Sugar-coated proteins: the importance of degree of polymerisation of oligo-galacturonic acid on protein binding and aggregation

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dc.contributor.authorXu, AYen_AU
dc.contributor.authorMelton, LDen_AU
dc.contributor.authorRyan, TMen_AU
dc.contributor.authorMata, JPen_AU
dc.contributor.authorJameson, GBen_AU
dc.contributor.authorRekas, Aen_AU
dc.contributor.authorWilliams, MAKen_AU
dc.contributor.authorMcGillivray, DJen_AU
dc.date.accessioned2023-11-28T06:09:25Zen_AU
dc.date.available2023-11-28T06:09:25Zen_AU
dc.date.issued2017-03-14en_AU
dc.date.statistics2023-11-21en_AU
dc.description.abstractWe have simplified the structural heterogeneity of protein–polysaccharide binding by investigating protein binding to oligosaccharides. The interactions between bovine beta-lactoglobulin A (βLgA) and oligo-galacturonic acids (OGAs) with various numbers of sugar residues have been investigated with a range of biophysical techniques. We show that the βLgA–OGA interaction is critically dependent on the length of the oligosaccharide. Isothermal titration calorimetry results suggest that a minimum length of 7 or 8 sugar residues is required in order to exhibit appreciable exothermic interactions with βLgA – shorter oligosaccharides show no enthalpic interactions at any concentration ratio. When titrating βLgA into OGAs with more than 7–8 sugar residues the sample solution also became turbid with increasing amounts of βLgA, indicating the formation of macroscopic assemblies. Circular dichroism, thioflavin T fluorescence and small angle X-ray/neutron scattering experiments revealed two structural regimes during the titration. When OGAs were in excess, βLgA formed discrete assemblies upon OGA binding, and no subsequent aggregation was observed. However, when βLgA was present in excess, multi-scale structures were formed and this eventually led to the separation of the solution into two liquid-phases. © 2017 The Royal Society of Chemistryen_AU
dc.description.sponsorshipWe wish to thank the Riddet Institute for CoRE funding for this project including a PhD scholarship for AYX and the University of Auckland for a contribution to financial support. We would like to thank the Australian Synchrotron for providing SAXS beam time (AS151/SAXS/9044), and Australian Nuclear Science and Technology Organisation for providing SANS beam time (P4512). Dr Yang Xun is acknowledged for her assistance with SAXS experiments.en_AU
dc.identifier.citationXu, A. Y., Melton, L. D., Ryan, T. M., Mata, J. P., Jameson, G. B., Rekas, A., Williams, M. A. K., & McGillivray, D. J. (2017). Sugar-coated proteins: the importance of degree of polymerisation of oligo-galacturonic acid on protein binding and aggregation. Soft Matter, 13(14), 2698-2707. doi:10.1039/C6SM02660Een_AU
dc.identifier.issn1744-6848en_AU
dc.identifier.issue14en_AU
dc.identifier.journaltitleSoft Matteren_AU
dc.identifier.pagination2698-2707en_AU
dc.identifier.urihttps://apo.ansto.gov.au/handle/10238/15247en_AU
dc.identifier.volume13en_AU
dc.language.isoenen_AU
dc.publisherRoyal Society of Chemistryen_AU
dc.relation.urihttps://doi.org/10.1039/C6SM02660Een_AU
dc.subjectProteinsen_AU
dc.subjectPolymerizationen_AU
dc.subjectPolysaccharidesen_AU
dc.subjectCalorimetryen_AU
dc.subjectEnthalpyen_AU
dc.subjectNeutron diffractionen_AU
dc.titleSugar-coated proteins: the importance of degree of polymerisation of oligo-galacturonic acid on protein binding and aggregationen_AU
dc.typeJournal Articleen_AU
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