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dc.creatorRadibratović, Milica
dc.creatorAl-Hanish, Ayah
dc.creatorMinić, Simeon
dc.creatorRadomirović, Mirjana
dc.creatorMilčić, Miloš
dc.creatorStanić-Vučinić, Dragana
dc.creatorĆirković Veličković, Tanja
dc.date.accessioned2019-11-20T14:51:24Z
dc.date.available2019-11-20T14:51:24Z
dc.date.issued2019
dc.identifier.issn0308-8146
dc.identifier.urihttps://cer.ihtm.bg.ac.rs/handle/123456789/3212
dc.description.abstractα-Lactalbumin (ALA) is a Ca2+-binding protein which constitutes up to 20% of whey protein. At acidic pH, and in the apo-state at elevated temperatures, ALA is the classic 'molten globule' (MG). This study examined epigallocatechin-3-gallate (EGCG) binding to ALA in its apo form (apoALA) and stabilizing effect on protein structure thereof. EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free formen
dc.language.isoensr
dc.publisherElseviersr
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172024/RS//sr
dc.relationinfo:eu-repo/grantAgreement/EC/H2020/810752/EU//sr
dc.rightsrestrictedAccesssr
dc.sourceFood Chemistrysr
dc.subjectMolecular dynamics simulationsr
dc.subjectFluorescence quenchingsr
dc.subjectProtein stabilitysr
dc.subjectNoncovalent interactionssr
dc.subjectEpigallocatechin-3-gallatesr
dc.subjectApo α-lactalbuminsr
dc.titleStabilization of apo α-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics studyen
dc.typearticlesr
dc.rights.licenseARRsr
dcterms.abstractРадибратовић, Милица; Радомировић, Мирјана; Минић, Симеон; Ћирковић Величковић, Тања; Aл-Ханисх, Ayах; Вучинић-Станић, Драгана; Милчић, Милош;
dc.citation.volume278
dc.citation.spage388
dc.citation.epage395
dc.citation.rankaM21~
dc.identifier.pmid30583389
dc.identifier.doi10.1016/j.foodchem.2018.11.038
dc.identifier.scopus2-s2.0-85056756045
dc.identifier.wos000453529300048
dc.type.versionpublishedVersionsr


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Приказ основних података о документу