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Binding of quercetin and curcumin to human serum albumin in aqueous dimethyl sulfoxide and in aqueous ethanol.


ABSTRACT: The paper reports the spectrofluorimetric and calorimetric study of binding of two hydrophobic biologically active molecules with antioxidant ability, flavonoids quercetin, and curcumin, to human serum albumin (HSA) in water, aqueous DMSO (0.05 and 0.1 mol. fraction of DMSO), and aqueous ethanol (0.05 mol. fraction of EtOH). Both flavonoids induce the quenching of HSA fluorescence. The stability constants of associates, as well as the changes in enthalpy of the reaction between quercetin and protein, were evaluated. The influence of solvent composition and additions of hydroxypropyl-β-cyclodextrin as a solubilizer of hydrophobic molecules, on the association processes is discussed.

Supplementary information

The online version contains supplementary material available at 10.1007/s10973-022-11216-8.

SUBMITTER: Usacheva T 

PROVIDER: S-EPMC8897738 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature

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Binding of quercetin and curcumin to human serum albumin in aqueous dimethyl sulfoxide and in aqueous ethanol.

Usacheva Tatyana T   Gamov George G   Bychkova Anna A   Anufrikov Yuriy Y   Shasherina Anna A   Alister Diana D   Kuranova Natalya N   Sharnin Valentin V  

Journal of thermal analysis and calorimetry 20220305 9


The paper reports the spectrofluorimetric and calorimetric study of binding of two hydrophobic biologically active molecules with antioxidant ability, flavonoids quercetin, and curcumin, to human serum albumin (HSA) in water, aqueous DMSO (0.05 and 0.1 mol. fraction of DMSO), and aqueous ethanol (0.05 mol. fraction of EtOH). Both flavonoids induce the quenching of HSA fluorescence. The stability constants of associates, as well as the changes in enthalpy of the reaction between quercetin and pro  ...[more]

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