The polyphenolic phytoalexin polydatin inhibits amyloid aggregation of recombinant human prion protein
Preeti Rana Sirohi, Anchala Kumari, Nikita Admane, Pallavi Somvanshi, Abhinav Grover
Abstract
oligomers. The detailed structural analysis using molecular dynamics simulations elucidated the induction of antagonistic mobilities in the β2-α2 loop, α3 helix and the N-terminal amyloidogenic region of prions. This study puts forward novel prion fibrillogenesis inhibitory potential of polydatin, specifically by stabilizing the N-terminal amyloidogenic region. Collectively our results affirm the importance of polydatin in crippling the prion pathogenesis and may serve as a structural scaffold for designing novel therapeutic agents targeting amyloidogenic transition in prions.
Topics & Concepts
ChemistryNeurodegenerationFibrillogenesisRecombinant DNABiochemistryAmyloid βAmyloid (mycology)Prion proteinProtein foldingProtein aggregationFibrilBiophysicsCell biologyBiologyGeneDiseasePathologyMedicineInorganic chemistryPrion Diseases and Protein MisfoldingAlzheimer's disease research and treatmentsNeurological diseases and metabolism