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

Archive ouverte

Collu, Francesca | Spiga, Enrico | Chakroun, Nesrine | Rezaei, Human | Fraternali, Franca

Edité par CCSD ; Royal Society of Chemistry -

International audience. 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 -rich H2H3 domain of the ovine prion protein (H2H3-OvPrP(Sc)), known to be the portion of prion protein carrying oligomerization activity.

Consulter en ligne

Suggestions

Du même auteur

Decrypting Prion Protein Conversion into a β-Rich Conformer by Molecular Dynamics.

Archive ouverte | Chakroun, Nesrine | CCSD

International audience. Prion diseases are fatal neurodegenerative diseases characterized by the formation of β-rich oligomers and the accumulation of amyloid fibrillar deposits in the central nervous system. Unders...

The oligomerization properties of prion protein are restricted to the H2H3 domain.

Archive ouverte | Chakroun, Nesrine | CCSD

International audience. The propensity of the prion protein (PrP) to adopt different structures is a clue to its pathological behavior. The determination of the region involved in the PrP(C) to PrP(Sc) conversion is...

Characterisation of the prion protein oligomerisation by md simulations and small angle X-ray scattering

Archive ouverte | Chakroun, Nesrine | CCSD

International audience

Chargement des enrichissements...