Đurković, Filip T.

Link to this page

http://cherry.chem.bg.ac.rs/APP/faces/author.xhtml?author_id=orcid%3A%3A0000-0003-1507-1277&item_offset=0&project_offset=0&sort_by=dc.date.issued
Authority KeyName Variants
orcid::0000-0003-1507-1277
  • Đurković, Filip T. (5)
Projects

Author's Bibliography

Development of iminosugar-based glycosidase inhibitors as drug candidates for SARS-CoV-2 virus via molecular modelling and in vitro studies

Ferjančić, Zorana; Bihelović, Filip; Vulović, Bojan; Matović, Radomir; Trmčić, Milena; Jankovic, Aleksandar; Pavlovic, Milos; Đurković, Filip T.; Prodanović, Radivoje; Djurdjevic Djelmas, Aleksandra; Kalicanin, Nevena; Zlatović, Mario; Sladić, Dušan; Vallet, Thomas; Vignuzzi, Marco; Saicic, Radomir N.

(Taylor and Francis Group, 2024) 

TY  - JOUR
AU  - Ferjančić, Zorana
AU  - Bihelović, Filip
AU  - Vulović, Bojan
AU  - Matović, Radomir
AU  - Trmčić, Milena
AU  - Jankovic, Aleksandar
AU  - Pavlovic, Milos
AU  - Đurković, Filip T.
AU  - Prodanović, Radivoje
AU  - Djurdjevic Djelmas, Aleksandra
AU  - Kalicanin, Nevena
AU  - Zlatović, Mario
AU  - Sladić, Dušan
AU  - Vallet, Thomas
AU  - Vignuzzi, Marco
AU  - Saicic, Radomir N.
PY  - 2024
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6475
AB  - We developed new iminosugar-based glycosidase inhibitors against SARS-CoV-2. Known drugs (miglustat, migalastat, miglitol, and swainsonine) were chosen as lead compounds to develop three classes of glycosidase inhibitors (α-glucosidase, α-galactosidase, and mannosidase). Molecular modelling of the lead compounds, synthesis of the compounds with the highest docking scores, enzyme inhibition tests, and in vitro antiviral assays afforded rationally designed inhibitors. Two highly active α-glucosidase inhibitors were discovered, where one of them is the most potent iminosugar-based anti-SARS-CoV-2 agent to date (EC90 = 1.94 µM in A549-ACE2 cells against Omicron BA.1 strain). However, galactosidase inhibitors did not exhibit antiviral activity, whereas mannosidase inhibitors were both active and cytotoxic. As our iminosugar-based drug candidates act by a host-directed mechanism, they should be more resilient to drug resistance. Moreover, this strategy could be extended to identify potential drug candidates for other viral infections.
PB  - Taylor and Francis Group
T2  - Journal of Enzyme Inhibition and Medicinal Chemistry
T1  - Development of iminosugar-based glycosidase inhibitors as drug candidates for SARS-CoV-2 virus via molecular modelling and in vitro studies
VL  - 39
IS  - 1
SP  - 2289007
DO  - 10.1080/14756366.2023.2289007
ER  - 
@article{
author = "Ferjančić, Zorana and Bihelović, Filip and Vulović, Bojan and Matović, Radomir and Trmčić, Milena and Jankovic, Aleksandar and Pavlovic, Milos and Đurković, Filip T. and Prodanović, Radivoje and Djurdjevic Djelmas, Aleksandra and Kalicanin, Nevena and Zlatović, Mario and Sladić, Dušan and Vallet, Thomas and Vignuzzi, Marco and Saicic, Radomir N.",
year = "2024",
abstract = "We developed new iminosugar-based glycosidase inhibitors against SARS-CoV-2. Known drugs (miglustat, migalastat, miglitol, and swainsonine) were chosen as lead compounds to develop three classes of glycosidase inhibitors (α-glucosidase, α-galactosidase, and mannosidase). Molecular modelling of the lead compounds, synthesis of the compounds with the highest docking scores, enzyme inhibition tests, and in vitro antiviral assays afforded rationally designed inhibitors. Two highly active α-glucosidase inhibitors were discovered, where one of them is the most potent iminosugar-based anti-SARS-CoV-2 agent to date (EC90 = 1.94 µM in A549-ACE2 cells against Omicron BA.1 strain). However, galactosidase inhibitors did not exhibit antiviral activity, whereas mannosidase inhibitors were both active and cytotoxic. As our iminosugar-based drug candidates act by a host-directed mechanism, they should be more resilient to drug resistance. Moreover, this strategy could be extended to identify potential drug candidates for other viral infections.",
publisher = "Taylor and Francis Group",
journal = "Journal of Enzyme Inhibition and Medicinal Chemistry",
title = "Development of iminosugar-based glycosidase inhibitors as drug candidates for SARS-CoV-2 virus via molecular modelling and in vitro studies",
volume = "39",
number = "1",
pages = "2289007",
doi = "10.1080/14756366.2023.2289007"
}
Ferjančić, Z., Bihelović, F., Vulović, B., Matović, R., Trmčić, M., Jankovic, A., Pavlovic, M., Đurković, F. T., Prodanović, R., Djurdjevic Djelmas, A., Kalicanin, N., Zlatović, M., Sladić, D., Vallet, T., Vignuzzi, M.,& Saicic, R. N.. (2024). Development of iminosugar-based glycosidase inhibitors as drug candidates for SARS-CoV-2 virus via molecular modelling and in vitro studies. in Journal of Enzyme Inhibition and Medicinal Chemistry
Taylor and Francis Group., 39(1), 2289007.
https://doi.org/10.1080/14756366.2023.2289007
Ferjančić Z, Bihelović F, Vulović B, Matović R, Trmčić M, Jankovic A, Pavlovic M, Đurković FT, Prodanović R, Djurdjevic Djelmas A, Kalicanin N, Zlatović M, Sladić D, Vallet T, Vignuzzi M, Saicic RN. Development of iminosugar-based glycosidase inhibitors as drug candidates for SARS-CoV-2 virus via molecular modelling and in vitro studies. in Journal of Enzyme Inhibition and Medicinal Chemistry. 2024;39(1):2289007.
doi:10.1080/14756366.2023.2289007 .
Ferjančić, Zorana, Bihelović, Filip, Vulović, Bojan, Matović, Radomir, Trmčić, Milena, Jankovic, Aleksandar, Pavlovic, Milos, Đurković, Filip T., Prodanović, Radivoje, Djurdjevic Djelmas, Aleksandra, Kalicanin, Nevena, Zlatović, Mario, Sladić, Dušan, Vallet, Thomas, Vignuzzi, Marco, Saicic, Radomir N., "Development of iminosugar-based glycosidase inhibitors as drug candidates for SARS-CoV-2 virus via molecular modelling and in vitro studies" in Journal of Enzyme Inhibition and Medicinal Chemistry, 39, no. 1 (2024):2289007,
https://doi.org/10.1080/14756366.2023.2289007 . .
4
1

