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Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin
dc.creator | Minić, Simeon L. | |
dc.creator | Stanić-Vučinić, Dragana | |
dc.creator | Radomirović, Mirjana Ž. | |
dc.creator | Radibratović, Milica | |
dc.creator | Milčić, Miloš K. | |
dc.creator | Nikolić, Milan | |
dc.creator | Ćirković-Veličković, Tanja | |
dc.date.accessioned | 2019-05-27T11:23:06Z | |
dc.date.available | 2018-07-13 | |
dc.date.issued | 2017 | |
dc.identifier.issn | 0308-8146 | |
dc.identifier.uri | https://cherry.chem.bg.ac.rs/handle/123456789/3035 | |
dc.description.abstract | Phycocyanobilin (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 (Ka = 2 × 106 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. | |
dc.publisher | Elsevier | |
dc.relation | info:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172024/RS// | |
dc.relation | info:eu-repo/grantAgreement/EC/FP7/256716/EU// | |
dc.rights | embargoedAccess | |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/4.0/ | |
dc.source | Food Chemistry | |
dc.subject | Antioxidant | |
dc.subject | Binding | |
dc.subject | Bovine serum albumin | |
dc.subject | Phycocyanobilin | |
dc.subject | Spirulina | |
dc.subject | Stability | |
dc.title | Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin | |
dc.type | article | |
dc.rights.license | BY-NC-ND | |
dcterms.abstract | Николић, Милан; Радибратовић, М.; Минић, Симеон Л. ; Станић-Вучинић, Драгана; Радомировић, Мирјана Ж.; Милчић, Милош К.; Ћирковић-Величковић, Тања; | |
dc.citation.volume | 239 | |
dc.citation.spage | 1090 | |
dc.citation.epage | 1099 | |
dc.identifier.wos | 000409918902275 | |
dc.identifier.doi | 10.1016/j.foodchem.2017.07.066 | |
dc.citation.rank | M21 | |
dc.description.other | This is peer-reviewed version of the following article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.; Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099. [https://doi.org/10.1016/j.foodchem.2017.07.066] | |
dc.description.other | Supplementary material: [http://cherry.chem.bg.ac.rs/handle/123456789/3139] | |
dc.type.version | acceptedVersion | |
dc.identifier.scopus | 2-s2.0-85024374977 | |
dc.identifier.fulltext | https://cherry.chem.bg.ac.rs/bitstream/id/7222/minic2017.pdf |