TY  - JOUR
AU  - Gajić, Mihajlo
AU  - Ilić, Budimir S.
AU  - Bondžić, Bojan
AU  - Džambaski, Zdravko
AU  - Filipović, Ana
AU  - Kocić, Gordana
AU  - Šmelcerović, Andrija
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6939
AB  - Xanthine oxidase (XO) is a versatile metalloflavoprotein enzyme that is best known for its rate-limiting role in the purine degradation pathway. Therapeutic inhibition of XO is based on its role in a variety of diseases that is attributed either to the hyperproduction of uric acid, or the hyperproduction of reactive oxygen species. Herein, we report the assessment of XO inhibitory properties of 24 1,2,3,4-tetrahydroisoquinoline derivatives, among which compound 
16 exhibited IC50 value of 135.72 ± 2.71 µM. The interaction of compound 16 with XO enzyme was simulated using the Site Finder module, molecular docking and molecular dynamics. Molecular modeling suggests that interactions with Met 1038, Gln 1040, Thr 1077, Gln 1194 and Val 1259 are an important factor for inhibitor affinity toward the XO enzyme. Our proposed binding model might be beneficial for the discovery of new active 1,2,3,4-tetrahydroisoquinoline-based inhibitors of XO enzyme.
AB  - Ksantin oksidaza (XO) je metaloflavoproteinski enzim, koji je najpoznatiji po svojoj ulozi ograničavanja brzine razgradnje purinskih nukleotida. Terapijska inhibicija XO zasniva se na njenoj ulozi u brojnim bolestima, koje su povezane bilo sa hiperprodukcijom mokraćne kiseline ili hiperprodukcijom reaktivnih kiseoničnih vrsta. U ovom radu izvršeno je ispitivanje sposobnosti inhibicije XO 24 derivata 1,2,3,4-tetrahidroizohinolina, od kojih je jedinjenje 16 pokazalo IC50 vrednost od 135,72 µM ± 2,71 µM. Interakcija jedinjenja 16 sa XO enzimom simulirana je korišćenjem Site Finder modula molekularnog dokinga i molekularne dinamike. Molekulsko modelovanje ukazuje na to da su interakcije sa Met 1038, Gln 1040, Thr 1077, Gln 1194 i Val 1259 važan faktor postojanja afiniteta inhibitora prema XO enzimu. Naš predloženi model vezivanja mogao bi biti od značaja za razvoj novih aktivnih inhibitora XO zasnovanih na 1,2,3,4-tetrahidroizohinolinskom heterociklusu.
PB  - Acta Medica Medianae
T2  - Acta Medica Medianae
T1  - Xanthine Oxidase Inhibitory Properties of 1,2,3,4–Tetrahydroisoquinoline Derivatives
T1  - Inhibicija ksantin oksidaze derivatima 1,2,3,4-tetrahidroizohinolina
VL  - 60
IS  - 1
SP  - 48
EP  - 55
DO  - 10.5633/amm.2021.0106
ER  - 

@article{
author = "Gajić, Mihajlo and Ilić, Budimir S. and Bondžić, Bojan and Džambaski, Zdravko and Filipović, Ana and Kocić, Gordana and Šmelcerović, Andrija",
year = "2021",
abstract = "Xanthine oxidase (XO) is a versatile metalloflavoprotein enzyme that is best known for its rate-limiting role in the purine degradation pathway. Therapeutic inhibition of XO is based on its role in a variety of diseases that is attributed either to the hyperproduction of uric acid, or the hyperproduction of reactive oxygen species. Herein, we report the assessment of XO inhibitory properties of 24 1,2,3,4-tetrahydroisoquinoline derivatives, among which compound 
16 exhibited IC50 value of 135.72 ± 2.71 µM. The interaction of compound 16 with XO enzyme was simulated using the Site Finder module, molecular docking and molecular dynamics. Molecular modeling suggests that interactions with Met 1038, Gln 1040, Thr 1077, Gln 1194 and Val 1259 are an important factor for inhibitor affinity toward the XO enzyme. Our proposed binding model might be beneficial for the discovery of new active 1,2,3,4-tetrahydroisoquinoline-based inhibitors of XO enzyme., Ksantin oksidaza (XO) je metaloflavoproteinski enzim, koji je najpoznatiji po svojoj ulozi ograničavanja brzine razgradnje purinskih nukleotida. Terapijska inhibicija XO zasniva se na njenoj ulozi u brojnim bolestima, koje su povezane bilo sa hiperprodukcijom mokraćne kiseline ili hiperprodukcijom reaktivnih kiseoničnih vrsta. U ovom radu izvršeno je ispitivanje sposobnosti inhibicije XO 24 derivata 1,2,3,4-tetrahidroizohinolina, od kojih je jedinjenje 16 pokazalo IC50 vrednost od 135,72 µM ± 2,71 µM. Interakcija jedinjenja 16 sa XO enzimom simulirana je korišćenjem Site Finder modula molekularnog dokinga i molekularne dinamike. Molekulsko modelovanje ukazuje na to da su interakcije sa Met 1038, Gln 1040, Thr 1077, Gln 1194 i Val 1259 važan faktor postojanja afiniteta inhibitora prema XO enzimu. Naš predloženi model vezivanja mogao bi biti od značaja za razvoj novih aktivnih inhibitora XO zasnovanih na 1,2,3,4-tetrahidroizohinolinskom heterociklusu.",
publisher = "Acta Medica Medianae",
journal = "Acta Medica Medianae",
title = "Xanthine Oxidase Inhibitory Properties of 1,2,3,4–Tetrahydroisoquinoline Derivatives, Inhibicija ksantin oksidaze derivatima 1,2,3,4-tetrahidroizohinolina",
volume = "60",
number = "1",
pages = "48-55",
doi = "10.5633/amm.2021.0106"
}

