Previous cryo-EM structures of synucleinopathy patient-derived α-synuclein fibrils revealed a ‘mystery density’ at the core of the protofilaments. This study identifies polyphosphate, a universally conserved and ancient biomolecule, to fit this density, binding to the lysine-rich pocket and contributing to fiber stabilization
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In your coverage, please use this URL to provide access to the freely available paper in PLOS Biology : http://journals.plos.org/plosbiology/article?id=10.1371/journal.pbio.3002650
Article Title: Amyloid accelerator polyphosphate fits as the mystery density in α-synuclein fibrils
Author Countries : United States, India
Funding: This work was supported by the National Institute of Health grant R35 GM122506 to U.J. Salary was paid from NIH for P.H., P.M and J.L. The salary for B.S. was provided by the Howard Hughes Medical Institute. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
PLOS Biology
Computational simulation/modeling
Not applicable
Competing interests: I have read the journal’s policy and the authors of this manuscript have the following competing interests: UJ is a member of the PLOS Biology Editorial Board.