TY  - JOUR
AU  - Penezić, Ana Z.
AU  - Aćimović, Jelena M.
AU  - Pavićević, Ivan D.
AU  - Jovanović, Vesna B.
AU  - Takić, Marija
AU  - Mandić, Ljuba M.
PY  - 2019
UR  - http://rimi.imi.bg.ac.rs/handle/123456789/946
AB  - Cys34 thiol group of human serum albumin (HSA) represents major plasma antioxidant. Its reactivity is influenced by multiple factors. The influence of fatty acids (FA; saturated, mono, and poly unsaturated acids from fish oil) binding to HSA, on copper(II) binding affinity and Cys34 thiol group accessibility/reactivity, in the presence of carbonylation agent (methylglyoxal, MG) was examined. HSA-copper(II) content, thiol group reactivity, and HSA carbonylation level were monitored spectrophotometrically. Changes in HSA were followed by fluorescence spectroscopy and native PAG electrophoresis. FA/HSA molar ratio was screened by GC. Together, binding of copper(II) ions and FA to HSA increase the reactivity of Cys34 thiol group (depending on the type of FA), with constant contribution of copper(II) ions of one-third. Carbonylation of FA-HSA-Cu(II) complexes caused a decrease in the Cys34 thiol group content, accompanied by a decrease in the content of HSA-bound copper. The carbonylation level of guanidine groups was not affected by FAs and copper(II) binding. Fluorescent emission spectra of FA-HSA-Cu(II)-MG complexes showed conformational changes in HSA molecule. Although binding of fatty acids and copper ions caused a significant increase in the thiol group reactivity, Cys34 thiol from FA-HSA-Cu(II) complexes reacted with MG in smaller extent than expected, probably as a consequence of conformational changes introduced by carbonylation. Increase in the percentage of reacted-free thiol groups with MG (due to FA and copper binding) may not seem to be very significant, but it is very important in complex biological systems, where catalytic metal is present. [GRAPHICS] .
PB  - Springer, New York
T2  - Journal of Biological Inorganic Chemistry
T1  - The interplay between copper(II), human serum albumin, fatty acids, and carbonylating agent interferes with Cys 34 thiol reactivity and copper binding
EP  - 70
IS  - 1
SP  - 61
VL  - 24
DO  - 10.1007/s00775-018-1628-7
ER  - 

@article{
author = "Penezić, Ana Z. and Aćimović, Jelena M. and Pavićević, Ivan D. and Jovanović, Vesna B. and Takić, Marija and Mandić, Ljuba M.",
year = "2019",
abstract = "Cys34 thiol group of human serum albumin (HSA) represents major plasma antioxidant. Its reactivity is influenced by multiple factors. The influence of fatty acids (FA; saturated, mono, and poly unsaturated acids from fish oil) binding to HSA, on copper(II) binding affinity and Cys34 thiol group accessibility/reactivity, in the presence of carbonylation agent (methylglyoxal, MG) was examined. HSA-copper(II) content, thiol group reactivity, and HSA carbonylation level were monitored spectrophotometrically. Changes in HSA were followed by fluorescence spectroscopy and native PAG electrophoresis. FA/HSA molar ratio was screened by GC. Together, binding of copper(II) ions and FA to HSA increase the reactivity of Cys34 thiol group (depending on the type of FA), with constant contribution of copper(II) ions of one-third. Carbonylation of FA-HSA-Cu(II) complexes caused a decrease in the Cys34 thiol group content, accompanied by a decrease in the content of HSA-bound copper. The carbonylation level of guanidine groups was not affected by FAs and copper(II) binding. Fluorescent emission spectra of FA-HSA-Cu(II)-MG complexes showed conformational changes in HSA molecule. Although binding of fatty acids and copper ions caused a significant increase in the thiol group reactivity, Cys34 thiol from FA-HSA-Cu(II) complexes reacted with MG in smaller extent than expected, probably as a consequence of conformational changes introduced by carbonylation. Increase in the percentage of reacted-free thiol groups with MG (due to FA and copper binding) may not seem to be very significant, but it is very important in complex biological systems, where catalytic metal is present. [GRAPHICS] .",
publisher = "Springer, New York",
journal = "Journal of Biological Inorganic Chemistry",
title = "The interplay between copper(II), human serum albumin, fatty acids, and carbonylating agent interferes with Cys 34 thiol reactivity and copper binding",
pages = "70-61",
number = "1",
volume = "24",
doi = "10.1007/s00775-018-1628-7"
}

