Modelling and analysis of protein aggregation - Competing pathways in prion (PrP) polymerisation
ESAIM. Proceedings, Tome 45 (2014), pp. 189-198.

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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 ∑i ≥ 1i2 Ci, with ci being the concentration of fibrils of size i, were then measured as a function of time. An initial model, adapted from the Becker-Döring 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.
DOI : 10.1051/proc/201445019

Wafaâ Haffaf 1 ; Stéphanie Prigent 2

1 Inria, Paris-Rocquencourt, Domaine de Voluceau, BP105, 78153 Le Chesnay, France; LJLL, Laboratoire Jacques-Louis Lions, Pierre et Marie Curie University, Boite courrier 187, 75252 Paris Cedex 05, France
2 Inria; LJLL; INRA, VIM, Domaine de Vilvert, 78352 Jouy-en-Josas cedex, France
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     title = {Modelling and analysis of protein aggregation - {Competing} pathways in prion {(PrP)} polymerisation},
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Wafaâ Haffaf; Stéphanie Prigent. Modelling and analysis of protein aggregation - Competing pathways in prion (PrP) polymerisation. ESAIM. Proceedings, Tome 45 (2014), pp. 189-198. doi : 10.1051/proc/201445019. http://geodesic.mathdoc.fr/articles/10.1051/proc/201445019/

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