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dc.creatorRadibratović, Milica
dc.creatorMinic, Simeon
dc.creatorStanić-Vučinić, Dragana
dc.creatorNikolić, Milan
dc.creatorMilčić, Miloš
dc.creatorĆirković Veličković, Tanja
dc.date.accessioned2019-01-30T17:49:05Z
dc.date.available2019-01-30T17:49:05Z
dc.date.issued2016
dc.identifier.issn1932-6203
dc.identifier.urihttp://cer.ihtm.bg.ac.rs/handle/123456789/1891
dc.description.abstractPhycocyanobilin (PCB) binds with high affinity (2.2 x 10 6 M-1 at 25 degrees C) to human serum albumin (HSA) at sites located in IB and IIA subdomains. The aim of this study was to examine effects of PCB binding on protein conformation and stability. Using 300 ns molecular dynamics (MD) simulations, UV-VIS spectrophotometry, CD, FT-IR, spectrofluorimetry, thermal denaturation and susceptibility to trypsin digestion, we studied the effects of PCB binding on the stability and rigidity of HSA, as well as the conformational changes in PCB itself upon binding to the protein. MD simulation results demonstrated that HSA with PCB bound at any of the two sites showed greater rigidity and lower overall and individual domain flexibility compared to free HSA. Experimental data demonstrated an increase in the a-helical content of the protein and thermal and proteolytic stability upon ligand binding. PCB bound to HSA undergoes a conformational change to a more elongated conformation in the binding pockets of HSA. PCB binding to HSA stabilizes the structure of this flexible transport protein, making it more thermostable and resistant to proteolysis. The results from this work explain at molecular level, conformational changes and stabilization of HSA structure upon ligand binding. The resultant increased thermal and proteolytic stability of HSA may provide greater longevity to HSA in plasma.en
dc.publisherPublic Library Science, San Francisco
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172024/RS//
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/256716/EU//
dc.rightsopenAccess
dc.sourcePlos One
dc.titleStabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Studyen
dc.typearticle
dc.rights.licenseBY
dcterms.abstractВелицковиц, Тања Цирковиц; Станиц-Вуциниц, Драгана; Радибратовић, Милица; Николиц, Милан; Милциц, Милос; Миниц, Симеон;
dc.citation.volume11
dc.citation.issue12
dc.citation.other11(12):
dc.citation.rankM21
dc.identifier.pmid27959940
dc.identifier.doi10.1371/journal.pone.0167973
dc.identifier.rcubConv_3665
dc.identifier.fulltexthttp://cer.ihtm.bg.ac.rs//bitstream/id/8328/1889.pdf
dc.identifier.scopus2-s2.0-85006056883
dc.identifier.wos000392753900028
dc.type.versionpublishedVersion


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