TY  - JOUR
AU  - Takić, Marija
AU  - Ranković, Slavica
AU  - Girek, Zdenka
AU  - Pavlović, Suzana
AU  - Jovanović, Petar
AU  - Jovanović, Vesna
AU  - Šarac, Ivana
PY  - 2024
UR  - http://rimi.imi.bg.ac.rs/handle/123456789/1483
AB  - The plant-derived α-linolenic acid (ALA) is an essential n-3 acid highly susceptible to oxidation, present in oils of flaxseeds, walnuts, canola, perilla, soy, and chia. After ingestion, it can be incorporated in to body lipid pools (particularly triglycerides and phospholipid membranes), and then endogenously metabolized through desaturation, elongation, and peroxisome oxidation to eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA), with a very limited efficiency (particularly for DHA), beta-oxidized as an energy source, or directly metabolized to C18-oxilipins. At this moment, data in the literature about the effects of ALA supplementation on metabolic syndrome (MetS) in humans are inconsistent, indicating no effects or some positive effects on all MetS components (abdominal obesity, dyslipidemia, impaired insulin sensitivity and glucoregulation, blood pressure, and liver steatosis). The major effects of ALA on MetS seem to be through its conversion to more potent EPA and DHA, the impact on the n-3/n-6 ratio, and the consecutive effects on the formation of oxylipins and endocannabinoids, inflammation, insulin sensitivity, and insulin secretion, as well as adipocyte and hepatocytes function. It is important to distinguish the direct effects of ALA from the effects of EPA and DHA metabolites. This review summarizes the most recent findings on this topic and discusses the possible mechanisms.
PB  - Basel : MDPI (Multidisciplinary Digital Publishing Institute)
T2  - International Journal of Molecular Sciences
T2  - International Journal of Molecular Sciences
T1  - Current Insights into the Effects of Dietary α-Linolenic Acid Focusing on Alterations of Polyunsaturated Fatty Acid Profiles in Metabolic Syndrome
IS  - 9
SP  - 4909
VL  - 25
DO  - 10.3390/ijms25094909
ER  - 

@article{
author = "Takić, Marija and Ranković, Slavica and Girek, Zdenka and Pavlović, Suzana and Jovanović, Petar and Jovanović, Vesna and Šarac, Ivana",
year = "2024",
abstract = "The plant-derived α-linolenic acid (ALA) is an essential n-3 acid highly susceptible to oxidation, present in oils of flaxseeds, walnuts, canola, perilla, soy, and chia. After ingestion, it can be incorporated in to body lipid pools (particularly triglycerides and phospholipid membranes), and then endogenously metabolized through desaturation, elongation, and peroxisome oxidation to eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA), with a very limited efficiency (particularly for DHA), beta-oxidized as an energy source, or directly metabolized to C18-oxilipins. At this moment, data in the literature about the effects of ALA supplementation on metabolic syndrome (MetS) in humans are inconsistent, indicating no effects or some positive effects on all MetS components (abdominal obesity, dyslipidemia, impaired insulin sensitivity and glucoregulation, blood pressure, and liver steatosis). The major effects of ALA on MetS seem to be through its conversion to more potent EPA and DHA, the impact on the n-3/n-6 ratio, and the consecutive effects on the formation of oxylipins and endocannabinoids, inflammation, insulin sensitivity, and insulin secretion, as well as adipocyte and hepatocytes function. It is important to distinguish the direct effects of ALA from the effects of EPA and DHA metabolites. This review summarizes the most recent findings on this topic and discusses the possible mechanisms.",
publisher = "Basel : MDPI (Multidisciplinary Digital Publishing Institute)",
journal = "International Journal of Molecular Sciences, International Journal of Molecular Sciences",
title = "Current Insights into the Effects of Dietary α-Linolenic Acid Focusing on Alterations of Polyunsaturated Fatty Acid Profiles in Metabolic Syndrome",
number = "9",
pages = "4909",
volume = "25",
doi = "10.3390/ijms25094909"
}

Takić, M., Ranković, S., Girek, Z., Pavlović, S., Jovanović, P., Jovanović, V.,& Šarac, I.. (2024). Current Insights into the Effects of Dietary α-Linolenic Acid Focusing on Alterations of Polyunsaturated Fatty Acid Profiles in Metabolic Syndrome. in International Journal of Molecular Sciences
Basel : MDPI (Multidisciplinary Digital Publishing Institute)., 25(9), 4909.
https://doi.org/10.3390/ijms25094909

Takić M, Ranković S, Girek Z, Pavlović S, Jovanović P, Jovanović V, Šarac I. Current Insights into the Effects of Dietary α-Linolenic Acid Focusing on Alterations of Polyunsaturated Fatty Acid Profiles in Metabolic Syndrome. in International Journal of Molecular Sciences. 2024;25(9):4909.
doi:10.3390/ijms25094909 .

