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pH-Dependent oligomerisation of γ-conglutin: A key element to understand its molecular mechanism of action

cris.virtual.author-orcid0000-0001-8799-1748
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cris.virtualsource.author-orcide45381b5-f3f6-460d-9d8e-5fca34e39285
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cris.virtualsource.author-orcid#PLACEHOLDER_PARENT_METADATA_VALUE#
dc.abstract.enDespite extensive research carried out on lupin seed γ-conglutin neither its mechanism of action as a hypoglycaemic nutraceutical compound nor its physiological role for the plant has been unveil. This article revealed a pH-dependent reversible association/dissociation equilibrium involving monomer, dimer and hexamer of Lupinus angustifolius γ-conglutin. The interaction between different oligomeric forms of this protein is reversible, and spectroscopic studies showed that the intact structure of γ-conglutin was preserved under the tested environmental conditions tested (pH 4.5–7.5). The obtained results prove that the hexameric form was preferred under basic conditions and was stabilised by a number of bonds formed upon association of individual protomers. The simultaneous occurrence of several oligomeric forms at a given pH value was shown, and their share was strongly driven by protein concentration. The main changes in oligomerisation of γ-conglutin take place in a pH range of 4.5–6.0, correlating with the pKaR values of the amino acid residues of His (6.0), Glu (4.1), and Asp (3.9). Moreover, a structural model of the protein in hexamer assembly was obtained based on small-angle X-ray scattering (SAXS) and negative staining cryo-electron microscopy (cryo-EM) analyses. The presented study provides essential knowledge about the colloidal dynamics and stability of γ-conglutin in solution, improving our understanding of fundamental environmental factors that could affect the health-promoting activity of this lupin seed protein.
dc.affiliationWydział Nauk o Żywności i Żywieniu
dc.affiliation.instituteKatedra Biochemii i Analizy Żywności
dc.contributor.authorCzubiński, Jarosław Edward
dc.contributor.authorKubíčková, Monika
dc.contributor.authorSzpotkowski, Kamil
dc.contributor.authorKomárek, Jan
dc.date.accessioned2025-08-13T07:17:31Z
dc.date.available2025-08-13T07:17:31Z
dc.date.issued2024
dc.description.bibliographyil., bibliogr.
dc.description.financepublication_nocost
dc.description.financecost0,00
dc.description.if12,4
dc.description.numberPart A (February 2024)
dc.description.points140
dc.description.volume147
dc.identifier.doi10.1016/j.foodhyd.2023.109386
dc.identifier.eissn1873-7137
dc.identifier.issn0268-005X
dc.identifier.urihttps://sciencerep.up.poznan.pl/handle/item/4165
dc.languageen
dc.relation.ispartofFood Hydrocolloids
dc.relation.pagesart. 109386
dc.rightsClosedAccess
dc.sciencecloudsend
dc.titlepH-Dependent oligomerisation of γ-conglutin: A key element to understand its molecular mechanism of action
dc.typeJournalArticle
dspace.entity.typePublication
oaire.citation.volume147