Solid-state NMR backbone chemical shift assignments of α-synuclein amyloid fibrils at fast MAS regime

The α-synuclein (α-syn) amyloid fibrils are involved in various neurogenerative diseases. Solid-state NMR (ssNMR) has been showed as a powerful tool to study α-syn aggregates. Here, we report the H, C and N back-bone chemical shifts of a new α-syn polymorph obtained using proton-detected ssNMR spect...

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Published inBiomolecular NMR assignments
Main Authors Toleikis, Zigmantas, Paluch, Piotr, Kuc, Ewelina, Petkus, Jana, Sulskis, Darius, Org-Tago, Mai-Liis, Samoson, Ago, Smirnovas, Vytautas, Stanek, Jan, Lends, Alons
Format Journal Article
LanguageEnglish
Published Netherlands 29.06.2024
Subjects
Amyloid fibrils
Fast magic-angle spinning
1H-detected solid-state NMR
α-synuclein
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Summary:The α-synuclein (α-syn) amyloid fibrils are involved in various neurogenerative diseases. Solid-state NMR (ssNMR) has been showed as a powerful tool to study α-syn aggregates. Here, we report the H, C and N back-bone chemical shifts of a new α-syn polymorph obtained using proton-detected ssNMR spectroscopy under fast (95 kHz) magic-angle spinning conditions. The manual chemical shift assignments were cross-validated using FLYA algorithm. The secondary structural elements of α-syn fibrils were calculated using C chemical shift differences and TALOS software.
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ISSN:1874-2718
1874-270X
1874-270X
DOI:10.1007/s12104-024-10186-2