BOND]17O⋅⋅⋅H[BOND]15N-Wasserstoffbrücken in Ac-Aβ(16–22)-NH2- (siehe Schema) und Aβ(11–25)-Amyloidfibrillen untersucht, die mit der Alzheimer-Krankheit in Verbindung gebracht werden. Die Methode, die eine Bestätigung für die Struktur dieser Fibrillen lieferte, könnte auch im Zusammenhang mit anderen biologischen Proben nützlich sein.

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