Takić, Marija, Ranković, Slavica, Girek, Zdenka, Pavlović, Suzana, Jovanović, Petar, Jovanović, Vesna, Šarac, Ivana, "Current Insights into the Effects of Dietary α-Linolenic Acid Focusing on Alterations of Polyunsaturated Fatty Acid Profiles in Metabolic Syndrome" in International Journal of Molecular Sciences, 25, no. 9 (2024):4909,
https://doi.org/10.3390/ijms25094909 . .

TY  - JOUR
AU  - Uzelac, Tamara
AU  - Smiljanić, Katarina
AU  - Takić, Marija
AU  - Šarac, Ivana
AU  - Oggiano, Gordana
AU  - Nikolić, Milan
AU  - Jovanović, Vesna
PY  - 2024
UR  - http://rimi.imi.bg.ac.rs/handle/123456789/1467
AB  - The binding of ubiquitous serum ligands (free fatty acids) to human serum albumin (HSA) or its glycation can affect thiol group reactivity, thus influencing its antioxidant activity. The effects of stearic acid (SA) and glucose binding on HSA structural changes and thiol group content and reactivity were monitored by fluoroscopy and the Ellman method during a 14-day incubation in molar ratios to HSA that mimic pathophysiological conditions. Upon incubation with 5 mM glucose, HSA glycation was the same as HSA without it, in three different HSA:SA molar ratios (HSA:SA-1:1-2-4). The protective effect of SA on the antioxidant property of HSA under different glucose regimes (5-10-20 mM) was significantly affected by molar ratios of HSA:SA. Thiol reactivity was fully restored with 5–20 mM glucose at a 1:1 HSA:SA ratio, while the highest thiol content recovery was in pathological glucose regimes at a 1:1 HSA:SA ratio. The SA affinity for HSA increased significantly (1.5- and 1.3-fold, p < 0.01) with 5 and 10 mM glucose compared to the control. These results deepen the knowledge about the possible regulation of the antioxidant role of HSA in diabetes and other pathophysiological conditions and enable the design of future HSA-drug studies which, in turn, is important for clinicians when designing information-based treatments.
PB  - Multidisciplinary Digital Publishing Institute (MDPI)
T2  - International Journal of Molecular Sciences
T1  - The Thiol Group Reactivity and the Antioxidant Property of Human Serum Albumin Are Controlled by the Joint Action of Fatty Acids and Glucose Binding
IS  - 4
SP  - 2335
VL  - 25
DO  - 10.3390/ijms25042335
ER  - 

@article{
author = "Uzelac, Tamara and Smiljanić, Katarina and Takić, Marija and Šarac, Ivana and Oggiano, Gordana and Nikolić, Milan and Jovanović, Vesna",
year = "2024",
abstract = "The binding of ubiquitous serum ligands (free fatty acids) to human serum albumin (HSA) or its glycation can affect thiol group reactivity, thus influencing its antioxidant activity. The effects of stearic acid (SA) and glucose binding on HSA structural changes and thiol group content and reactivity were monitored by fluoroscopy and the Ellman method during a 14-day incubation in molar ratios to HSA that mimic pathophysiological conditions. Upon incubation with 5 mM glucose, HSA glycation was the same as HSA without it, in three different HSA:SA molar ratios (HSA:SA-1:1-2-4). The protective effect of SA on the antioxidant property of HSA under different glucose regimes (5-10-20 mM) was significantly affected by molar ratios of HSA:SA. Thiol reactivity was fully restored with 5–20 mM glucose at a 1:1 HSA:SA ratio, while the highest thiol content recovery was in pathological glucose regimes at a 1:1 HSA:SA ratio. The SA affinity for HSA increased significantly (1.5- and 1.3-fold, p < 0.01) with 5 and 10 mM glucose compared to the control. These results deepen the knowledge about the possible regulation of the antioxidant role of HSA in diabetes and other pathophysiological conditions and enable the design of future HSA-drug studies which, in turn, is important for clinicians when designing information-based treatments.",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "International Journal of Molecular Sciences",
title = "The Thiol Group Reactivity and the Antioxidant Property of Human Serum Albumin Are Controlled by the Joint Action of Fatty Acids and Glucose Binding",
number = "4",
pages = "2335",
volume = "25",
doi = "10.3390/ijms25042335"
}

