Further exploration of the conformational space of α-synuclein fibrils: solid-state NMR assignment of a high-pH polymorph

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• 作者：Joeri Verasdonck ; Luc Bousset ; Julia Gath ; Ronald Melki…
• 关键词：Solid ; state NMR ; Polymorphism ; Synuclein
• 刊名：Biomolecular NMR Assignments
• 出版年：2016
• 出版时间：April 2016
• 年：2016
• 卷：10
• 期：1
• 页码：5-12
• 全文大小：2,164 KB
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• 作者单位：Joeri Verasdonck (1)
  Luc Bousset (2)
  Julia Gath (1)
  Ronald Melki (2)
  Anja Böckmann (3)
  Beat H. Meier (1)
  
  1. Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland
  2. Paris-Saclay Institute of Neuroscience, CNRS, Avenue de la Terrasse, 91198, Gif-sur-Yvette, France
  3. Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS/Université de Lyon 1, 7, passage du Vercors, 69367, Lyon, France
  
• 刊物类别：Physics and Astronomy
• 刊物主题：None Assigned
• 出版者：Springer Netherlands
• ISSN：1874-270X

文摘

Polymorphism is a common and important phenomenon for protein fibrils which has been linked to the appearance of strains in prion and other neurodegenerative diseases. Parkinson disease is a frequently occurring neurodegenerative pathology, tightly associated with the formation of Lewy bodies. These deposits mainly consist of α-synuclein in fibrillar, β-sheet-rich form. α-synuclein is known to form numerous different polymorphs, which show distinct structural features. Here, we describe the chemical shift assignments, and derive the secondary structure, of a polymorph that was fibrillized at higher-than-physiological pH conditions. The fibrillar core contains residues 40–95, with both the C- and N-terminus not showing any ordered, rigid parts. The chemical shifts are similar to those recorded previously for an assigned polymorph that was fibrillized at neutral pH.