Penezić, A. Z., Aćimović, J. M., Pavićević, I. D., Jovanović, V. B., Takić, M.,& Mandić, L. M.. (2019). The interplay between copper(II), human serum albumin, fatty acids, and carbonylating agent interferes with Cys 34 thiol reactivity and copper binding. in Journal of Biological Inorganic Chemistry
Springer, New York., 24(1), 61-70.
https://doi.org/10.1007/s00775-018-1628-7

Penezić AZ, Aćimović JM, Pavićević ID, Jovanović VB, Takić M, Mandić LM. The interplay between copper(II), human serum albumin, fatty acids, and carbonylating agent interferes with Cys 34 thiol reactivity and copper binding. in Journal of Biological Inorganic Chemistry. 2019;24(1):61-70.
doi:10.1007/s00775-018-1628-7 .

Penezić, Ana Z., Aćimović, Jelena M., Pavićević, Ivan D., Jovanović, Vesna B., Takić, Marija, Mandić, Ljuba M., "The interplay between copper(II), human serum albumin, fatty acids, and carbonylating agent interferes with Cys 34 thiol reactivity and copper binding" in Journal of Biological Inorganic Chemistry, 24, no. 1 (2019):61-70,
https://doi.org/10.1007/s00775-018-1628-7 . .

TY  - JOUR
AU  - Takić, Marija
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  - http://rimi.imi.bg.ac.rs/handle/123456789/730
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 & Function
T1  - Binding of enterolactone and enterodiol to human serum albumin: increase of cysteine-34 thiol group reactivity
EP  - 1226
IS  - 2
SP  - 1217
VL  - 7
DO  - 10.1039/c5fo01346a
ER  - 

@article{
author = "Takić, Marija 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 & Function",
title = "Binding of enterolactone and enterodiol to human serum albumin: increase of cysteine-34 thiol group reactivity",
pages = "1226-1217",
number = "2",
volume = "7",
doi = "10.1039/c5fo01346a"
}

Takić, 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 & Function
Royal Soc Chemistry, Cambridge., 7(2), 1217-1226.
https://doi.org/10.1039/c5fo01346a

Takić M, 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 & Function. 2016;7(2):1217-1226.
doi:10.1039/c5fo01346a .

Takić, Marija, 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 & Function, 7, no. 2 (2016):1217-1226,
https://doi.org/10.1039/c5fo01346a . .

TY  - JOUR
AU  - Pavićević, Ivan D.
AU  - Jovanović, Vesna B.
AU  - Takić, Marija
AU  - Penezić, Ana Z.
AU  - Aćimović, Jelena M.
AU  - Mandić, Ljuba M.
PY  - 2014
UR  - http://rimi.imi.bg.ac.rs/handle/123456789/534
AB  - Fatty acids (FAs) binding to human serum albumin (HSA) could lead to the changes of Cys-34 thiol group accessibility and reactivity, i.e. its scavenger capacity and antioxidant property. The influence of saturated, mono and poly unsaturated, and fish oil FAs binding to HSA on the carbonylation level and the reactivity of HSA-SH and HSA modified with methylglyoxal (MG-HSA-SH) was investigated. Changes of thiol group reactivity were followed by determination of pseudo first order rate constant (k') for thiols reaction with 5,5'-dithiobis(2-nitrobenzoic acid). HSA changes were monitored using native PAG electrophoresis and fluorescence spectroscopy. For FA/HSA molar ratios screening, qTLC and GC were used. FAs increase thiol group carbonylation levels from 8% to 20%. The k' values obtained for FAs-free HSA-SH and FAs-free MG-HSA-SH are almost equal (7.5 x 10(-3) and 7.7 x 10(-3) resp.). Binding of all FAs amplify the reactivity (k' values from 14.6 x 10(-3) to 26.0 x 10(-3) s(-1)) of HSA-SH group for 2-3.5 times in the order: palmitic, docosahexaenoic, fish oil extract, stearic, oleic, myristic and eicosapentaenoic acid, due to HSA conformational changes. FAs-bound MG-HSA-SH samples follow that pattern, but their k' values (from 9.8 x 10(-3) to 14.3 x 10(-3) s(-1)) were lower compared to unmodified HSA due to additional conformation changes of HSA molecules during carbonylation. Carbonylation level and reactivity of Cys34 thiol group of unmodified and carbonylated HSA depend on type of FAs bound to HSA, which implies the possibility for modulation of -SH reactivity (scavenger capacity and antioxidant property) by FAs as a supplement.
PB  - Elsevier Ireland Ltd, Clare
T2  - Chemico-Biological Interactions
T1  - Fatty acids binding to human serum albumin: Changes of reactivity and glycation level of Cysteine-34 free thiol group with methylglyoxal
EP  - 50
SP  - 42
VL  - 224
DO  - 10.1016/j.cbi.2014.10.008
ER  - 