Gajić, M., Ilić, B. S., Bondžić, B., Džambaski, Z., Filipović, A., Kocić, G.,& Šmelcerović, A.. (2021). Xanthine Oxidase Inhibitory Properties of 1,2,3,4–Tetrahydroisoquinoline Derivatives. in Acta Medica Medianae
Acta Medica Medianae., 60(1), 48-55.
https://doi.org/10.5633/amm.2021.0106

Gajić M, Ilić BS, Bondžić B, Džambaski Z, Filipović A, Kocić G, Šmelcerović A. Xanthine Oxidase Inhibitory Properties of 1,2,3,4–Tetrahydroisoquinoline Derivatives. in Acta Medica Medianae. 2021;60(1):48-55.
doi:10.5633/amm.2021.0106 .

Gajić, Mihajlo, Ilić, Budimir S., Bondžić, Bojan, Džambaski, Zdravko, Filipović, Ana, Kocić, Gordana, Šmelcerović, Andrija, "Xanthine Oxidase Inhibitory Properties of 1,2,3,4–Tetrahydroisoquinoline Derivatives" in Acta Medica Medianae, 60, no. 1 (2021):48-55,
https://doi.org/10.5633/amm.2021.0106 . .

TY  - JOUR
AU  - Ilić, Budimir S.
AU  - Gajić, Mihajlo
AU  - Bondžić, Bojan
AU  - Džambaski, Zdravko
AU  - Kocić, Gordana
AU  - Šmelcerović, Andrija
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4498
AB  - Deoxyribonuclease I (DNase I) inhibitory properties of two 1-(pyrrolidin-2-yl)propan-2-one derivatives were examined in vitro. Determined IC50 values of 1-[1-(4-methoxyphenyl)pyrrolidin-2-yl]propan-2-one (1) (192.13±16.95 μM) and 1-[1-(3,4,5-trimethoxyphenyl)pyrrolidin-2-yl]propan-2-one (2) (132.62±9.92 μM) exceed IC50 value of crystal violet, used as a positive control, 1.89- and 2.73-times, respectively. Compounds are predicted to be nontoxic and to have favorable pharmacokinetic profiles, with high gastrointestinal absorption and blood-brain barrier permeability. Molecular docking and molecular dynamics simulations suggest that interactions with Glu 39, Glu 78, Arg 111, Pro 137, Asp 251 and His 252 are an important factor for inhibitors affinity toward the DNase I. Determined inhibitory properties along with predicted ADMET profiles and observed interactions would be beneficial for the discovery of new active 1-(pyrrolidin-2-yl)propan-2-one-based inhibitors of DNase I.
PB  - Switzerland :Wiley-Blackwell
T2  - Chemistry and Biodisversity
T1  - Deoxyribonuclease I Inhibitory Properties, Molecular Docking and Molecular Dynamics Simulations of 1-(Pyrrolidin-2-yl)propan-2-one Derivatives
VL  - 18
IS  - 3
SP  - e2000996
DO  - 10.1002/cbdv.202000996
ER  - 

