Foldamers reveal and validate therapeutic targets associated with toxic α-synuclein self-assembly

Jemil Ahmed, Tessa C. Fitch, Courtney M. Donnelly, Johnson A. Joseph, Tyler D. Ball, Mikaela M. Bassil, Ahyun Son, Chen Zhang, Aurélie Ledreux, Scott Horowitz, Yan Qin, Daniel Paredes and Sunil Kumar ()
Additional contact information
Jemil Ahmed: University of Denver
Tessa C. Fitch: University of Denver
Courtney M. Donnelly: University of Denver
Johnson A. Joseph: University of Denver
Tyler D. Ball: University of Denver
Mikaela M. Bassil: University of Denver
Ahyun Son: University of Denver
Chen Zhang: University of Denver
Aurélie Ledreux: University of Denver
Scott Horowitz: University of Denver
Yan Qin: University of Denver
Daniel Paredes: University of Denver
Sunil Kumar: University of Denver

Nature Communications, 2022, vol. 13, issue 1, 1-17

Abstract: Abstract Parkinson’s disease (PD) is a progressive neurodegenerative disorder for which there is no successful prevention or intervention. The pathological hallmark for PD involves the self-assembly of functional Alpha-Synuclein (αS) into non-functional amyloid structures. One of the potential therapeutic interventions against PD is the effective inhibition of αS aggregation. However, the bottleneck towards achieving this goal is the identification of αS domains/sequences that are essential for aggregation. Using a protein mimetic approach, we have identified αS sequences-based targets that are essential for aggregation and will have significant therapeutic implications. An extensive array of in vitro, ex vivo, and in vivo assays is utilized to validate αS sequences and their structural characteristics that are essential for aggregation and propagation of PD phenotypes. The study aids in developing significant mechanistic and therapeutic insights into various facets of αS aggregation, which will pave the way for effective treatments for PD.

Date: 2022
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DOI: 10.1038/s41467-022-29724-4

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