Physical basis of amyloid fibril polymorphism

William Close, Matthias Neumann, Andreas Schmidt, Manuel Hora, Karthikeyan Annamalai, Matthias Schmidt, Bernd Reif, Volker Schmidt, Nikolaus Grigorieff () and Marcus Fändrich ()
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William Close: Ulm University
Matthias Neumann: Ulm University
Andreas Schmidt: Ulm University
Manuel Hora: Helmholtz Zentrum München
Karthikeyan Annamalai: Ulm University
Matthias Schmidt: Ulm University
Bernd Reif: Helmholtz Zentrum München
Volker Schmidt: Ulm University
Nikolaus Grigorieff: Howard Hughes Medical Institute
Marcus Fändrich: Ulm University

Nature Communications, 2018, vol. 9, issue 1, 1-7

Abstract: 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.

Date: 2018
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-03164-5

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DOI: 10.1038/s41467-018-03164-5

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