TY  - JOUR
AU  - Jelić, Ratomir
AU  - Stojanović, Stefan D.
AU  - Berić, Jelena D.
AU  - Odović, Jadranka
PY  - 2018
UR  - https://farfar.pharmacy.bg.ac.rs/handle/123456789/3031
AB  - The co-administration of several drugs in multidrug therapy may alter the binding of each drug to human serum albumin (HSA) and, thus, their pharmacology effect. Therefore, in this study, the interaction mechanism between HSA and two fluoroquinolones (FQs), sparfloxacin (SPF) and levofloxacin (LVF), was investigated using fluorescence and absorption methods in the absence and presence of the competing drugtigecycline (TGC). The UV-Vis and fluorescence spectroscopy results showed that the fluorescence quenching of HSA was a result of the formation of the HSA-SPF and HSA-LVF complexes. The fluorescence quenching of HSA-TGC revealed that tigecycline can regulate the binding sites, binding mode and binding affinity of fl uoroquinolones. The binding constants (KA) and binding sites (n) of the interaction systems were calculated. The results confirmed that the KA values of the HSA-FQ system decreased in the presence of TGC, indicating that TGC can affect the binding ability of FQ for HSA. This interaction may increase the free plasma concentration of unbound FQ and enhance their pharmacology effect.
AB  - Istovremena primena nekoliko lekova, u multilek terapiji, može izmeniti njihovo vezivanje za humani serumski albumin (HSA) i njihov farmakološki efekat. Zbog toga, u ovom radu je proučavan mehanizam interakcije između HSA i dva fluorohinolona (FQs): sparfloksacina (SPF) i levofloksacina (LVF) fluorescentnim i apsorpcionim metodama u odsustvu i prisustvu konkurentskog leka - tigeciklina (TGC). Rezultati UV-Vis i fluorescentne spektroskopije su pokazali da je gašenje fluorescencije u HSA rezultat formiranja HSA-SPF i HSA-LVF kompleksa. Gašenje fluoroscencije u HSA-TGC je pokazalo da tigeciklin može regulisati mesta vezivanja, način vezivanja i afinitet vezivanja fluorohinolona. Konstante vezivanja (KA) i broj vezujućih mesta (n) za interakcije u sistemu su izračunate. Rezultati su potvrdili da su vrednosti KA u HSA-FQ sistemu, smanjene u prisustvu TGC, a to ukazuje da TGC može da utiče na sposobnost vezivanja FQ za HSA. Ova interakcija može povećati slobodnu koncentraciju u plazmi nevezanog FQ i poboljšati njegov farmakološki efekat.
PB  - Univerzitet u Kragujevcu - Fakultet medicinskih nauka, Kragujevac
T2  - Serbian Journal of Experimental and Clinical Research
T1  - The effect of tigecycline on the binding of fluoroquinolones to human serum albumin
T1  - Dejstvo tigeciklina na vezivanje fluorohinolona za humani serumski albumin
VL  - 19
IS  - 1
SP  - 17
EP  - 25
DO  - 10.1515/SJECR-2017-0006
ER  - 

