A micellar on-pathway intermediate step explains the kinetics of prion amyloid formation.

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 descr...

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Main Authors: Erwan Hingant, Pascaline Fontes, Maria Teresa Alvarez-Martinez, Jacques-Damien Arnaud, Jean-Pierre Liautard, Laurent Pujo-Menjouet
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-08-01
Series:PLoS Computational Biology
Online Access:http://europepmc.org/articles/PMC4125056?pdf=render
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author Erwan Hingant
Pascaline Fontes
Maria Teresa Alvarez-Martinez
Jacques-Damien Arnaud
Jean-Pierre Liautard
Laurent Pujo-Menjouet
author_facet Erwan Hingant
Pascaline Fontes
Maria Teresa Alvarez-Martinez
Jacques-Damien Arnaud
Jean-Pierre Liautard
Laurent Pujo-Menjouet
author_sort Erwan Hingant
collection DOAJ
description 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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spelling doaj.art-b865c0f123a84a3097055e648c76773d2022-12-22T03:15:32ZengPublic Library of Science (PLoS)PLoS Computational Biology1553-734X1553-73582014-08-01108e100373510.1371/journal.pcbi.1003735A micellar on-pathway intermediate step explains the kinetics of prion amyloid formation.Erwan HingantPascaline FontesMaria Teresa Alvarez-MartinezJacques-Damien ArnaudJean-Pierre LiautardLaurent Pujo-MenjouetIn 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.http://europepmc.org/articles/PMC4125056?pdf=render
spellingShingle Erwan Hingant
Pascaline Fontes
Maria Teresa Alvarez-Martinez
Jacques-Damien Arnaud
Jean-Pierre Liautard
Laurent Pujo-Menjouet
A micellar on-pathway intermediate step explains the kinetics of prion amyloid formation.
PLoS Computational Biology
title A micellar on-pathway intermediate step explains the kinetics of prion amyloid formation.
title_full A micellar on-pathway intermediate step explains the kinetics of prion amyloid formation.
title_fullStr A micellar on-pathway intermediate step explains the kinetics of prion amyloid formation.
title_full_unstemmed A micellar on-pathway intermediate step explains the kinetics of prion amyloid formation.
title_short A micellar on-pathway intermediate step explains the kinetics of prion amyloid formation.
title_sort micellar on pathway intermediate step explains the kinetics of prion amyloid formation
url http://europepmc.org/articles/PMC4125056?pdf=render
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