Probing the early stages of prion protein (PrP) aggregation with atomistic molecular dynamics simulations

Abstract

Prions are self-replicating infectious proteinaceous agents whose conformations are capable of forming amyloid-like aggregate fibrils. Here we present molecular dynamics simulations aimed at investigating the aggregation process of the β-rich H2H3 domain of the ovine prion protein (H2H3-OvPrPSc), known to be the portion of prion protein carrying oligomerization activity.

Journal details

Volume 54
Issue number 57
Pages 8007-8010
Available online
Publication date

Crick labs/facilities