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A Micellar On-Pathway Intermediate Step Explains the Kinetics of Prion Amyloid Formation.

Authors :
Hingant, Erwan
Fontes, Pascaline
Alvarez-Martinez, Maria Teresa
Arnaud, Jacques-Damien
Liautard, Jean-Pierre
Pujo-Menjouet, Laurent
Source :
PLoS Computational Biology; Aug2014, Vol. 10 Issue 8, p1-11, 11p, 3 Diagrams, 1 Chart, 4 Graphs
Publication Year :
2014

Abstract

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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
1553734X
Volume :
10
Issue :
8
Database :
Complementary Index
Journal :
PLoS Computational Biology
Publication Type :
Academic Journal
Accession number :
97810539
Full Text :
https://doi.org/10.1371/journal.pcbi.1003735