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.
%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
}