Issue 57, 2018

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.

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

Supplementary files

Article information

Article type
Communication
Submitted
22 May 2018
Accepted
14 Jun 2018
First published
03 Jul 2018

Chem. Commun., 2018,54, 8007-8010

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

F. Collu, E. Spiga, N. Chakroun, H. Rezaei and F. Fraternali, Chem. Commun., 2018, 54, 8007 DOI: 10.1039/C8CC04089C

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