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TitleLeveraging bioorthogonal conjugation for alpha synuclein fibril surveillance.
Journal, issue, pagesbioRxiv, Year 2025
Publish dateSep 17, 2025
AuthorsRebecca A Jenkins / Samantha Wu / Gretchen Fujimura / Andrés Heredia / Cameron W Flowers / Chuanqi Sun / Michael R Sawaya / Joseph A Loo / Jose A Rodriguez /
PubMed AbstractAlpha synuclein (α-syn) amyloid fibrils are associated with various neurodegenerative diseases. To better understand the molecular and cellular basis for α-syn fibril persistence and spread, we ...Alpha synuclein (α-syn) amyloid fibrils are associated with various neurodegenerative diseases. To better understand the molecular and cellular basis for α-syn fibril persistence and spread, we implemented a fluorophore labeling strategy to surveil pre-formed α-syn fibrils in solution and in cells. We leveraged amber codon mediated incorporation of a tetrazine-based artificial amino acid (TetV2.0) to install a cyclooctene-conjugated Janeliaflour, JF549, at four sites on human α-syn: residues 4, 60, 96 and 136. Fast coupling occurred under mild buffer conditions and in the presence of the disease-associated cofactor and cytotoxic lipid, psychosine. Labeled fibrils retained their polymorphic features, seeded the growth of new fibrils , and induced the seeding of positive puncta in α-syn FRET biosensor HEK293T cells. This allowed simultaneous tracking of exogenous and endogenous α-syn aggregates in biosensor cells, and their localization within the cells. In doing so, our approach facilitates more detailed mechanistic investigation of α-syn aggregates.
External linksbioRxiv / PubMed:41000844 / PubMed Central
MethodsEM (helical sym.)
Resolution2.72 Å
Structure data

72396

9y0s

EMDB-72396, PDB-9y0s:
CryoEM structure of alpha-synuclein fibril induced by psychosine
Method: EM (helical sym.) / Resolution: 2.72 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / alpha-synuclein / amyloid / lipid

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