@article{
author = "Jelić, Ratomir and Stojanović, Stefan D. and Berić, Jelena D. and Odović, Jadranka",
year = "2018",
abstract = "The co-administration of several drugs in multidrug therapy may alter the binding of each drug to human serum albumin (HSA) and, thus, their pharmacology effect. Therefore, in this study, the interaction mechanism between HSA and two fluoroquinolones (FQs), sparfloxacin (SPF) and levofloxacin (LVF), was investigated using fluorescence and absorption methods in the absence and presence of the competing drugtigecycline (TGC). The UV-Vis and fluorescence spectroscopy results showed that the fluorescence quenching of HSA was a result of the formation of the HSA-SPF and HSA-LVF complexes. The fluorescence quenching of HSA-TGC revealed that tigecycline can regulate the binding sites, binding mode and binding affinity of fl uoroquinolones. The binding constants (KA) and binding sites (n) of the interaction systems were calculated. The results confirmed that the KA values of the HSA-FQ system decreased in the presence of TGC, indicating that TGC can affect the binding ability of FQ for HSA. This interaction may increase the free plasma concentration of unbound FQ and enhance their pharmacology effect., Istovremena primena nekoliko lekova, u multilek terapiji, može izmeniti njihovo vezivanje za humani serumski albumin (HSA) i njihov farmakološki efekat. Zbog toga, u ovom radu je proučavan mehanizam interakcije između HSA i dva fluorohinolona (FQs): sparfloksacina (SPF) i levofloksacina (LVF) fluorescentnim i apsorpcionim metodama u odsustvu i prisustvu konkurentskog leka - tigeciklina (TGC). Rezultati UV-Vis i fluorescentne spektroskopije su pokazali da je gašenje fluorescencije u HSA rezultat formiranja HSA-SPF i HSA-LVF kompleksa. Gašenje fluoroscencije u HSA-TGC je pokazalo da tigeciklin može regulisati mesta vezivanja, način vezivanja i afinitet vezivanja fluorohinolona. Konstante vezivanja (KA) i broj vezujućih mesta (n) za interakcije u sistemu su izračunate. Rezultati su potvrdili da su vrednosti KA u HSA-FQ sistemu, smanjene u prisustvu TGC, a to ukazuje da TGC može da utiče na sposobnost vezivanja FQ za HSA. Ova interakcija može povećati slobodnu koncentraciju u plazmi nevezanog FQ i poboljšati njegov farmakološki efekat.",
publisher = "Univerzitet u Kragujevcu - Fakultet medicinskih nauka, Kragujevac",
journal = "Serbian Journal of Experimental and Clinical Research",
title = "The effect of tigecycline on the binding of fluoroquinolones to human serum albumin, Dejstvo tigeciklina na vezivanje fluorohinolona za humani serumski albumin",
volume = "19",
number = "1",
pages = "17-25",
doi = "10.1515/SJECR-2017-0006"
}

Jelić, R., Stojanović, S. D., Berić, J. D.,& Odović, J.. (2018). The effect of tigecycline on the binding of fluoroquinolones to human serum albumin. in Serbian Journal of Experimental and Clinical Research
Univerzitet u Kragujevcu - Fakultet medicinskih nauka, Kragujevac., 19(1), 17-25.
https://doi.org/10.1515/SJECR-2017-0006

Jelić R, Stojanović SD, Berić JD, Odović J. The effect of tigecycline on the binding of fluoroquinolones to human serum albumin. in Serbian Journal of Experimental and Clinical Research. 2018;19(1):17-25.
doi:10.1515/SJECR-2017-0006 .

Jelić, Ratomir, Stojanović, Stefan D., Berić, Jelena D., Odović, Jadranka, "The effect of tigecycline on the binding of fluoroquinolones to human serum albumin" in Serbian Journal of Experimental and Clinical Research, 19, no. 1 (2018):17-25,
https://doi.org/10.1515/SJECR-2017-0006 . .

TY  - JOUR
AU  - Berić, Jelena D.
AU  - Jelić, Ratomir
AU  - Nešić, Dejan M.
AU  - Trbojević-Stanković, Jasna
AU  - Odović, Jadranka
PY  - 2017
UR  - https://farfar.pharmacy.bg.ac.rs/handle/123456789/2794
AB  - The plasma protein binding (PPB) data of twelve antipsychotics (aripiprazole, clozapine, olanzapine, quetiapine, risperidone, sertindole, ziprasidone, chlorpromazine, flupentixol, fluphenazine, haloperidol, zuclopenthixol) were estimated using computed molecular descriptors, which included the electronic descriptor - polar surface area (PSA), the constitutional parameter - molecular weight (Mw), the geometric descriptor - volume value (Vol), the lipophilicity descriptor (logP) and aqueous solubility data (logS), and the acidity descriptor (pK(a)). The relationships between computed molecular properties of the selected antipsychotics and their PPB data were investigated by simple linear regression analysis. Low correlations were obtained between the PPB data of the antipsychotics and PSA, Mw, Vol, pKa, logS (R  lt  0.30) values, while relatively higher correlations (0.35 lt R-2 lt 0.70) were obtained for the majority of logP values. Multiple linear regression (MLR) analysis was applied to access reliable correlations of the PPB data of the antipsychotics and the computed molecular descriptors. Relationships with acceptable probability values (P lt 0.05) were established for five lipophilicity descriptors (logP values) with application of the acidity descriptor (pKa) as independent variables: AlogP (R-2=0.705), XlogP3 (R-2=0.679), ClogP (R-2=0.590), XlogP2 (R-2=0.567), as well as for the experimental lipophilicity parameter, logPexp (R-2=0.635). The best correlations obtained in MLR using AlogP and pKa as independent variables were checked using three additional antipsychotics: loxapine, sulpiride and amisulpride, with the PPB values of 97%, "less than" 40% and 17%, respectively. Their predicted PPB values were relatively close to the literature data. The proposed technique confirmed that lipophilicity, together with acidity significantly influences the PPB of antipsychotics. The described procedure can be regarded as an additional in vitro approach to the modeling of the investigated group of drugs.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - Estimation of plasma protein binding of selected antipsychotics using computed molecular properties
VL  - 69
IS  - 3
SP  - 463
EP  - 468
DO  - 10.2298/ABS160912121B
ER  - 

