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Binding of enterolactone and enterodiol to human serum albumin: increase of cysteine-34 thiol group reactivity

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2016
2052.pdf (1016.Kb)
Authors
Takić, Marija M.
Jovanović, Vesna B.
Pavićević, Ivan D.
Uzelac, Tamara N.
Aćimović, Jelena M.
Ristić-Medić, Danijela
Mandić, Ljuba M.
Article (Published version)
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Abstract
The 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 bindin...g 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.

Source:
Food and Function, 2016, 7, 2, 1217-1226
Publisher:
  • Royal Soc Chemistry, Cambridge
Funding / projects:
  • Allergens, antibodies, enzymes and small physiologically important molecules: design, structure, function and relevance (RS-172049)
  • Biological effects, nutritional intake and status of folate and polysaturate fatty acid (PUFA): improvement of nutrition in Serbia (RS-41030)
  • Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (EU-256716)

DOI: 10.1039/c5fo01346a

ISSN: 2042-6496

PubMed: 26838610

WoS: 000370692900060

Scopus: 2-s2.0-84959328527
[ Google Scholar ]
10
11
URI
https://cherry.chem.bg.ac.rs/handle/123456789/2054
Collections
  • Publikacije
Institution/Community
Hemijski fakultet
TY  - JOUR
AU  - Takić, Marija M.
AU  - Jovanović, Vesna B.
AU  - Pavićević, Ivan D.
AU  - Uzelac, Tamara N.
AU  - Aćimović, Jelena M.
AU  - Ristić-Medić, Danijela
AU  - Mandić, Ljuba M.
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2054
AB  - The 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.
PB  - Royal Soc Chemistry, Cambridge
T2  - Food and Function
T1  - Binding of enterolactone and enterodiol to human serum albumin: increase of cysteine-34 thiol group reactivity
VL  - 7
IS  - 2
SP  - 1217
EP  - 1226
DO  - 10.1039/c5fo01346a
UR  - Kon_3010
ER  - 
@article{
author = "Takić, Marija M. and Jovanović, Vesna B. and Pavićević, Ivan D. and Uzelac, Tamara N. and Aćimović, Jelena M. and Ristić-Medić, Danijela and Mandić, Ljuba M.",
year = "2016",
abstract = "The 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.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Food and Function",
title = "Binding of enterolactone and enterodiol to human serum albumin: increase of cysteine-34 thiol group reactivity",
volume = "7",
number = "2",
pages = "1217-1226",
doi = "10.1039/c5fo01346a",
url = "Kon_3010"
}
Takić, M. M., Jovanović, V. B., Pavićević, I. D., Uzelac, T. N., Aćimović, J. M., Ristić-Medić, D.,& Mandić, L. M.. (2016). Binding of enterolactone and enterodiol to human serum albumin: increase of cysteine-34 thiol group reactivity. in Food and Function
Royal Soc Chemistry, Cambridge., 7(2), 1217-1226.
https://doi.org/10.1039/c5fo01346a
Kon_3010
Takić MM, Jovanović VB, Pavićević ID, Uzelac TN, Aćimović JM, Ristić-Medić D, Mandić LM. Binding of enterolactone and enterodiol to human serum albumin: increase of cysteine-34 thiol group reactivity. in Food and Function. 2016;7(2):1217-1226.
doi:10.1039/c5fo01346a
Kon_3010 .
Takić, Marija M., Jovanović, Vesna B., Pavićević, Ivan D., Uzelac, Tamara N., Aćimović, Jelena M., Ristić-Medić, Danijela, Mandić, Ljuba M., "Binding of enterolactone and enterodiol to human serum albumin: increase of cysteine-34 thiol group reactivity" in Food and Function, 7, no. 2 (2016):1217-1226,
https://doi.org/10.1039/c5fo01346a .,
Kon_3010 .

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