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

期刊论文
发表日期：

2024年6月29日

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Zigmantas Toleikis,
Piotr Paluch,
Ewelina Kuc,
Jana Petkus,
Darius Sulskis,
Mai-Liis Org-Tago,
Ago Samoson,
Vytautas Smirnovas,
Jan Stanek,
Alons Lends

摘要

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 ¹H, ¹³C and ¹⁵N 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 ¹³C chemical shift differences and TALOS software.