Size distribution of amyloid fibrils. Mathematical models and experimental data.
Doumic, Marie; Rezaei, Human; Hoffmann, Marc; Wafaâ, Haffaf; Prigent, Stephanie (2014), Size distribution of amyloid fibrils. Mathematical models and experimental data., International Journal of Pure and Applied Mathematics, 93, 6, p. 845-878. http://dx.doi.org/10.12732/ijpam.v93i6.10
TypeArticle accepté pour publication ou publié
External document linkhttp://hal.upmc.fr/hal-00958785
Journal nameInternational Journal of Pure and Applied Mathematics
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Abstract (EN)More than twenty types of proteins can adopt misfolded conformations, which can coaggregate into amyloid fibrils, and are related to pathologies such as Alzheimer's disease. Numerous reactions have been proposed to take part to their aggregation kinetics, though the relative importance of each reaction in vivo is unclear. We have statistically analysed the shape of the size distribution of prion fibrils, with the peculiar example of truncated data due to the experimental technique (electron microscopy). A model of polymerization and depolymerization succeeds in explaining the exponential law, which can be followed by the experimental distribution. The effect of other reactions is exposed by reviewing mathematical models on length distribution: activation steps, with nucleation compared to initiation, disaggregation steps, with depolymerization compared to fragmentation, and additional processes such as filament coalescence or secondary nucleation.
Subjects / Keywordskernel density estimation; statistical test; Becker-Döring system; PrP fiber; protein aggregation
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