Uzelac, T., Smiljanić, K., Takić, M., Šarac, I., Oggiano, G., Nikolić, M.,& Jovanović, V.. (2024). The Thiol Group Reactivity and the Antioxidant Property of Human Serum Albumin Are Controlled by the Joint Action of Fatty Acids and Glucose Binding. in International Journal of Molecular Sciences
Multidisciplinary Digital Publishing Institute (MDPI)., 25(4), 2335.
https://doi.org/10.3390/ijms25042335

Uzelac T, Smiljanić K, Takić M, Šarac I, Oggiano G, Nikolić M, Jovanović V. The Thiol Group Reactivity and the Antioxidant Property of Human Serum Albumin Are Controlled by the Joint Action of Fatty Acids and Glucose Binding. in International Journal of Molecular Sciences. 2024;25(4):2335.
doi:10.3390/ijms25042335 .

Uzelac, Tamara, Smiljanić, Katarina, Takić, Marija, Šarac, Ivana, Oggiano, Gordana, Nikolić, Milan, Jovanović, Vesna, "The Thiol Group Reactivity and the Antioxidant Property of Human Serum Albumin Are Controlled by the Joint Action of Fatty Acids and Glucose Binding" in International Journal of Molecular Sciences, 25, no. 4 (2024):2335,
https://doi.org/10.3390/ijms25042335 . .

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  - Pavićević, Ivan D.
AU  - Jovanović, Vesna B.
AU  - Takić, Marija
AU  - Aćimović, Jelena M.
AU  - Penezić, Ana Z.
AU  - Mandić, Ljuba M.
PY  - 2016
UR  - http://rimi.imi.bg.ac.rs/handle/123456789/698
AB  - Non-esterified fatty acids bound to the human serum albumin (HSA) contribute to several HSAs properties of special concern in pathologies, for instance to the reactivity of the free HSA-Cys34 thiol group (important antioxidative thiol pool in plasma), and to the affinity for binding of molecules and ions (for example cobalt as a prominent biomarker in heart ischemia). Therefore, the method for determination of FAs bound to HSA was developed. FAs were released from HSA (previously isolated from serum by ammonium sulfate precipitation) using acidic copper(II) sulfate in phosphoric acid, extracted by n-heptane-chloroform (4:1, v/v) mixture, spotted on TL silica-gel and then developed with n-heptane-chloroform-acetic acid (5:3:03, v/v/v). Common office flatbed scanner and software solution for densitometric image analysis, developed in R, were used. The linearity of calibration curve in concentration range from 0.1 to 5.0 mmol/L stearic acid was achieved. The method was proved to be precise (with RSD of 1.4-4.7%) and accurate. Accuracy was examined by standard addition method (recoveries 97.2-102.5%) and by comparison to results of GC. The method is sample saving, technically less demanding, and cheap, and therefore suitable for determination of FAs/HSA ratio when elevated concentrations of free FAs are reliable diagnostic/risk parameter of pathological states.
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Pharmaceutical & Biomedical Analysis
T1  - Quantification of total content of non-esterified fatty acids bound to human serum albumin
EP  - 49
SP  - 43
VL  - 129
DO  - 10.1016/j.jpba.2016.06.043
ER  - 

@article{
author = "Pavićević, Ivan D. and Jovanović, Vesna B. and Takić, Marija and Aćimović, Jelena M. and Penezić, Ana Z. and Mandić, Ljuba M.",
year = "2016",
abstract = "Non-esterified fatty acids bound to the human serum albumin (HSA) contribute to several HSAs properties of special concern in pathologies, for instance to the reactivity of the free HSA-Cys34 thiol group (important antioxidative thiol pool in plasma), and to the affinity for binding of molecules and ions (for example cobalt as a prominent biomarker in heart ischemia). Therefore, the method for determination of FAs bound to HSA was developed. FAs were released from HSA (previously isolated from serum by ammonium sulfate precipitation) using acidic copper(II) sulfate in phosphoric acid, extracted by n-heptane-chloroform (4:1, v/v) mixture, spotted on TL silica-gel and then developed with n-heptane-chloroform-acetic acid (5:3:03, v/v/v). Common office flatbed scanner and software solution for densitometric image analysis, developed in R, were used. The linearity of calibration curve in concentration range from 0.1 to 5.0 mmol/L stearic acid was achieved. The method was proved to be precise (with RSD of 1.4-4.7%) and accurate. Accuracy was examined by standard addition method (recoveries 97.2-102.5%) and by comparison to results of GC. The method is sample saving, technically less demanding, and cheap, and therefore suitable for determination of FAs/HSA ratio when elevated concentrations of free FAs are reliable diagnostic/risk parameter of pathological states.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Pharmaceutical & Biomedical Analysis",
title = "Quantification of total content of non-esterified fatty acids bound to human serum albumin",
pages = "49-43",
volume = "129",
doi = "10.1016/j.jpba.2016.06.043"
}