@article{
author = "Ilić, Budimir S. and Gajić, Mihajlo and Bondžić, Bojan and Džambaski, Zdravko and Kocić, Gordana and Šmelcerović, Andrija",
year = "2021",
abstract = "Deoxyribonuclease I (DNase I) inhibitory properties of two 1-(pyrrolidin-2-yl)propan-2-one derivatives were examined in vitro. Determined IC50 values of 1-[1-(4-methoxyphenyl)pyrrolidin-2-yl]propan-2-one (1) (192.13±16.95 μM) and 1-[1-(3,4,5-trimethoxyphenyl)pyrrolidin-2-yl]propan-2-one (2) (132.62±9.92 μM) exceed IC50 value of crystal violet, used as a positive control, 1.89- and 2.73-times, respectively. Compounds are predicted to be nontoxic and to have favorable pharmacokinetic profiles, with high gastrointestinal absorption and blood-brain barrier permeability. Molecular docking and molecular dynamics simulations suggest that interactions with Glu 39, Glu 78, Arg 111, Pro 137, Asp 251 and His 252 are an important factor for inhibitors affinity toward the DNase I. Determined inhibitory properties along with predicted ADMET profiles and observed interactions would be beneficial for the discovery of new active 1-(pyrrolidin-2-yl)propan-2-one-based inhibitors of DNase I.",
publisher = "Switzerland :Wiley-Blackwell",
journal = "Chemistry and Biodisversity",
title = "Deoxyribonuclease I Inhibitory Properties, Molecular Docking and Molecular Dynamics Simulations of 1-(Pyrrolidin-2-yl)propan-2-one Derivatives",
volume = "18",
number = "3",
pages = "e2000996",
doi = "10.1002/cbdv.202000996"
}

Ilić, B. S., Gajić, M., Bondžić, B., Džambaski, Z., Kocić, G.,& Šmelcerović, A.. (2021). Deoxyribonuclease I Inhibitory Properties, Molecular Docking and Molecular Dynamics Simulations of 1-(Pyrrolidin-2-yl)propan-2-one Derivatives. in Chemistry and Biodisversity
Switzerland :Wiley-Blackwell., 18(3), e2000996.
https://doi.org/10.1002/cbdv.202000996

Ilić BS, Gajić M, Bondžić B, Džambaski Z, Kocić G, Šmelcerović A. Deoxyribonuclease I Inhibitory Properties, Molecular Docking and Molecular Dynamics Simulations of 1-(Pyrrolidin-2-yl)propan-2-one Derivatives. in Chemistry and Biodisversity. 2021;18(3):e2000996.
doi:10.1002/cbdv.202000996 .

Ilić, Budimir S., Gajić, Mihajlo, Bondžić, Bojan, Džambaski, Zdravko, Kocić, Gordana, Šmelcerović, Andrija, "Deoxyribonuclease I Inhibitory Properties, Molecular Docking and Molecular Dynamics Simulations of 1-(Pyrrolidin-2-yl)propan-2-one Derivatives" in Chemistry and Biodisversity, 18, no. 3 (2021):e2000996,
https://doi.org/10.1002/cbdv.202000996 . .

TY  - DATA
AU  - Ilić, Budimir S.
AU  - Gajić, Mihajlo
AU  - Bondžić, Bojan
AU  - Džambaski, Zdravko
AU  - Kocić, Gordana
AU  - Šmelcerović, Andrija
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4499
AB  - Experimental Section: 1.1. Chemicals. 1.2. Compounds. 1.3. Evaluation of deoxyribonuclease I inhibition. 1.4. In silico molecular and ADMET properties. 1.5. In silico PAINS and promiscuity assessment. 1.6. Molecular docking. 1.6.1. Ligand preparation. 1.6.2. Receptor preparation  1.6.3. Binding site selection 1.6.4. Docking protocol 1.7. Molecular dynamics simulation . Table S1. Summary of the top five inhibitor-binding sites in DNase I. Additional references.
PB  - Switzerland : Wiley-Blackwell
T2  - Chemistry and Biodisversity
T1  - Supporting information for: "Deoxyribonuclease I Inhibitory Properties, Molecular Docking and Molecular Dynamics Simulations of 1-(Pyrrolidin-2-yl)propan-2-one Derivatives"
UR  - https://hdl.handle.net/21.15107/rcub_cer_4499
ER  - 

@misc{
author = "Ilić, Budimir S. and Gajić, Mihajlo and Bondžić, Bojan and Džambaski, Zdravko and Kocić, Gordana and Šmelcerović, Andrija",
year = "2021",
abstract = "Experimental Section: 1.1. Chemicals. 1.2. Compounds. 1.3. Evaluation of deoxyribonuclease I inhibition. 1.4. In silico molecular and ADMET properties. 1.5. In silico PAINS and promiscuity assessment. 1.6. Molecular docking. 1.6.1. Ligand preparation. 1.6.2. Receptor preparation  1.6.3. Binding site selection 1.6.4. Docking protocol 1.7. Molecular dynamics simulation . Table S1. Summary of the top five inhibitor-binding sites in DNase I. Additional references.",
publisher = "Switzerland : Wiley-Blackwell",
journal = "Chemistry and Biodisversity",
title = "Supporting information for: "Deoxyribonuclease I Inhibitory Properties, Molecular Docking and Molecular Dynamics Simulations of 1-(Pyrrolidin-2-yl)propan-2-one Derivatives"",
url = "https://hdl.handle.net/21.15107/rcub_cer_4499"
}

