Journal
NATURE COMMUNICATIONS
Volume 9, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-018-03164-5
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Funding
- National Institutes of Health [P01 GM62580]
- Landesgraduiertenforderungsgesetzes Baden-Wurttemberg
- German Federal Ministry of Education and Research (GERAMY-German consortium for systemic light chain (AL) amyloidosis) [01GM1107]
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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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