Pavićević, I. D., Jovanović, V. B., Takić, M., Aćimović, J. M., Penezić, A. Z.,& Mandić, L. M.. (2016). Quantification of total content of non-esterified fatty acids bound to human serum albumin. in Journal of Pharmaceutical & Biomedical Analysis
Elsevier Science Bv, Amsterdam., 129, 43-49.
https://doi.org/10.1016/j.jpba.2016.06.043

Pavićević ID, Jovanović VB, Takić M, Aćimović JM, Penezić AZ, Mandić LM. Quantification of total content of non-esterified fatty acids bound to human serum albumin. in Journal of Pharmaceutical & Biomedical Analysis. 2016;129:43-49.
doi:10.1016/j.jpba.2016.06.043 .

Pavićević, Ivan D., Jovanović, Vesna B., Takić, Marija, Aćimović, Jelena M., Penezić, Ana Z., Mandić, Ljuba M., "Quantification of total content of non-esterified fatty acids bound to human serum albumin" in Journal of Pharmaceutical & Biomedical Analysis, 129 (2016):43-49,
https://doi.org/10.1016/j.jpba.2016.06.043 . .

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  - CONF
AU  - Aćimović, Jelena M.
AU  - Penezić, Ana Z.
AU  - Pavićević, Ivan D.
AU  - Jovanović, Vesna B.
AU  - Takić, Marija
AU  - Uzelac, Tamara N.
AU  - Mandić, Ljuba M.
PY  - 2016
UR  - http://rimi.imi.bg.ac.rs/handle/123456789/739
PB  - Wiley-Blackwell, Hoboken
C3  - FEBS Journal
T1  - Binding of FAs and Cu(II) ions to HSA changes its Cys34 thiol group antioxidant capacity and carbonylation pattern with methylglyoxal
EP  - 417
SP  - 417
VL  - 283
UR  - https://hdl.handle.net/21.15107/rcub_rimi_739
ER  - 

@conference{
author = "Aćimović, Jelena M. and Penezić, Ana Z. and Pavićević, Ivan D. and Jovanović, Vesna B. and Takić, Marija and Uzelac, Tamara N. and Mandić, Ljuba M.",
year = "2016",
publisher = "Wiley-Blackwell, Hoboken",
journal = "FEBS Journal",
title = "Binding of FAs and Cu(II) ions to HSA changes its Cys34 thiol group antioxidant capacity and carbonylation pattern with methylglyoxal",
pages = "417-417",
volume = "283",
url = "https://hdl.handle.net/21.15107/rcub_rimi_739"
}

Aćimović, J. M., Penezić, A. Z., Pavićević, I. D., Jovanović, V. B., Takić, M., Uzelac, T. N.,& Mandić, L. M.. (2016). Binding of FAs and Cu(II) ions to HSA changes its Cys34 thiol group antioxidant capacity and carbonylation pattern with methylglyoxal. in FEBS Journal
Wiley-Blackwell, Hoboken., 283, 417-417.
https://hdl.handle.net/21.15107/rcub_rimi_739

Aćimović JM, Penezić AZ, Pavićević ID, Jovanović VB, Takić M, Uzelac TN, Mandić LM. Binding of FAs and Cu(II) ions to HSA changes its Cys34 thiol group antioxidant capacity and carbonylation pattern with methylglyoxal. in FEBS Journal. 2016;283:417-417.
https://hdl.handle.net/21.15107/rcub_rimi_739 .

Aćimović, Jelena M., Penezić, Ana Z., Pavićević, Ivan D., Jovanović, Vesna B., Takić, Marija, Uzelac, Tamara N., Mandić, Ljuba M., "Binding of FAs and Cu(II) ions to HSA changes its Cys34 thiol group antioxidant capacity and carbonylation pattern with methylglyoxal" in FEBS Journal, 283 (2016):417-417,
https://hdl.handle.net/21.15107/rcub_rimi_739 .

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 . .

