Physical basis of amyloid fibril polymorphism

William Close; Matthias Neumann; Andreas Schmidt; Manuel Hora; Karthikeyan Annamalai; Matthias Schmidt; Bernd Reif; Volker Schmidt; Nikolaus Grigorieff; Marcus Fändrich

doi:10.1038/s41467-018-03164-5

Nature Communications (Feb 2018)

Physical basis of amyloid fibril polymorphism

William Close,
Matthias Neumann,
Andreas Schmidt,
Manuel Hora,
Karthikeyan Annamalai,
Matthias Schmidt,
Bernd Reif,
Volker Schmidt,
Nikolaus Grigorieff,
Marcus Fändrich

Affiliations

William Close: Institute of Protein Biochemistry, Ulm University
Matthias Neumann: Institute of Stochastics, Ulm University
Andreas Schmidt: Institute of Protein Biochemistry, Ulm University
Manuel Hora: Institute for Structural Biology, Helmholtz Zentrum München
Karthikeyan Annamalai: Institute of Protein Biochemistry, Ulm University
Matthias Schmidt: Institute of Protein Biochemistry, Ulm University
Bernd Reif: Institute for Structural Biology, Helmholtz Zentrum München
Volker Schmidt: Institute of Stochastics, Ulm University
Nikolaus Grigorieff: Janelia Research Campus, Howard Hughes Medical Institute
Marcus Fändrich: Institute of Protein Biochemistry, Ulm University

DOI: https://doi.org/10.1038/s41467-018-03164-5
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 7

Abstract

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Amyloid fibril structures can display polymorphism. Here the authors reveal the cryo-EM structures of several different fibril morphologies of a peptide derived from an amyloidogenic immunoglobulin light chain and present a mathematical analysis of physical factors that influence fibril polymorphism.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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