Ilić, B. S., Gajić, M., Bondžić, B., Džambaski, Z., Kocić, G.,& Šmelcerović, A.. (2021). Supporting information for: "Deoxyribonuclease I Inhibitory Properties, Molecular Docking and Molecular Dynamics Simulations of 1-(Pyrrolidin-2-yl)propan-2-one Derivatives". in Chemistry and Biodisversity
Switzerland : Wiley-Blackwell..
https://hdl.handle.net/21.15107/rcub_cer_4499

Ilić BS, Gajić M, Bondžić B, Džambaski Z, Kocić G, Šmelcerović A. Supporting information for: "Deoxyribonuclease I Inhibitory Properties, Molecular Docking and Molecular Dynamics Simulations of 1-(Pyrrolidin-2-yl)propan-2-one Derivatives". in Chemistry and Biodisversity. 2021;.
https://hdl.handle.net/21.15107/rcub_cer_4499 .

Ilić, Budimir S., Gajić, Mihajlo, Bondžić, Bojan, Džambaski, Zdravko, Kocić, Gordana, Šmelcerović, Andrija, "Supporting information for: "Deoxyribonuclease I Inhibitory Properties, Molecular Docking and Molecular Dynamics Simulations of 1-(Pyrrolidin-2-yl)propan-2-one Derivatives"" in Chemistry and Biodisversity (2021),
https://hdl.handle.net/21.15107/rcub_cer_4499 .

TY  - DATA
AU  - Ilić, Budimir S.
AU  - Gajić, Mihajlo
AU  - Bondžić, Bojan
AU  - Džambaski, Zdravko
AU  - Kocić, Gordana
AU  - Šmelcerović, Andrija
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4500
AB  - Animation of molecular dynamics simulations: 1‐[1‐(4‐methoxyphenyl)pyrrolidin‐2‐yl]propan‐2‐one / DNase I
PB  - Switzerland : Wiley-Blackwell
T2  - Chemistry and Biodisversity
T1  - Supporting data for: "Deoxyribonuclease I Inhibitory Properties, Molecular Docking and Molecular Dynamics Simulations of 1-(Pyrrolidin-2-yl)propan-2-one Derivatives". Animation of molecular dynamics simulations I.
UR  - https://hdl.handle.net/21.15107/rcub_cer_4500
ER  - 

@misc{
author = "Ilić, Budimir S. and Gajić, Mihajlo and Bondžić, Bojan and Džambaski, Zdravko and Kocić, Gordana and Šmelcerović, Andrija",
year = "2021",
abstract = "Animation of molecular dynamics simulations: 1‐[1‐(4‐methoxyphenyl)pyrrolidin‐2‐yl]propan‐2‐one / DNase I",
publisher = "Switzerland : Wiley-Blackwell",
journal = "Chemistry and Biodisversity",
title = "Supporting data for: "Deoxyribonuclease I Inhibitory Properties, Molecular Docking and Molecular Dynamics Simulations of 1-(Pyrrolidin-2-yl)propan-2-one Derivatives". Animation of molecular dynamics simulations I.",
url = "https://hdl.handle.net/21.15107/rcub_cer_4500"
}

Ilić, B. S., Gajić, M., Bondžić, B., Džambaski, Z., Kocić, G.,& Šmelcerović, A.. (2021). Supporting data for: "Deoxyribonuclease I Inhibitory Properties, Molecular Docking and Molecular Dynamics Simulations of 1-(Pyrrolidin-2-yl)propan-2-one Derivatives". Animation of molecular dynamics simulations I.. in Chemistry and Biodisversity
Switzerland : Wiley-Blackwell..
https://hdl.handle.net/21.15107/rcub_cer_4500

Ilić BS, Gajić M, Bondžić B, Džambaski Z, Kocić G, Šmelcerović A. Supporting data for: "Deoxyribonuclease I Inhibitory Properties, Molecular Docking and Molecular Dynamics Simulations of 1-(Pyrrolidin-2-yl)propan-2-one Derivatives". Animation of molecular dynamics simulations I.. in Chemistry and Biodisversity. 2021;.
https://hdl.handle.net/21.15107/rcub_cer_4500 .

Ilić, Budimir S., Gajić, Mihajlo, Bondžić, Bojan, Džambaski, Zdravko, Kocić, Gordana, Šmelcerović, Andrija, "Supporting data for: "Deoxyribonuclease I Inhibitory Properties, Molecular Docking and Molecular Dynamics Simulations of 1-(Pyrrolidin-2-yl)propan-2-one Derivatives". Animation of molecular dynamics simulations I." in Chemistry and Biodisversity (2021),
https://hdl.handle.net/21.15107/rcub_cer_4500 .