TY  - JOUR
AU  - Jovanović, Vesna B.
AU  - Pavićević, Ivan D.
AU  - Takić, Marija
AU  - Penezic-Romanjuk, Ana Z.
AU  - Aćimović, Jelena M.
AU  - Mandić, Ljuba M.
PY  - 2014
UR  - http://rimi.imi.bg.ac.rs/handle/123456789/558
AB  - During investigation of the changes of the Cys34 thiol group of human serum albumin (HSA) (isolated by affinity chromatography with Cibacron Blue (CB)) in diabetes, we found that the HSA-SH content was higher (11-33%) than the total serum thiol content. The influence of fatty acids (FA) binding to HSA on this discrepancy was investigated in vitro (using fluorescence and CD spectroscopy and GC) and with HSA samples from diabetic (n=20) and control groups (n=17). HSA-bound FA determine the selection of HSA molecules by CB and enhance reactivity and/or accessibility of the SH group. A high content of polyunsaturated FA (35.6%) leads to weaker binding of HSA molecules to CB. Rate constants of DTNB reaction with the SH group of HSA applied to a CB column, bound-HSA and unbound-HSA fractions, were 4.8 x 10(-3), 21.6 x 10(-3), and 11.2 x 10(-3) s(-1), respectively. The HSA-SH group of diabetics is more reactive compared with control individuals (rate constants 20.9 x 10(-3)+/- 4.4 x 10(-3) vs 12.9 x 10(-3)+/- 2.6 x 10(-3) s(-1), P lt 0.05). Recovery values of the SH group obtained after chromatography of HSA with bound stearic acid ranged from 110 to 140%, while those for defatted HSA were from 98.5 to 101.7%. Thus, HSA-bound FA leads to an increase of HSA-SH content and a contribution to total serum thiols, which make the determination of the thiol group unreliable.
PB  - Academic Press Inc Elsevier Science, San Diego
T2  - Analytical Biochemistry
T1  - The influence of fatty acids on determination of human serum albumin thiol group
EP  - 57
SP  - 50
VL  - 448
DO  - 10.1016/j.ab.2013.11.030
ER  - 

@article{
author = "Jovanović, Vesna B. and Pavićević, Ivan D. and Takić, Marija and Penezic-Romanjuk, Ana Z. and Aćimović, Jelena M. and Mandić, Ljuba M.",
year = "2014",
abstract = "During investigation of the changes of the Cys34 thiol group of human serum albumin (HSA) (isolated by affinity chromatography with Cibacron Blue (CB)) in diabetes, we found that the HSA-SH content was higher (11-33%) than the total serum thiol content. The influence of fatty acids (FA) binding to HSA on this discrepancy was investigated in vitro (using fluorescence and CD spectroscopy and GC) and with HSA samples from diabetic (n=20) and control groups (n=17). HSA-bound FA determine the selection of HSA molecules by CB and enhance reactivity and/or accessibility of the SH group. A high content of polyunsaturated FA (35.6%) leads to weaker binding of HSA molecules to CB. Rate constants of DTNB reaction with the SH group of HSA applied to a CB column, bound-HSA and unbound-HSA fractions, were 4.8 x 10(-3), 21.6 x 10(-3), and 11.2 x 10(-3) s(-1), respectively. The HSA-SH group of diabetics is more reactive compared with control individuals (rate constants 20.9 x 10(-3)+/- 4.4 x 10(-3) vs 12.9 x 10(-3)+/- 2.6 x 10(-3) s(-1), P lt 0.05). Recovery values of the SH group obtained after chromatography of HSA with bound stearic acid ranged from 110 to 140%, while those for defatted HSA were from 98.5 to 101.7%. Thus, HSA-bound FA leads to an increase of HSA-SH content and a contribution to total serum thiols, which make the determination of the thiol group unreliable.",
publisher = "Academic Press Inc Elsevier Science, San Diego",
journal = "Analytical Biochemistry",
title = "The influence of fatty acids on determination of human serum albumin thiol group",
pages = "57-50",
volume = "448",
doi = "10.1016/j.ab.2013.11.030"
}

Jovanović, V. B., Pavićević, I. D., Takić, M., Penezic-Romanjuk, A. Z., Aćimović, J. M.,& Mandić, L. M.. (2014). The influence of fatty acids on determination of human serum albumin thiol group. in Analytical Biochemistry
Academic Press Inc Elsevier Science, San Diego., 448, 50-57.
https://doi.org/10.1016/j.ab.2013.11.030

Jovanović VB, Pavićević ID, Takić M, Penezic-Romanjuk AZ, Aćimović JM, Mandić LM. The influence of fatty acids on determination of human serum albumin thiol group. in Analytical Biochemistry. 2014;448:50-57.
doi:10.1016/j.ab.2013.11.030 .

Jovanović, Vesna B., Pavićević, Ivan D., Takić, Marija, Penezic-Romanjuk, Ana Z., Aćimović, Jelena M., Mandić, Ljuba M., "The influence of fatty acids on determination of human serum albumin thiol group" in Analytical Biochemistry, 448 (2014):50-57,
https://doi.org/10.1016/j.ab.2013.11.030 . .