@article{
author = "Pavićević, Ivan D. and Jovanović, Vesna B. and Takić, Marija and Penezić, Ana Z. and Aćimović, Jelena M. and Mandić, Ljuba M.",
year = "2014",
abstract = "Fatty acids (FAs) binding to human serum albumin (HSA) could lead to the changes of Cys-34 thiol group accessibility and reactivity, i.e. its scavenger capacity and antioxidant property. The influence of saturated, mono and poly unsaturated, and fish oil FAs binding to HSA on the carbonylation level and the reactivity of HSA-SH and HSA modified with methylglyoxal (MG-HSA-SH) was investigated. Changes of thiol group reactivity were followed by determination of pseudo first order rate constant (k') for thiols reaction with 5,5'-dithiobis(2-nitrobenzoic acid). HSA changes were monitored using native PAG electrophoresis and fluorescence spectroscopy. For FA/HSA molar ratios screening, qTLC and GC were used. FAs increase thiol group carbonylation levels from 8% to 20%. The k' values obtained for FAs-free HSA-SH and FAs-free MG-HSA-SH are almost equal (7.5 x 10(-3) and 7.7 x 10(-3) resp.). Binding of all FAs amplify the reactivity (k' values from 14.6 x 10(-3) to 26.0 x 10(-3) s(-1)) of HSA-SH group for 2-3.5 times in the order: palmitic, docosahexaenoic, fish oil extract, stearic, oleic, myristic and eicosapentaenoic acid, due to HSA conformational changes. FAs-bound MG-HSA-SH samples follow that pattern, but their k' values (from 9.8 x 10(-3) to 14.3 x 10(-3) s(-1)) were lower compared to unmodified HSA due to additional conformation changes of HSA molecules during carbonylation. Carbonylation level and reactivity of Cys34 thiol group of unmodified and carbonylated HSA depend on type of FAs bound to HSA, which implies the possibility for modulation of -SH reactivity (scavenger capacity and antioxidant property) by FAs as a supplement.",
publisher = "Elsevier Ireland Ltd, Clare",
journal = "Chemico-Biological Interactions",
title = "Fatty acids binding to human serum albumin: Changes of reactivity and glycation level of Cysteine-34 free thiol group with methylglyoxal",
pages = "50-42",
volume = "224",
doi = "10.1016/j.cbi.2014.10.008"
}

Pavićević, I. D., Jovanović, V. B., Takić, M., Penezić, A. Z., Aćimović, J. M.,& Mandić, L. M.. (2014). Fatty acids binding to human serum albumin: Changes of reactivity and glycation level of Cysteine-34 free thiol group with methylglyoxal. in Chemico-Biological Interactions
Elsevier Ireland Ltd, Clare., 224, 42-50.
https://doi.org/10.1016/j.cbi.2014.10.008

Pavićević ID, Jovanović VB, Takić M, Penezić AZ, Aćimović JM, Mandić LM. Fatty acids binding to human serum albumin: Changes of reactivity and glycation level of Cysteine-34 free thiol group with methylglyoxal. in Chemico-Biological Interactions. 2014;224:42-50.
doi:10.1016/j.cbi.2014.10.008 .

Pavićević, Ivan D., Jovanović, Vesna B., Takić, Marija, Penezić, Ana Z., Aćimović, Jelena M., Mandić, Ljuba M., "Fatty acids binding to human serum albumin: Changes of reactivity and glycation level of Cysteine-34 free thiol group with methylglyoxal" in Chemico-Biological Interactions, 224 (2014):42-50,
https://doi.org/10.1016/j.cbi.2014.10.008 . .