TY  - DATA
AU  - Ilić, Budimir S.
AU  - Gajić, Mihajlo
AU  - Bondžić, Bojan
AU  - Džambaski, Zdravko
AU  - Kocić, Gordana
AU  - Šmelcerović, Andrija
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4501
AB  - Animation of molecular dynamics simulations: 1‐[1‐(3,4,5‐trimethoxyphenyl)pyrrolidin‐2‐yl]propan‐2‐one / DNase I
PB  - Switzerland : Wiley-Blackwell
T2  - Chemistry and Biodisversity
T1  - Supporting data for: "Deoxyribonuclease I Inhibitory Properties, Molecular Docking and Molecular Dynamics Simulations of 1-(Pyrrolidin-2-yl)propan-2-one Derivatives". Animation of molecular dynamics simulations II.
UR  - https://hdl.handle.net/21.15107/rcub_cer_4501
ER  - 

@misc{
author = "Ilić, Budimir S. and Gajić, Mihajlo and Bondžić, Bojan and Džambaski, Zdravko and Kocić, Gordana and Šmelcerović, Andrija",
year = "2021",
abstract = "Animation of molecular dynamics simulations: 1‐[1‐(3,4,5‐trimethoxyphenyl)pyrrolidin‐2‐yl]propan‐2‐one / DNase I",
publisher = "Switzerland : Wiley-Blackwell",
journal = "Chemistry and Biodisversity",
title = "Supporting data for: "Deoxyribonuclease I Inhibitory Properties, Molecular Docking and Molecular Dynamics Simulations of 1-(Pyrrolidin-2-yl)propan-2-one Derivatives". Animation of molecular dynamics simulations II.",
url = "https://hdl.handle.net/21.15107/rcub_cer_4501"
}

Ilić, B. S., Gajić, M., Bondžić, B., Džambaski, Z., Kocić, G.,& Šmelcerović, A.. (2021). Supporting data for: "Deoxyribonuclease I Inhibitory Properties, Molecular Docking and Molecular Dynamics Simulations of 1-(Pyrrolidin-2-yl)propan-2-one Derivatives". Animation of molecular dynamics simulations II.. in Chemistry and Biodisversity
Switzerland : Wiley-Blackwell..
https://hdl.handle.net/21.15107/rcub_cer_4501

Ilić BS, Gajić M, Bondžić B, Džambaski Z, Kocić G, Šmelcerović A. Supporting data for: "Deoxyribonuclease I Inhibitory Properties, Molecular Docking and Molecular Dynamics Simulations of 1-(Pyrrolidin-2-yl)propan-2-one Derivatives". Animation of molecular dynamics simulations II.. in Chemistry and Biodisversity. 2021;.
https://hdl.handle.net/21.15107/rcub_cer_4501 .

Ilić, Budimir S., Gajić, Mihajlo, Bondžić, Bojan, Džambaski, Zdravko, Kocić, Gordana, Šmelcerović, Andrija, "Supporting data for: "Deoxyribonuclease I Inhibitory Properties, Molecular Docking and Molecular Dynamics Simulations of 1-(Pyrrolidin-2-yl)propan-2-one Derivatives". Animation of molecular dynamics simulations II." in Chemistry and Biodisversity (2021),
https://hdl.handle.net/21.15107/rcub_cer_4501 .

TY  - JOUR
AU  - Gajić, Mihajlo
AU  - Džambaski, Zdravko
AU  - Ilić, Budimir S.
AU  - Kocić, Gordana
AU  - Bondžić, Bojan
AU  - Šmelcerović, Andrija
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4729
AB  - In this study, seven new 4-oxothiazolidine derivatives were synthesized and assayed, along 7 known derivatives, for inhibitory properties against deoxyribonuclease I (DNase I) and xanthine oxidase (XO) in vitro. Among tested compounds, (5Z)-Ethyl-2-(2-(cyanomethylene)-4-oxothiazolidin-5-yliden)acetate (6) exhibited inhibitory activity against both enzymes (DNase I IC50 = 67.94 ± 5.99 μM; XO IC50 = 98.98 ± 13.47 μM), therefore being the first reported dual inhibitor of DNase I and XO. Observed DNase I inhibition qualifies compound 6 as the most potent small organic DNase I inhibitor reported so far. Derivatives of 2-alkyliden-4-oxothiazolidinone (1) inhibited DNase I below 200 μM, while the other tested 4-oxothiazolidine derivatives remained inactive against both enzymes. The molecular docking and molecular dynamics simulations into the binding sites of DNase I and XO enzyme allowed us to clarify the binding modes of this 4-oxothiazolidine derivative, which might aid future development of dual DNase I and XO.
PB  - Elsevier
T2  - Chemico-Biological Interactions
T1  - Synthesis and analysis of 4-oxothiazolidines as potential dual inhibitors of deoxyribonuclease I and xanthine oxidase
VL  - 345
SP  - 109536
DO  - 10.1016/j.cbi.2021.109536
ER  - 

