Simple item page
 

Heat-induced changes in lupin seed γ-conglutin structure promote its interaction with model phospholipid membranes

cris.virtual.author-orcid0000-0001-8799-1748
cris.virtual.author-orcid0000-0002-1438-1217
cris.virtualsource.author-orcide45381b5-f3f6-460d-9d8e-5fca34e39285
cris.virtualsource.author-orcid1c802429-36ee-40e7-b72f-32f16b32d8de
dc.abstract.enA number of scientific data indicate that γ-conglutin can be internalised by different human cells and undergoes secretion from the seed in response to high temperature. In both of these cases, the protein must interact in some manner with biological membranes, however, the mechanisms underlying this phenomenon remain unknown. Herein, we found that the remarkable change of total surface hydrophobicity after appropriate heat treatment of γ-conglutin monomer led to its interaction with model membranes (liposomes). Before the interaction, the protein undergoes an intriguing thermal unfolding pattern which was studied based on a spectroscopic approach. Insight into the interaction mechanism with liposomes was possible thanks to applying two molecular probes that were differentially localised in the lipid bilayer. The results show that the thermal rearranged γ-coglutin monomer affects hydrocarbon chains in model membranes leading to their morphology change and disruption. The main driving force of this phenomenon is based on hydrophobic interaction.
dc.affiliationWydział Nauk o Żywności i Żywieniu
dc.affiliation.instituteKatedra Biochemii i Analizy Żywności
dc.contributor.authorCzubiński, Jarosław
dc.contributor.authorDwiecki, Krzysztof
dc.date.accessioned2025-09-16T11:01:57Z
dc.date.available2025-09-16T11:01:57Z
dc.date.issued2022
dc.description.bibliographyil., bibliogr.
dc.description.financepublication_nocost
dc.description.financecost0,00
dc.description.if8,8
dc.description.number16 April 2022
dc.description.points200
dc.description.volume374
dc.identifier.doi10.1016/j.foodchem.2021.131533
dc.identifier.eissn1873-7072
dc.identifier.issn0308-8146
dc.identifier.urihttps://sciencerep.up.poznan.pl/handle/item/4818
dc.languageen
dc.relation.ispartofFood Chemistry
dc.relation.pagesart. 131533
dc.rightsClosedAccess
dc.sciencecloudnosend
dc.subject.enlupin seed
dc.subject.enγ-conglutin
dc.subject.enmodel membranes
dc.subject.enprotein surface hydrophobicity
dc.subject.enprotein structure
dc.subject.enprotein thermostability
dc.titleHeat-induced changes in lupin seed γ-conglutin structure promote its interaction with model phospholipid membranes
dc.typeJournalArticle
dspace.entity.typePublication
oaire.citation.volume374