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TitleStructure-Toxicity Relationship in Intermediate Fibrils from α-Synuclein Condensates.
Journal, issue, pagesJ Am Chem Soc, Vol. 146, Issue 15, Page 10537-10549, Year 2024
Publish dateApr 3, 2024
AuthorsSerene W Chen / Joseph D Barritt / Roberta Cascella / Alessandra Bigi / Cristina Cecchi / Martina Banchelli / Angelo Gallo / James A Jarvis / Fabrizio Chiti / Christopher M Dobson / Giuliana Fusco / Alfonso De Simone /
PubMed AbstractThe aberrant aggregation of α-synuclein (αS) into amyloid fibrils is associated with a range of highly debilitating neurodegenerative conditions, including Parkinson's disease. Although the ...The aberrant aggregation of α-synuclein (αS) into amyloid fibrils is associated with a range of highly debilitating neurodegenerative conditions, including Parkinson's disease. Although the structural properties of mature amyloids of αS are currently understood, the nature of transient protofilaments and fibrils that appear during αS aggregation remains elusive. Using solid-state nuclear magnetic resonance (ssNMR), cryogenic electron microscopy (cryo-EM), and biophysical methods, we here characterized intermediate amyloid fibrils of αS forming during the aggregation from liquid-like spherical condensates to mature amyloids adopting the structure of pathologically observed aggregates. These transient amyloid intermediates, which induce significant levels of cytotoxicity when incubated with neuronal cells, were found to be stabilized by a small core in an antiparallel β-sheet conformation, with a disordered N-terminal region of the protein remaining available to mediate membrane binding. In contrast, mature amyloids that subsequently appear during the aggregation showed different structural and biological properties, including low levels of cytotoxicity, a rearranged structured core embedding also the N-terminal region, and a reduced propensity to interact with the membrane. The characterization of these two fibrillar forms of αS, and the use of antibodies and designed mutants, enabled us to clarify the role of critical structural elements endowing intermediate amyloid species with the ability to interact with membranes and induce cytotoxicity.
External linksJ Am Chem Soc / PubMed:38567991 / PubMed Central
MethodsEM (helical sym.)
Resolution3.3 Å
Structure data

19184

8ri9

EMDB-19184, PDB-8ri9:
Late alpha-Synuclein fibril structure from liquid-liquid phase separations.
Method: EM (helical sym.) / Resolution: 3.3 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / Amyloid / Fibril / Neurodegeneration / Parkinson's Disease

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