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Close, W.* ; Neumann, M.* ; Schmidt, A.* ; Hora, M. ; Annamalai, K.* ; Schmidt, M.* ; Reif, B. ; Schmidt, V.* ; Grigorieff, N.* ; Fändrich, M.*

Physical basis of amyloid fibril polymorphism.

Nat. Commun. 9:699 (2018)
Verlagsversion Forschungsdaten DOI
Open Access Gold
Creative Commons Lizenzvertrag
Polymorphism is a key feature of amyloid fibril structures but it remains challenging to explain these variations for a particular sample. Here, we report electron cryomicroscopy-based reconstructions from different fibril morphologies formed by a peptide fragment from an amyloidogenic immunoglobulin light chain. The observed fibril morphologies vary in the number and cross-sectional arrangement of a structurally conserved building block. A comparison with the theoretically possible constellations reveals the experimentally observed spectrum of fibril morphologies to be governed by opposing sets of forces that primarily arise from the beta-sheet twist, as well as peptide-peptide interactions within the fibril cross-section. Our results provide a framework for rationalizing and predicting the structure and polymorphism of cross-beta fibrils, and suggest that a small number of physical parameters control the observed fibril architectures.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Solid-state Nmr; Cryo-em; In-vivo; Beta; A-beta(1-40); Aggregation; Backbone; Sequence; Reveals; Disease
ISSN (print) / ISBN 2041-1723
e-ISSN 2041-1723
Zeitschrift Nature Communications
Quellenangaben Band: 9, Heft: 1, Seiten: , Artikelnummer: 699 Supplement: ,
Verlag Nature Publishing Group
Verlagsort London
Begutachtungsstatus Peer reviewed