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Rodina, N. ; Sarkar, R. ; Tsakalos, D.* ; Suladze, S.* ; Niu, Z.* ; Reif, B.

Manual and automatic assignment of two different Aβ40 amyloid fibril polymorphs using MAS solid-state NMR spectroscopy.

Biomol. NMR Assign., DOI: 10.1007/s12104-024-10189-z (2024)
Verlagsversion Forschungsdaten DOI PMC
Open Access Hybrid
Creative Commons Lizenzvertrag
Amyloid fibrils from Alzheimer's amyloid-beta peptides (Aβ) are found to be polymorphic. So far, 14 Aβ40 fibril structures have been determined. The mechanism of why one particular protein sequence adopts so many different three-dimensional structures is yet not understood. In this work, we describe the assignment of the NMR chemical shifts of two Alzheimer's disease fibril polymorphs, P1 and P2, which are formed by the amyloid-beta peptide Aβ40. The assignment is based on 13C-detected 3D NCACX and NCOCX experiments MAS solid-state NMR experiments. The fibril samples are prepared using an extensive seeding protocol in the absence and presence of the small heat shock protein αB-crystallin. In addition to manual assignments, we obtain chemical shift assignments using the automation software ARTINA. We present an analysis of the secondary chemical shifts and a discussion on the differences between the manual and automated assignment strategies.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Abeta Peptide ; Amyloid Fibrils ; Assignment ; Automated Assignment ; Carbon-detection ; Solid-state Nmr; Nuclear-magnetic-resonance; Structural Basis; Algorithm; Peptides; Backbone; Model; C-13
Sprache englisch
Veröffentlichungsjahr 2024
HGF-Berichtsjahr 2024
ISSN (print) / ISBN 1874-2718
e-ISSN 1874-270X
Zeitschrift Biomolecular NMR Assignments
Verlag Springer
Verlagsort Van Godewijckstraat 30, 3311 Gz Dordrecht, Netherlands
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Structural Biology (STB)
POF Topic(s) 30203 - Molecular Targets and Therapies
Forschungsfeld(er) Enabling and Novel Technologies
PSP-Element(e) G-503090-001
Förderungen Helmholtz-Gemeinschaft
SFB 1035 (German Research Foundation DFG)
Helmholtz Zentrum Mnchen - Deutsches Forschungszentrum fr Gesundheit und Umwelt (GmbH) (4209)
DOI 10.1007/s12104-024-10189-z
WOS ID 001287474700001
Scopus ID 85200962686
PubMed ID 39120652
Erfassungsdatum 2024-09-27
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