%0 Journal Article %1 WOS:000670220700005 %A Sergio, Luciana M %A Martins, Yandara A %A Amaral, Jackson L %A Franca, Victor L B %A de Freitas, Camila F %A Neto, Antonio Medina %A Hioka, Noboru %A I, Maria Ravanelli %A Mareze-Costa, Cecilia %A da Costa, Silvio Claudio %A Freire, Valder N %A Brunaldi, Kellen %C ELSEVIER HOUSE, BROOKVALE PLAZA, EAST PARK SHANNON, CO, CLARE, 00000, IRELAND %D 2021 %I ELSEVIER IRELAND LTD %J CHEMICO-BIOLOGICAL INTERACTIONS %K A; Albumin; Fluorescence Molecular Rebaudioside Steviolbioside; analysis; docking spectroscopy} {Steviol; %R 10.1016/j.cbi.2021.109526 %T Molecular insight on the binding of stevia glycosides to bovine serum albumin %V 344 %X The interaction of the steviol and its glycosides (SG), steviolbioside, and rebaudioside A, with bovine serum albumin (BSA) was studied by absorption and fluorescence spectroscopy techniques alongside molecular docking. The stevia derivatives quenched the fluorescence of BSA by a dynamic quenching mechanism, indicating the interaction between the stevia derivatives and BSA. The binding constant (Kb) of steviol was 100-1000-fold higher than those of SG. The stevia derivative/BSA binding reaction was spontaneous and involved the formation of hydrogen bonds and van der Waals interactions between steviol and steviolbioside with BSA, and water reorganization around the rebaudioside A/BSA complex. Molecular docking pointed out the FA1 and FA9 binding sites of BSA as the probable binding sites of steviol and SG, respectively. In conclusion, steviol enhanced hydrophobicity and small size compared to SG may favor its binding to BSA. As steviol and its glycosides share binding sites on BSA with free fatty acids and drugs, they may be competitively displaced from plasma albumin under various physiological states or disease conditions. These findings are clinically relevant and provide an insight into the pharmacokinetics and pharmacodynamics of the stevia glycosides.

@article{WOS:000670220700005, abstract = {The interaction of the steviol and its glycosides (SG), steviolbioside, and rebaudioside A, with bovine serum albumin (BSA) was studied by absorption and fluorescence spectroscopy techniques alongside molecular docking. The stevia derivatives quenched the fluorescence of BSA by a dynamic quenching mechanism, indicating the interaction between the stevia derivatives and BSA. The binding constant (Kb) of steviol was 100-1000-fold higher than those of SG. The stevia derivative/BSA binding reaction was spontaneous and involved the formation of hydrogen bonds and van der Waals interactions between steviol and steviolbioside with BSA, and water reorganization around the rebaudioside A/BSA complex. Molecular docking pointed out the FA1 and FA9 binding sites of BSA as the probable binding sites of steviol and SG, respectively. In conclusion, steviol enhanced hydrophobicity and small size compared to SG may favor its binding to BSA. As steviol and its glycosides share binding sites on BSA with free fatty acids and drugs, they may be competitively displaced from plasma albumin under various physiological states or disease conditions. These findings are clinically relevant and provide an insight into the pharmacokinetics and pharmacodynamics of the stevia glycosides.}, added-at = {2022-05-23T20:00:14.000+0200}, address = {ELSEVIER HOUSE, BROOKVALE PLAZA, EAST PARK SHANNON, CO, CLARE, 00000, IRELAND}, author = {Sergio, Luciana M and Martins, Yandara A and Amaral, Jackson L and Franca, Victor L B and de Freitas, Camila F and Neto, Antonio Medina and Hioka, Noboru and I, Maria Ravanelli and Mareze-Costa, Cecilia and da Costa, Silvio Claudio and Freire, Valder N and Brunaldi, Kellen}, biburl = {https://www.bibsonomy.org/bibtex/2746362c930c8d2b5695f903ba8404300/ppgfis_ufc_br}, doi = {10.1016/j.cbi.2021.109526}, interhash = {7ac29ab148216b056ad8e04114bcdc87}, intrahash = {746362c930c8d2b5695f903ba8404300}, issn = {0009-2797}, journal = {CHEMICO-BIOLOGICAL INTERACTIONS}, keywords = {A; Albumin; Fluorescence Molecular Rebaudioside Steviolbioside; analysis; docking spectroscopy} {Steviol;}, publisher = {ELSEVIER IRELAND LTD}, pubstate = {published}, timestamp = {2022-05-23T20:00:14.000+0200}, title = {Molecular insight on the binding of stevia glycosides to bovine serum albumin}, tppubtype = {article}, volume = 344, year = 2021 }