@article{
author = "Gajić, Mihajlo and Džambaski, Zdravko and Ilić, Budimir S. and Kocić, Gordana and Bondžić, Bojan and Šmelcerović, Andrija",
year = "2021",
abstract = "In this study, seven new 4-oxothiazolidine derivatives were synthesized and assayed, along 7 known derivatives, for inhibitory properties against deoxyribonuclease I (DNase I) and xanthine oxidase (XO) in vitro. Among tested compounds, (5Z)-Ethyl-2-(2-(cyanomethylene)-4-oxothiazolidin-5-yliden)acetate (6) exhibited inhibitory activity against both enzymes (DNase I IC50 = 67.94 ± 5.99 μM; XO IC50 = 98.98 ± 13.47 μM), therefore being the first reported dual inhibitor of DNase I and XO. Observed DNase I inhibition qualifies compound 6 as the most potent small organic DNase I inhibitor reported so far. Derivatives of 2-alkyliden-4-oxothiazolidinone (1) inhibited DNase I below 200 μM, while the other tested 4-oxothiazolidine derivatives remained inactive against both enzymes. The molecular docking and molecular dynamics simulations into the binding sites of DNase I and XO enzyme allowed us to clarify the binding modes of this 4-oxothiazolidine derivative, which might aid future development of dual DNase I and XO.",
publisher = "Elsevier",
journal = "Chemico-Biological Interactions",
title = "Synthesis and analysis of 4-oxothiazolidines as potential dual inhibitors of deoxyribonuclease I and xanthine oxidase",
volume = "345",
pages = "109536",
doi = "10.1016/j.cbi.2021.109536"
}

Gajić, M., Džambaski, Z., Ilić, B. S., Kocić, G., Bondžić, B.,& Šmelcerović, A.. (2021). Synthesis and analysis of 4-oxothiazolidines as potential dual inhibitors of deoxyribonuclease I and xanthine oxidase. in Chemico-Biological Interactions
Elsevier., 345, 109536.
https://doi.org/10.1016/j.cbi.2021.109536

Gajić M, Džambaski Z, Ilić BS, Kocić G, Bondžić B, Šmelcerović A. Synthesis and analysis of 4-oxothiazolidines as potential dual inhibitors of deoxyribonuclease I and xanthine oxidase. in Chemico-Biological Interactions. 2021;345:109536.
doi:10.1016/j.cbi.2021.109536 .

Gajić, Mihajlo, Džambaski, Zdravko, Ilić, Budimir S., Kocić, Gordana, Bondžić, Bojan, Šmelcerović, Andrija, "Synthesis and analysis of 4-oxothiazolidines as potential dual inhibitors of deoxyribonuclease I and xanthine oxidase" in Chemico-Biological Interactions, 345 (2021):109536,
https://doi.org/10.1016/j.cbi.2021.109536 . .

TY  - JOUR
AU  - Gajić, Mihajlo
AU  - Ilić, Budimir S.
AU  - Bondžić, Bojan
AU  - Džambaski, Zdravko
AU  - Kojić, Vesna V.
AU  - Jakimov, Dimitar S.
AU  - Kocić, Gordana
AU  - Šmelcerović, Andrija
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4815
AB  - Herein we report an assessment of 24 1,2,3,4-tetrahydroisoquinoline derivatives for potential DNase I (deoxyribonuclease I) inhibitory properties in vitro. Four of them inhibited DNase I with IC50 values below 200 μM. The most potent was 1-(6,7-dimethoxy-1,2,3,4-tetrahydroisoquinolin-1-yl)propan-2-one (2) (IC50=134.35±11.38 μM) exhibiting slightly better IC50 value compared to three other active compounds, 2-[2-(4-fluorophenyl)-1,2,3,4-tetrahydroisoquinolin-1-yl]-1-phenylethan-1-one (15) (IC50=147.51±14.87 μM), 2-[2-(4-fluorophenyl)-1,2,3,4-tetrahydroisoquinolin-1-yl]cyclohexan-1-one (18) (IC50=149.07±2.98 μM) and 2-[6,7-dimethoxy-2-(p-tolyl)-1,2,3,4-tetrahydroisoquinolin-1-yl]cyclohexan-1-one (22) (IC50=148.31±2.96 μM). Cytotoxicity assessment of the active DNase I inhibitors revealed a lack of toxic effects on the healthy cell lines MRC-5. Molecular docking and molecular dynamics simulations suggest that interactions with Glu 39, His 134, Asn 170, Tyr 211, Asp 251 and His 252 are an important factor for inhibitors affinity toward the DNase I. Observed interactions would be beneficial for the discovery of new active 1,2,3,4-tetrahydroisoquinoline-based inhibitors of DNase I, but might also encourage researchers to further explore and utilize potential therapeutic application of DNase I inhibitors, based on a versatile role of DNase I during apoptotic cell death.
PB  - Wiley
T2  - Chemistry and Biodisversity
T1  - 1,2,3,4-Tetrahydroisoquinoline Derivatives as a Novel Deoxyribonuclease I Inhibitors
VL  - 18
IS  - 8
SP  - e2100261
DO  - 10.1002/cbdv.202100261
ER  - 

