Estimation from Moments Measurements for Amyloid Depolymerisation

Abstract : Estimating reaction rates and size distributions of protein polymers is an important step for understanding the mechanisms of protein misfolding and aggregation, a key feature for amyloid diseases. This study aims at {setting} this framework problem when the experimental measurements consist in the time-dynamics of a moment of the population (\emph{i.e.} for instance the total polymerised mass, as in Thioflavine T measurements, or the second moment measured by Static Light Scattering). We propose a general methodology, and we solve the problem theoretically and numerically in the case of a depolymerising system. We then apply our method to experimental data of degrading oligomers, and conclude that smaller aggregates of ovPrP protein should be more stable than larger ones. This has an important biological implication, since it is commonly admitted that small oligomers constitute the most cytotoxic species during prion misfolding process.
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Article dans une revue
Journal of Theoretical Biology, Elsevier, 2016, 〈10.1016/j.jtbi.2016.02.037〉
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Soumis le : jeudi 24 décembre 2015 - 10:47:09
Dernière modification le : jeudi 15 novembre 2018 - 19:46:41


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Aurora Armiento, Marie Doumic, Philippe Moireau, Human Rezaei. Estimation from Moments Measurements for Amyloid Depolymerisation. Journal of Theoretical Biology, Elsevier, 2016, 〈10.1016/j.jtbi.2016.02.037〉. 〈hal-01248255〉



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