A micellar on-pathway intermediate step explains the kinetics of prion amyloid formation.
2014
Erwan Hingant | Pascaline Fontes | Maria Teresa Alvarez-Martinez | Jacques-Damien Arnaud | Jean-Pierre Liautard | Laurent Pujo-Menjouet
In a previous work by Alvarez-Martinez et al. (2011), the authors pointed out some fallacies in the mainstream interpretation of the prion amyloid formation. It appeared necessary to propose an original hypothesis able to reconcile the in vitro data with the predictions of a mathematical model describing the problem. Here, a model is developed accordingly with the hypothesis that an intermediate on-pathway leads to the conformation of the prion protein into an amyloid competent isoform thanks to a structure, called micelles, formed from hydrodynamic interaction. The authors also compare data to the prediction of their model and propose a new hypothesis for the formation of infectious prion amyloids.
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