Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy

Theint Theint; Philippe S. Nadaud; Darryl Aucoin; Jonathan J. Helmus; Simon P. Pondaven; Krystyna Surewicz; Witold K. Surewicz; Christopher P. Jaroniec

doi:10.1038/s41467-017-00794-z

Nature Communications (Sep 2017)

Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy

Theint Theint,
Philippe S. Nadaud,
Darryl Aucoin,
Jonathan J. Helmus,
Simon P. Pondaven,
Krystyna Surewicz,
Witold K. Surewicz,
Christopher P. Jaroniec

Affiliations

Theint Theint: Department of Chemistry and Biochemistry, The Ohio State University
Philippe S. Nadaud: Department of Chemistry and Biochemistry, The Ohio State University
Darryl Aucoin: Department of Chemistry and Biochemistry, The Ohio State University
Jonathan J. Helmus: Department of Chemistry and Biochemistry, The Ohio State University
Simon P. Pondaven: Department of Chemistry and Biochemistry, The Ohio State University
Krystyna Surewicz: Department of Physiology and Biophysics, Case Western Reserve University
Witold K. Surewicz: Department of Physiology and Biophysics, Case Western Reserve University
Christopher P. Jaroniec: Department of Chemistry and Biochemistry, The Ohio State University

DOI: https://doi.org/10.1038/s41467-017-00794-z
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 10

Abstract

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Prion diseases can be transmitted across species. Here the authors use solid-state NMR to study prion protein (PrP) amyloids from human, mouse and Syrian hamster and show that their structural differences are mainly governed by two residues, which helps to understand interspecies PrP propagation on a molecular level.

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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