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dc.creatorMinić, Simeon L.
dc.creatorStanić-Vučinić, Dragana
dc.creatorRadomirović, Mirjana Ž.
dc.creatorRadibratović, Milica
dc.creatorMilčić, Miloš K.
dc.creatorNikolić, Milan
dc.creatorĆirković-Veličković, Tanja
dc.date.accessioned2018-11-22T00:45:37Z
dc.date.available2018-11-22T00:45:37Z
dc.date.issued2018
dc.identifier.issn0308-8146
dc.identifier.urihttp://cherry.chem.bg.ac.rs/handle/123456789/2515
dc.description.abstractPhycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (K-a = 2 x 10(6) M-1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin. (C) 2017 Elsevier Ltd. All rights reserved.en
dc.publisherElsevier
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172024/RS//
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/256716/EU//
dc.rightsrestrictedAccess
dc.sourceFood Chemistry
dc.subjectSpirulinaen
dc.subjectPhycocyanobilinen
dc.subjectBovine serum albuminen
dc.subjectBindingen
dc.subjectStabilityen
dc.subjectAntioxidanten
dc.titleCharacterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albuminen
dc.typearticle
dc.rights.licenseARR
dcterms.abstractМиниц, Симеон; Радомировић, Мирјана; Станић-Вучинић, Драгана; Милчић, Милош; Николић, Милан; Ћирковић-Величковић, Тања; Радибратовиц, Милица;
dc.citation.volume239
dc.citation.spage1090
dc.citation.epage1099
dc.identifier.wos000408740200129
dc.identifier.doi10.1016/j.foodchem.2017.07.066
dc.citation.other239: 1090-1099
dc.citation.rankaM21
dc.identifier.pmid28873526
dc.description.otherPeer-reviewed article: [http://cherry.chem.bg.ac.rs/handle/123456789/3035]
dc.description.otherSupplementary material: [http://cherry.chem.bg.ac.rs/handle/123456789/3139]
dc.type.versionpublishedVersionen
dc.identifier.scopus2-s2.0-85024374977
dc.identifier.rcubKon_3331


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