Insights into the role of protein molecule size and structure on interfacial properties using designed sequences

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dc.contributor.authorDwyer, MDen_AU
dc.contributor.authorHe, Len_AU
dc.contributor.authorJames, Men_AU
dc.contributor.authorNelson, Aen_AU
dc.contributor.authorMiddelberg, APJen_AU
dc.date.accessioned2013-03-15T04:37:55Zen_AU
dc.date.available2013-03-15T04:37:55Zen_AU
dc.date.issued2013-03-06en_AU
dc.date.statistics2013-03-15en_AU
dc.description.abstractMixtures of a large, structured protein with a smaller, unstructured component are inherently complex and hard to characterize at interfaces, leading to difficulties in understanding their interfacial behaviours and, therefore, formulation optimization. Here, we investigated interfacial properties of such a mixed system. Simplicity was achieved using designed sequences in which chemical differences had been eliminated to isolate the effect of molecular size and structure, namely a short unstructured peptide (DAMP1) and its longer structured protein concatamer (DAMP4). Interfacial tension measurements suggested that the size and bulk structuring of the larger molecule led to much slower adsorption kinetics. Neutron reflectometry at equilibrium revealed that both molecules adsorbed as a monolayer to the air–water interface (indicating unfolding of DAMP4 to give a chain of four connected DAMP1 molecules), with a concentration ratio equal to that in the bulk. This suggests the overall free energy of adsorption is equal despite differences in size and bulk structure. At small interfacial extensional strains, only molecule packing influenced the stress response. At larger strains, the effect of size became apparent, with DAMP4 registering a higher stress response and interfacial elasticity. When both components were present at the interface, most stress-dissipating movement was achieved by DAMP1. This work thus provides insights into the role of proteins' molecular size and structure on their interfacial properties, and the designed sequences introduced here can serve as effective tools for interfacial studies of proteins and polymers. © 2013, The Royal Societyen_AU
dc.identifier.articlenumber20120987en_AU
dc.identifier.citationDwyer, M. D., He, L., James, M., Nelson, A., Middelberg, A. P. J. (2013). Insights into the role of protein molecule size and structure on interfacial properties using designed sequences. Journal of the Royal Society Interface, 10(80), 20120987. doi:10.1098/rsif.2012.0987en_AU
dc.identifier.govdoc4905en_AU
dc.identifier.issn1742-5689en_AU
dc.identifier.issue80en_AU
dc.identifier.journaltitleJournal of the Royal Society Interfaceen_AU
dc.identifier.urihttp://dx.doi.org/10.1098/rsif.2012.0987en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/4526en_AU
dc.identifier.volume10en_AU
dc.language.isoenen_AU
dc.publisherRoyal Society of Chemistryen_AU
dc.subjectPeptidesen_AU
dc.subjectAdsorptionen_AU
dc.subjectRheologyen_AU
dc.subjectPolystyreneen_AU
dc.subjectElasticityen_AU
dc.subjectInterfacesen_AU
dc.titleInsights into the role of protein molecule size and structure on interfacial properties using designed sequencesen_AU
dc.typeJournal Articleen_AU
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