Abstract
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 β-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-β fibrils, and suggest that a small number of physical parameters control the observed fibril architectures.
Originalsprache | englisch |
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Aufsatznummer | 699 |
Fachzeitschrift | Nature Communications |
Jahrgang | 9 |
Ausgabenummer | 1 |
DOIs | |
Publikationsstatus | Veröffentlicht - 1 Dez. 2018 |
Extern publiziert | Ja |
ASJC Scopus subject areas
- Allgemeine Chemie
- Allgemeine Biochemie, Genetik und Molekularbiologie
- Allgemeine Physik und Astronomie