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Issue 57, 2018
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Probing the early stages of prion protein (PrP) aggregation with atomistic molecular dynamics simulations

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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

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Publication details

The article was received on 22 May 2018, accepted on 14 Jun 2018 and first published on 03 Jul 2018


Article type: Communication
DOI: 10.1039/C8CC04089C
Citation: Chem. Commun., 2018,54, 8007-8010
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    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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