@article{
author = "Gajić, Mihajlo and Ilić, Budimir S. and Bondžić, Bojan and Džambaski, Zdravko and Kojić, Vesna V. and Jakimov, Dimitar S. and Kocić, Gordana and Šmelcerović, Andrija",
year = "2021",
abstract = "Herein we report an assessment of 24 1,2,3,4-tetrahydroisoquinoline derivatives for potential DNase I (deoxyribonuclease I) inhibitory properties in vitro. Four of them inhibited DNase I with IC50 values below 200 μM. The most potent was 1-(6,7-dimethoxy-1,2,3,4-tetrahydroisoquinolin-1-yl)propan-2-one (2) (IC50=134.35±11.38 μM) exhibiting slightly better IC50 value compared to three other active compounds, 2-[2-(4-fluorophenyl)-1,2,3,4-tetrahydroisoquinolin-1-yl]-1-phenylethan-1-one (15) (IC50=147.51±14.87 μM), 2-[2-(4-fluorophenyl)-1,2,3,4-tetrahydroisoquinolin-1-yl]cyclohexan-1-one (18) (IC50=149.07±2.98 μM) and 2-[6,7-dimethoxy-2-(p-tolyl)-1,2,3,4-tetrahydroisoquinolin-1-yl]cyclohexan-1-one (22) (IC50=148.31±2.96 μM). Cytotoxicity assessment of the active DNase I inhibitors revealed a lack of toxic effects on the healthy cell lines MRC-5. Molecular docking and molecular dynamics simulations suggest that interactions with Glu 39, His 134, Asn 170, Tyr 211, Asp 251 and His 252 are an important factor for inhibitors affinity toward the DNase I. Observed interactions would be beneficial for the discovery of new active 1,2,3,4-tetrahydroisoquinoline-based inhibitors of DNase I, but might also encourage researchers to further explore and utilize potential therapeutic application of DNase I inhibitors, based on a versatile role of DNase I during apoptotic cell death.",
publisher = "Wiley",
journal = "Chemistry and Biodisversity",
title = "1,2,3,4-Tetrahydroisoquinoline Derivatives as a Novel Deoxyribonuclease I Inhibitors",
volume = "18",
number = "8",
pages = "e2100261",
doi = "10.1002/cbdv.202100261"
}

Gajić, M., Ilić, B. S., Bondžić, B., Džambaski, Z., Kojić, V. V., Jakimov, D. S., Kocić, G.,& Šmelcerović, A.. (2021). 1,2,3,4-Tetrahydroisoquinoline Derivatives as a Novel Deoxyribonuclease I Inhibitors. in Chemistry and Biodisversity
Wiley., 18(8), e2100261.
https://doi.org/10.1002/cbdv.202100261

Gajić M, Ilić BS, Bondžić B, Džambaski Z, Kojić VV, Jakimov DS, Kocić G, Šmelcerović A. 1,2,3,4-Tetrahydroisoquinoline Derivatives as a Novel Deoxyribonuclease I Inhibitors. in Chemistry and Biodisversity. 2021;18(8):e2100261.
doi:10.1002/cbdv.202100261 .

Gajić, Mihajlo, Ilić, Budimir S., Bondžić, Bojan, Džambaski, Zdravko, Kojić, Vesna V., Jakimov, Dimitar S., Kocić, Gordana, Šmelcerović, Andrija, "1,2,3,4-Tetrahydroisoquinoline Derivatives as a Novel Deoxyribonuclease I Inhibitors" in Chemistry and Biodisversity, 18, no. 8 (2021):e2100261,
https://doi.org/10.1002/cbdv.202100261 . .

