The polyphenolic phytoalexin polydatin inhibits amyloid aggregation of recombinant human prion protein.

ABSTRACT: Prion diseases involve misfolded and highly infectious aggregates of prion protein (PrP^Sc) which forms amyloid plaques leading to fatal neurodegeneration. The absence of clinically proven therapeutics makes the discovery of effective remedial interventions a prime concern. Herein, we report novel prion intervention by the polyphenolic phytoalexin, polydatin which binds with moderate affinity to the recombinant protease resistant core of human prion protein, encompassing the sequence 90-231 (rPrP^res) and inhibits its conversion into the highly neurotoxic forms. An extensive evaluation using biophysical techniques revealed that polydatin incubated rPrP^res samples generate off-pathway oligomers having reduced cross-β sheet signature, and relatively smal

SUBMITTER: Sirohi PR 

PROVIDER: S-EPMC9037109 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature