Petkova, A. T. ; Buntkowsky, G. ; Dyda, F. ; Leapman, R. D. ; Yau, W. M. ; Tycko, R. (2004)
Solid state NMR reveals a pH-dependent antiparallel beta-sheet registry in fibrils formed by a beta-amyloid peptide.
In: Journal of Molecular Biology, 335 (1)
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
We report solid state nuclear magnetic resonance (NMR) measurements that probe the supramolecular organization of beta-sheets in the cross-beta motif of amyloid fibrils formed by residues 11-25 of the beta-amyloid peptide associated with Alzheimer's disease (Abeta(11-25)). Fibrils were prepared at pH 7.4 and pH 2.4. The solid state NMR data indicate that the central hydrophobic segment of Abeta(11-25) (sequence LVFFA) adopts a beta-strand conformation and participates in antiparallel beta-sheets at both pH values, but that the registry of intermolecular hydrogen bonds is pH-dependent. Moreover, both registries determined for Abeta(11-25) fibrils are different from the hydrogen bond registry in the antiparallel beta-sheets of Abeta(16-22) fibrils at pH 7.4 determined in earlier solid state NMR studies. In all three cases, the hydrogen bond registry is highly ordered, with no detectable "registry-shift" defects. These results suggest that the supramolecular organization of beta-sheets in amyloid fibrils is determined by a sensitive balance of multiple side-chain-side-chain interactions. Recent structural models for Abeta(11-25) fibrils based on X-ray fiber diffraction data are inconsistent with the solid state NMR data at both pH values. (C) 2003 Elsevier Ltd. All rights reserved.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2004 |
| Autor(en): | Petkova, A. T. ; Buntkowsky, G. ; Dyda, F. ; Leapman, R. D. ; Yau, W. M. ; Tycko, R. |
| Art des Eintrags: | Bibliographie |
| Titel: | Solid state NMR reveals a pH-dependent antiparallel beta-sheet registry in fibrils formed by a beta-amyloid peptide |
| Sprache: | Englisch |
| Publikationsjahr: | 2004 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Journal of Molecular Biology |
| Jahrgang/Volume einer Zeitschrift: | 335 |
| (Heft-)Nummer: | 1 |
| URL / URN: | http://apps.webofknowledge.com/full_record.do?product=WOS&se... |
| Kurzbeschreibung (Abstract): | We report solid state nuclear magnetic resonance (NMR) measurements that probe the supramolecular organization of beta-sheets in the cross-beta motif of amyloid fibrils formed by residues 11-25 of the beta-amyloid peptide associated with Alzheimer's disease (Abeta(11-25)). Fibrils were prepared at pH 7.4 and pH 2.4. The solid state NMR data indicate that the central hydrophobic segment of Abeta(11-25) (sequence LVFFA) adopts a beta-strand conformation and participates in antiparallel beta-sheets at both pH values, but that the registry of intermolecular hydrogen bonds is pH-dependent. Moreover, both registries determined for Abeta(11-25) fibrils are different from the hydrogen bond registry in the antiparallel beta-sheets of Abeta(16-22) fibrils at pH 7.4 determined in earlier solid state NMR studies. In all three cases, the hydrogen bond registry is highly ordered, with no detectable "registry-shift" defects. These results suggest that the supramolecular organization of beta-sheets in amyloid fibrils is determined by a sensitive balance of multiple side-chain-side-chain interactions. Recent structural models for Abeta(11-25) fibrils based on X-ray fiber diffraction data are inconsistent with the solid state NMR data at both pH values. (C) 2003 Elsevier Ltd. All rights reserved. |
| Freie Schlagworte: | amyloid fibrils hydrogen bond registry antiparallel beta-sheets solid state nmr alzheimer's disease nuclear-magnetic-resonance side-chain interactions c-13 chemical-shifts x-ray-diffraction supramolecular structure structural constraints rotational-echo c-alpha conformation parallel |
| Zusätzliche Informationen: | 761BP Times Cited:205 Cited References Count:49 |
| Fachbereich(e)/-gebiet(e): | 07 Fachbereich Chemie 07 Fachbereich Chemie > Eduard Zintl-Institut > Fachgebiet Physikalische Chemie |
| Hinterlegungsdatum: | 27 Okt 2014 20:47 |
| Letzte Änderung: | 29 Mai 2019 10:50 |
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