Modelling and analysis of protein aggregation - completing pathways in prion (PrP) polymerisation - Sorbonne Université Access content directly
Other Publications Year : 2014

Modelling and analysis of protein aggregation - completing pathways in prion (PrP) polymerisation

Abstract

Protein aggregation leading to the formation of amyloid fibrils is involved in several neurodegenerative diseases such as prion diseases. To clarify how these fibrils are able to incorporate additional units, prion fibril aggregation and disaggregation kinetics were experimentally studied using Static Light Scattering (SLS). Values that are functions of Σ i^2 c_i (for i >0) with c_i being the concentration of fibrils of size i, were then measured as a function of time. An initial model, adapted from the Becker-D¨oring system that considers all fibrils to react similarly is not able to reproduce the observed in vitro behaviour. Our second model involves an additional compartment of fibrils unable to incorporate more prion units. This model leads to kinetic coefficients which are biologically plausible and correctly simulates the first experimental steps for prion aggregation.
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Dates and versions

hal-00958804 , version 1 (14-03-2014)

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  • HAL Id : hal-00958804 , version 1

Cite

Stephanie Prigent, Hadjer Wafaa Haffaf. Modelling and analysis of protein aggregation - completing pathways in prion (PrP) polymerisation. 2014. ⟨hal-00958804⟩
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