Stojanović, Stefan

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  • Stojanović, Stefan (1)
  • Stojanović, Stefan D. (1)
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Author's Bibliography

Spectroscopic studies on the drug–drug interaction: the influence of fluoroquinolones on the affinity of tigecycline to human serum albumin and identification of the binding site

Stojanović, Stefan; Nićiforović, Jovan; Živanović, Sandra; Odović, Jadranka; Jelić, Ratomir

(Springer, 2020)

TY  - JOUR
AU  - Stojanović, Stefan
AU  - Nićiforović, Jovan
AU  - Živanović, Sandra
AU  - Odović, Jadranka
AU  - Jelić, Ratomir
PY  - 2020
UR  - https://farfar.pharmacy.bg.ac.rs/handle/123456789/3614
AB  - bstract: Concomitant use of two or more drugs in therapy is becoming a more frequent phenomenon and clinically relevant drug–drug interactions at the level of binding to human serum albumin (HSA) are more often. The influence of fluoroquinolones–sparfloxacin, levofloxacin, and ciprofloxacin, on the interaction between tigecycline and HSA, was investigated in vitro by means of fluorescence and absorption spectroscopy. The results of UV–Vis and fluorescence spectroscopy showed that the fluorescence quenching of HSA was a result of the formation of new complexes through a static quenching process. The binding constants (Ka) and the number of binding sites (n) of all systems were calculated. The presence of sparfloxacin and ciprofloxacin increases and that of levofloxacin slightly decreases the binding constant of the HSA–tigecycline system. Competitive binding studies in the presence of site-specific markers showed that tigecycline was not significantly displaced by ibuprofen, but warfarin showed a significant displacement of tigecycline. These results suggest that the competitive binding of tigecycline and warfarin to HSA exists. The results confirm that the binding site of tigecycline is mainly located in Sudlow’s site I (subdomain IIA) of HSA. Graphic abstract: [Figure not available: see fulltext.
PB  - Springer
T2  - Monatshefte fur Chemie
T1  - Spectroscopic studies on the drug–drug interaction: the influence of fluoroquinolones on the affinity of tigecycline to human serum albumin and identification of the binding site
VL  - 151
SP  - 999
EP  - 1007
DO  - 10.1007/s00706-020-02627-0
ER  - 
@article{
author = "Stojanović, Stefan and Nićiforović, Jovan and Živanović, Sandra and Odović, Jadranka and Jelić, Ratomir",
year = "2020",
abstract = "bstract: Concomitant use of two or more drugs in therapy is becoming a more frequent phenomenon and clinically relevant drug–drug interactions at the level of binding to human serum albumin (HSA) are more often. The influence of fluoroquinolones–sparfloxacin, levofloxacin, and ciprofloxacin, on the interaction between tigecycline and HSA, was investigated in vitro by means of fluorescence and absorption spectroscopy. The results of UV–Vis and fluorescence spectroscopy showed that the fluorescence quenching of HSA was a result of the formation of new complexes through a static quenching process. The binding constants (Ka) and the number of binding sites (n) of all systems were calculated. The presence of sparfloxacin and ciprofloxacin increases and that of levofloxacin slightly decreases the binding constant of the HSA–tigecycline system. Competitive binding studies in the presence of site-specific markers showed that tigecycline was not significantly displaced by ibuprofen, but warfarin showed a significant displacement of tigecycline. These results suggest that the competitive binding of tigecycline and warfarin to HSA exists. The results confirm that the binding site of tigecycline is mainly located in Sudlow’s site I (subdomain IIA) of HSA. Graphic abstract: [Figure not available: see fulltext.",
publisher = "Springer",
journal = "Monatshefte fur Chemie",
title = "Spectroscopic studies on the drug–drug interaction: the influence of fluoroquinolones on the affinity of tigecycline to human serum albumin and identification of the binding site",
volume = "151",
pages = "999-1007",
doi = "10.1007/s00706-020-02627-0"
}
Stojanović, S., Nićiforović, J., Živanović, S., Odović, J.,& Jelić, R.. (2020). Spectroscopic studies on the drug–drug interaction: the influence of fluoroquinolones on the affinity of tigecycline to human serum albumin and identification of the binding site. in Monatshefte fur Chemie
Springer., 151, 999-1007.
https://doi.org/10.1007/s00706-020-02627-0
Stojanović S, Nićiforović J, Živanović S, Odović J, Jelić R. Spectroscopic studies on the drug–drug interaction: the influence of fluoroquinolones on the affinity of tigecycline to human serum albumin and identification of the binding site. in Monatshefte fur Chemie. 2020;151:999-1007.
doi:10.1007/s00706-020-02627-0 .
Stojanović, Stefan, Nićiforović, Jovan, Živanović, Sandra, Odović, Jadranka, Jelić, Ratomir, "Spectroscopic studies on the drug–drug interaction: the influence of fluoroquinolones on the affinity of tigecycline to human serum albumin and identification of the binding site" in Monatshefte fur Chemie, 151 (2020):999-1007,
https://doi.org/10.1007/s00706-020-02627-0 . .
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The effect of tigecycline on the binding of fluoroquinolones to human serum albumin

Jelić, Ratomir; Stojanović, Stefan D.; Berić, Jelena D.; Odović, Jadranka

(Univerzitet u Kragujevcu - Fakultet medicinskih nauka, Kragujevac, 2018)

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 . .
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