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The fold of α-synuclein fibrils

Vilar, Marçal, Chou, Hui-Ting, Lührs, Thorsten, Maji, Samir K., Riek-Loher, Dominique, Verel, Rene, Manning, Gerard, Stahlberg, Henning, Riek, Roland·2008·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.0712179105
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Abstract

The aggregation of proteins into amyloid fibrils is associated with several neurodegenerative diseases. In Parkinson's disease it is believed that the aggregation of α-synuclein (α-syn) from monomers by intermediates into amyloid fibrils is the toxic disease-causative mechanism. Here, we studied the structure of α-syn in its amyloid state by using various biophysical approaches. Quenched hydrogen/deuterium exchange NMR spectroscopy identified five β-strands within the fibril core comprising residues 35–96 and solid-state NMR data from amyloid fibrils comprising the fibril core residues 30–110 confirmed the presence of β-sheet secondary structure. The data suggest that β1-strand interacts with β2, β2 with β3, β3 with β4, and β4 with β5. High-resolution cryoelectron microscopy revealed the protofilament boundaries of ≈2 × 3.5 nm. Based on the combination of these data and published structural studies, a fold of α-syn in the fibrils is proposed and discussed.

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Crossref · 10.1073/pnas.0712179105

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  • In the disease-associated, aggregated state of α-Syn, the N-terminal residues (37 through 97) adopt a β-sheet structure.

    “It has been reported that in the disease-associated, aggregated state of α-Syn, the N-terminal residues (37 through 97), adopts a β-sheet structure [49].”

    From LRP1 is a neuronal receptor for α-synuclein uptake and spread (2022) · cites this paper as [49]

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Metadata

Authors
Vilar, M., Chou, H.-T., Lührs, T., Maji, S. K., Riek-Loher, D., Verel, R., Manning, G., Stahlberg, H., & Riek, R.
Affiliations
  • The Salk Institute for Biological Studies, North Torrey Pines Road, La Jolla, CA 92037;
  • Molecular and Cellular Biology, University of California, 1 Shields Avenue, Davis, CA 95616; and
  • Laboratory of Physical Chemistry, Eidgenössische Technische Hochschule Zurich, 8093 Zurich, Switzerland
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2008-06-24
Volume
105
Issue
25
Pages
8637-8642
ISSN
  • 0027-8424
  • 1091-6490
DOI
10.1073/pnas.0712179105
Cited by
541
References
2
Language
en

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