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dc.contributor.authorFoderà, Vitoen
dc.contributor.authorZaccone, Alessioen
dc.contributor.authorLattuada, Marcoen
dc.contributor.authorDonald, Atheneen
dc.date.accessioned2013-09-09T08:41:15Z
dc.date.available2013-09-09T08:41:15Z
dc.date.issued2013-09-05en
dc.identifier.citationPhys. Rev. Lett. 111, 108105 (2013) [5 pages].en
dc.identifier.issn0031-9007
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/244952
dc.description.abstractThe possibility for proteins to aggregate in different superstructures, i.e. large-scale polymorphism, has been widely observed, but an understanding of the physicochemical mechanisms behind it is still out of reach. Here we present a theoretical model for the description of a generic aggregate formed from an ensemble of charged proteins. The model predicts the formation of multifractal structures with the geometry of the growth determined by the electrostatic interactions between single proteins. The model predictions are successfully verified in comparison with experimental curves for aggregate growth allowing us to reveal the mechanism of formation of such complex structures. The model is general and is able to predict aggregate morphologies occurring both in vivo and in vitro. Our findings provide a framework where the physical interactions between single proteins, the aggregate morphology, and the growth kinetics are connected into a single model in agreement with the experimental data.
dc.description.sponsorshipFunding from the Engineering and Physical Sciences Research Council (EP/H004939/1), the Swiss National Science Foundation (Grants Nr. PBEZP2-131153 and Nr. 200020-126487/1) is gratefully acknowledged. A.Z. acknowledges support from the Ernest Oppenheimer Fellowship at Cambridge.
dc.languageEnglishen
dc.language.isoenen
dc.publisherAmerican Physical Society
dc.rightsAttribution-NonCommercial 2.0 UK: England & Wales*
dc.rights.urihttp://creativecommons.org/licenses/by-nc/2.0/uk/*
dc.titleElectrostatics Controls the Formation of Amyloid Superstructures in Protein Aggregationen
dc.typeArticle
dc.description.versionThis is the accepted version of the original publication in Physical Review Letters, which is published online here: http://prl.aps.org/abstract/PRL/v111/i10/e108105. © 2013 American Physical Societyen
prism.publicationDate2013en
prism.publicationNamePhysical Review Lettersen
prism.volume111en
dc.rioxxterms.funderEPSRC
dc.rioxxterms.funderSwiss National Science Foundation
dc.rioxxterms.projectidEP/H004939/1
dc.rioxxterms.projectidPBEZP2-131153
dc.rioxxterms.projectid200020-126487/1
rioxxterms.versionofrecord10.1103/PhysRevLett.111.108105en
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserveden
rioxxterms.licenseref.startdate2013-09-05en
dc.contributor.orcidDonald, Athene [0000-0003-4423-9673]
dc.identifier.eissn1079-7114
rioxxterms.typeJournal Article/Reviewen
pubs.funder-project-idEPSRC (EP/H006028/1)


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Except where otherwise noted, this item's licence is described as Attribution-NonCommercial 2.0 UK: England & Wales