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dc.creatorTakic, Marija M.
dc.creatorJovanović, Vesna B.
dc.creatorPavicevic, Ivan D.
dc.creatorUzelac, Tamara N.
dc.creatorAćimović, Jelena M.
dc.creatorRistic-Medic, Danijela K.
dc.creatorMandić, Ljuba M.
dc.date.accessioned2018-11-22T00:35:40Z
dc.date.available2018-11-22T00:35:40Z
dc.date.issued2016
dc.identifier.issn2042-6496
dc.identifier.urihttp://cherry.chem.bg.ac.rs/handle/123456789/2054
dc.description.abstractThe interaction of polyphenolic molecules with human serum albumin (HSA) could lead to changes in the reactivity of the HSA Cys34 thiol group (HSA-SH). The influences of enterolactone (EL) and enterodiol (ED) binding on HSA-SH reactivity in fatty acid (FA)-free HSA, and in HSA with bound stearic acid (S) in S/HSA molar ratios of 1 : 1 and 4 : 1, were investigated by the determination of the pseudo first order rate constants (k') for the thiol reaction with 5,5'-dithiobis-(2-nitrobenzoic acid). The binding affinities and binding sites of EL and ED were also determined, using fluorescence measurements of the intrinsic fluorescence of Trp214 and diazepam (binding site marker). EL and ED binding to HSA increased the reactivity of HSA-SH in all assayed HSA-enterolignan complexes by 9.1-33.1%. The strongest effects were obtained for FA-free HSA-enterolignan complexes. S modulated/reduced the effect of EL on HSA-SH reactivity, while its influence on the effect of ED was negligible. The binding of enterolignans to HSA was investigated: the binding constants were the highest for FA-free HSA (EL: 11.64 x 10(4) M-1 and ED: 5.59 x 10(4) M-1 at 37 degrees C) and the lowest for S/HSA 4 : 1-enterolignan complexes (EL: 2.43 x 10(4) M-1 and ED: 1.92 x 10(4) M-1). When the S/HSA ratio was increased, the binding affinities and number of binding sites for EL and ED were decreased. At the same time, a high correlation between binding constants and increased Cys34 reactivity was found (r = 0.974). Competitive experiments using diazepam indicated that the binding of ED and of EL was located in the hydrophobic pocket of site II in HSA. Overall, it is evident that stearic acid could modulate the enterolignan effects on HSA-SH reactivity as well as their binding to HSA. This finding could be important for pharmacokinetics and the expression of enterolignan antioxidant effects in vivo after an intake of lignan rich food.en
dc.publisherRoyal Soc Chemistry, Cambridge
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172049/RS//
dc.relationinfo:eu-repo/grantAgreement/MESTD/Integrated and Interdisciplinary Research (IIR or III)/41030/RS//
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/256716/EU//
dc.rightsopenAccess
dc.sourceFood and Function
dc.titleBinding of enterolactone and enterodiol to human serum albumin: increase of cysteine-34 thiol group reactivityen
dc.typearticle
dc.rights.licenseBY-NC
dcterms.abstractТакиц, Марија М.; Јовановић, Весна; Aћимовић, Јелена; Мандић, Љуба М.; Узелац, Тамара Н.; Ристиц-Медиц, Данијела К.; Павицевиц, Иван Д.;
dc.citation.volume7
dc.citation.issue2
dc.citation.spage1217
dc.citation.epage1226
dc.identifier.wos000370692900060
dc.identifier.doi10.1039/c5fo01346a
dc.citation.other7(2): 1217-1226
dc.citation.rankM21
dc.identifier.pmid26838610
dc.type.versionpublishedVersion
dc.identifier.scopus2-s2.0-84959328527
dc.identifier.rcubKon_3010


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