Research output: Contribution to journal › Article › peer-review
Binding of quercetin and curcumin to human serum albumin in aqueous dimethyl sulfoxide and in aqueous ethanol. / Usacheva, Tatyana; Gamov, George; Bychkova, Anna; Anufrikov, Yuriy; Shasherina, Anna; Alister, Diana; Kuranova, Natalya; Sharnin, Valentin.
In: Journal of Thermal Analysis and Calorimetry, Vol. 147, No. 9, 05.03.2022, p. 5511-5518.Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - Binding of quercetin and curcumin to human serum albumin in aqueous dimethyl sulfoxide and in aqueous ethanol
AU - Usacheva, Tatyana
AU - Gamov, George
AU - Bychkova, Anna
AU - Anufrikov, Yuriy
AU - Shasherina, Anna
AU - Alister, Diana
AU - Kuranova, Natalya
AU - Sharnin, Valentin
N1 - Publisher Copyright: © 2022, Akadémiai Kiadó, Budapest, Hungary.
PY - 2022/3/5
Y1 - 2022/3/5
N2 - 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.
AB - 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.
KW - калориметрия титрования
KW - СЫВОРОТОЧНЫЙ АЛЬБУМИН
KW - КВЕРЦЕТИН
KW - Albumin
KW - Binding constant
KW - Calorimetry
KW - Curcumin
KW - Enthalpy
KW - Mixed solvents
KW - Quercetin
UR - http://www.scopus.com/inward/record.url?scp=85125639393&partnerID=8YFLogxK
UR - https://www.mendeley.com/catalogue/2033b747-6835-3da5-849b-0e3f89d0b26b/
U2 - 10.1007/s10973-022-11216-8
DO - 10.1007/s10973-022-11216-8
M3 - Article
AN - SCOPUS:85125639393
VL - 147
SP - 5511
EP - 5518
JO - Journal of Thermal Analysis and Calorimetry
JF - Journal of Thermal Analysis and Calorimetry
SN - 1388-6150
IS - 9
ER -
ID: 100663165