@article{
author = "Berić, Jelena D. and Jelić, Ratomir and Nešić, Dejan M. and Trbojević-Stanković, Jasna and Odović, Jadranka",
year = "2017",
abstract = "The plasma protein binding (PPB) data of twelve antipsychotics (aripiprazole, clozapine, olanzapine, quetiapine, risperidone, sertindole, ziprasidone, chlorpromazine, flupentixol, fluphenazine, haloperidol, zuclopenthixol) were estimated using computed molecular descriptors, which included the electronic descriptor - polar surface area (PSA), the constitutional parameter - molecular weight (Mw), the geometric descriptor - volume value (Vol), the lipophilicity descriptor (logP) and aqueous solubility data (logS), and the acidity descriptor (pK(a)). The relationships between computed molecular properties of the selected antipsychotics and their PPB data were investigated by simple linear regression analysis. Low correlations were obtained between the PPB data of the antipsychotics and PSA, Mw, Vol, pKa, logS (R  lt  0.30) values, while relatively higher correlations (0.35 lt R-2 lt 0.70) were obtained for the majority of logP values. Multiple linear regression (MLR) analysis was applied to access reliable correlations of the PPB data of the antipsychotics and the computed molecular descriptors. Relationships with acceptable probability values (P lt 0.05) were established for five lipophilicity descriptors (logP values) with application of the acidity descriptor (pKa) as independent variables: AlogP (R-2=0.705), XlogP3 (R-2=0.679), ClogP (R-2=0.590), XlogP2 (R-2=0.567), as well as for the experimental lipophilicity parameter, logPexp (R-2=0.635). The best correlations obtained in MLR using AlogP and pKa as independent variables were checked using three additional antipsychotics: loxapine, sulpiride and amisulpride, with the PPB values of 97%, "less than" 40% and 17%, respectively. Their predicted PPB values were relatively close to the literature data. The proposed technique confirmed that lipophilicity, together with acidity significantly influences the PPB of antipsychotics. The described procedure can be regarded as an additional in vitro approach to the modeling of the investigated group of drugs.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "Estimation of plasma protein binding of selected antipsychotics using computed molecular properties",
volume = "69",
number = "3",
pages = "463-468",
doi = "10.2298/ABS160912121B"
}

Berić, J. D., Jelić, R., Nešić, D. M., Trbojević-Stanković, J.,& Odović, J.. (2017). Estimation of plasma protein binding of selected antipsychotics using computed molecular properties. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 69(3), 463-468.
https://doi.org/10.2298/ABS160912121B

Berić JD, Jelić R, Nešić DM, Trbojević-Stanković J, Odović J. Estimation of plasma protein binding of selected antipsychotics using computed molecular properties. in Archives of Biological Sciences. 2017;69(3):463-468.
doi:10.2298/ABS160912121B .

Berić, Jelena D., Jelić, Ratomir, Nešić, Dejan M., Trbojević-Stanković, Jasna, Odović, Jadranka, "Estimation of plasma protein binding of selected antipsychotics using computed molecular properties" in Archives of Biological Sciences, 69, no. 3 (2017):463-468,
https://doi.org/10.2298/ABS160912121B . .