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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)

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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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Publication type Article: Journal article

Document type Scientific Article

Corresponding Author

Keywords Abeta Peptide ; Amyloid Fibrils ; Assignment ; Automated Assignment ; Carbon-detection ; Solid-state Nmr; Nuclear-magnetic-resonance; Structural Basis; Algorithm; Peptides; Backbone; Model; C-13

ISSN (print) / ISBN 1874-2718

e-ISSN 1874-270X

Journal Biomolecular NMR Assignments

Publisher Springer

Publishing Place Van Godewijckstraat 30, 3311 Gz Dordrecht, Netherlands

Non-patent literature Publications

Reviewing status Peer reviewed

Institute(s) Institute of Structural Biology (STB)

Grants Helmholtz-Gemeinschaft
SFB 1035 (German Research Foundation DFG)
Helmholtz Zentrum Mnchen - Deutsches Forschungszentrum fr Gesundheit und Umwelt (GmbH) (4209)