Solid-state NMR backbone chemical shift assignments of α-synuclein amyloid fibrils at fast MAS regime-Reference-Cited by-同舟云学术

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

Published:2024-04-30 Issue: Volume: Page:
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Author:

Toleikis Zigmantas¹,Paluch Piotr²,Kuc Ewelina²,Petkus Jana¹,Sulskis Darius³,Org-Tago Mai-Liis⁴,Samoson Ago⁴,Smirnovas Vytautas³,Stanek Jan²,Lends Alons¹

Affiliation:

1. Latvijas Organiskās Sintēzes Institūts

2. University of Warsaw

3. Vilnius University

4. Tallinn University of Technology

Abstract

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 a-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 a-syn fibrils were calculated using ¹³C chemical shift differences and TALOS software.

Publisher

Springer Science and Business Media LLC

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