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A model for amorphous aggregation processes

dc.contributor.authorStranks, Samuel
dc.contributor.authorEcroyd, Heath
dc.contributor.authorVan Sluyter, Steven
dc.contributor.authorWaters, Elizabeth
dc.contributor.authorCarver, John
dc.contributor.authorvon Smekal, Lorenz
dc.date.accessioned2015-12-10T23:08:40Z
dc.date.issued2009
dc.date.updated2016-02-24T10:45:23Z
dc.description.abstractThe amorphous aggregation of proteins is associated with many phenomena, ranging from the formation of protein wine haze to the development of cataract in the eye lens and the precipitation of recombinant proteins during their expression and purification. While much literature exists describing models for linear protein aggregation, such as amyloid fibril formation, there are few reports of models which address amorphous aggregation. Here, we propose a model to describe the amorphous aggregation of proteins which is also more widely applicable to other situations where a similar process occurs, such as in the formation of colloids and nanoclusters. As first applications of the model, we have tested it against experimental turbidimetry data of three proteins relevant to the wine industry and biochemistry, namely, thaumatin, a thaumatinlike protein, and α -lactalbumin. The model is very robust and describes amorphous experimental data to a high degree of accuracy. Details about the aggregation process, such as shape parameters of the aggregates and rate constants, can also be extracted.
dc.identifier.issn1063-651X
dc.identifier.urihttp://hdl.handle.net/1885/63214
dc.publisherAmerican Physical Society
dc.sourcePhysical Review E
dc.subjectKeywords: Aggregation process; Amorphous aggregation; Amyloid fibril formation; Experimental data; Eye lens; High degree of accuracy; Protein aggregation; Recombinant protein; Shape parameters; Thaumatin; Thaumatin-like protein; Wine industry; Agglomeration; Bioche
dc.titleA model for amorphous aggregation processes
dc.typeJournal article
local.bibliographicCitation.issue5
local.bibliographicCitation.startpage051907-1 - 051907-13
local.contributor.affiliationStranks, Samuel, University of Adelaide
local.contributor.affiliationEcroyd, Heath, The University of Adelaide
local.contributor.affiliationVan Sluyter, Steven, The University of Melbourne
local.contributor.affiliationWaters, Elizabeth, University of Melbourne
local.contributor.affiliationCarver, John, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationvon Smekal, Lorenz, The University of Adelaide
local.contributor.authoruidCarver, John, u1571001
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.identifier.absfor030406 - Proteins and Peptides
local.identifier.absseo970103 - Expanding Knowledge in the Chemical Sciences
local.identifier.ariespublicationU4217927xPUB781
local.identifier.citationvolume80
local.identifier.doi10.1103/PhysRevE.80.051907
local.identifier.scopusID2-s2.0-71049157206
local.identifier.thomsonID000272309500072
local.type.statusPublished Version

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