TY  - JOUR
AU  - Kolarević, Ana
AU  - Ilić, Budimir S.
AU  - Kocić, Gordana
AU  - Džambaski, Zdravko
AU  - Šmelcerović, Andrija
AU  - Bondžić, Bojan
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2998
AB  - Twelve new thiazolidinones were synthesized and, together with 41 previously
synthesized thiazolidinones, evaluated for inhibitory activity against deoxyribonuclease I (DNase I) in vitro. Ten compounds inhibited commercial bovine pancreatic DNase I with an IC50 below 200 μM and showed to be more potent DNase I inhibitors than crystal violet (IC50 = 365.90 ± 47.33 μM), used as a positive control. Moreover, three compounds were active against DNase I in rat
liver homogenate, having an IC50 below 200 μM. (3‐Methyl‐1,4‐dioxothiazolidin‐2‐ylidene)‐N‐(2‐phenylethyl)ethanamide (41) exhibited the most potent DNase I inhibition against both commercial and rat liver DNase I with IC50 values of 115.96 ± 11.70 and 151.36 ± 15.85 μM, respectively. Site Finder and molecular docking defined the thiazolidinones interactions with the most important catalytic residues of DNase I, including the H‐acceptor interaction with residues His 134 and His 252 and/or H‐donor interaction with residues Glu 39 and Asp 168. The three most active compounds against both commercial and rat liver DNase I (31, 38, and 41) exhibited favorable physico‐chemical, pharmacokinetic, and toxicological properties. These observations could be
utilized to guide the rational design and optimization of novel thiazolidinone inhibitors. Thiazolidinones as novel DNase I inhibitors could have potential therapeutic applications due to the significant involvement of DNase I in the pathophysiology of many disease conditions.
PB  - Wiley
T2  - Journal of Cellular Biochemistry
T1  - Synthesis and DNase I inhibitory properties of some 4‐thiazolidinone derivatives
VL  - 120
IS  - 1
SP  - 264
EP  - 274
DO  - 10.1002/jcb.27339
ER  - 

@article{
author = "Kolarević, Ana and Ilić, Budimir S. and Kocić, Gordana and Džambaski, Zdravko and Šmelcerović, Andrija and Bondžić, Bojan",
year = "2018",
abstract = "Twelve new thiazolidinones were synthesized and, together with 41 previously
synthesized thiazolidinones, evaluated for inhibitory activity against deoxyribonuclease I (DNase I) in vitro. Ten compounds inhibited commercial bovine pancreatic DNase I with an IC50 below 200 μM and showed to be more potent DNase I inhibitors than crystal violet (IC50 = 365.90 ± 47.33 μM), used as a positive control. Moreover, three compounds were active against DNase I in rat
liver homogenate, having an IC50 below 200 μM. (3‐Methyl‐1,4‐dioxothiazolidin‐2‐ylidene)‐N‐(2‐phenylethyl)ethanamide (41) exhibited the most potent DNase I inhibition against both commercial and rat liver DNase I with IC50 values of 115.96 ± 11.70 and 151.36 ± 15.85 μM, respectively. Site Finder and molecular docking defined the thiazolidinones interactions with the most important catalytic residues of DNase I, including the H‐acceptor interaction with residues His 134 and His 252 and/or H‐donor interaction with residues Glu 39 and Asp 168. The three most active compounds against both commercial and rat liver DNase I (31, 38, and 41) exhibited favorable physico‐chemical, pharmacokinetic, and toxicological properties. These observations could be
utilized to guide the rational design and optimization of novel thiazolidinone inhibitors. Thiazolidinones as novel DNase I inhibitors could have potential therapeutic applications due to the significant involvement of DNase I in the pathophysiology of many disease conditions.",
publisher = "Wiley",
journal = "Journal of Cellular Biochemistry",
title = "Synthesis and DNase I inhibitory properties of some 4‐thiazolidinone derivatives",
volume = "120",
number = "1",
pages = "264-274",
doi = "10.1002/jcb.27339"
}

Kolarević, A., Ilić, B. S., Kocić, G., Džambaski, Z., Šmelcerović, A.,& Bondžić, B.. (2018). Synthesis and DNase I inhibitory properties of some 4‐thiazolidinone derivatives. in Journal of Cellular Biochemistry
Wiley., 120(1), 264-274.
https://doi.org/10.1002/jcb.27339

Kolarević A, Ilić BS, Kocić G, Džambaski Z, Šmelcerović A, Bondžić B. Synthesis and DNase I inhibitory properties of some 4‐thiazolidinone derivatives. in Journal of Cellular Biochemistry. 2018;120(1):264-274.
doi:10.1002/jcb.27339 .

Kolarević, Ana, Ilić, Budimir S., Kocić, Gordana, Džambaski, Zdravko, Šmelcerović, Andrija, Bondžić, Bojan, "Synthesis and DNase I inhibitory properties of some 4‐thiazolidinone derivatives" in Journal of Cellular Biochemistry, 120, no. 1 (2018):264-274,
https://doi.org/10.1002/jcb.27339 . .