Sintetičke studije za dobijanje (+)-rauvomina B i drugih članova makrolinske/sarpaginske grupe alkaloida

Đurković, Filip T.; Ferjančić, Zorana; Bihelović, Filip

(Belgrade : Serbian Chemical Society, 2022) 

TY  - CONF
AU  - Đurković, Filip T.
AU  - Ferjančić, Zorana
AU  - Bihelović, Filip
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5934
AB  - Indole alkaloid (+)-rauvomine B1
 contains cyclopropane ring incorporated in the 
unprecedented 6/5/6/6/3/5 hexacyclic structure ornate with six stereocenters, making this 
compound a challenging synthetic task. 
Our strategy for (+)-rauvomine B total synthesis proceeds via a key tetracyclic 
intermediate, which could be efficiently prepared from commercially available N-Boc-(S)-
tryptophan in 4 steps: 1) homologization to homotryptophan 2) aldol reaction 3) Pictet Spengler reaction 4) elimination. This efficient route also enabled several other members 
of macroline/sarpagine indole alkaloids to be synthesized from this common intermediate,
via unified strategy.
PB  - Belgrade : Serbian Chemical Society
C3  - 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine
T1  - Sintetičke studije za dobijanje (+)-rauvomina B i drugih članova  makrolinske/sarpaginske grupe alkaloida
T1  - Synthetic studies towards (+)-rauvomine B and other  macroline/sarpagine alkaloids
IS  - 58
SP  - 134
EP  - 134
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5934
ER  - 
@conference{
author = "Đurković, Filip T. and Ferjančić, Zorana and Bihelović, Filip",
year = "2022",
abstract = "Indole alkaloid (+)-rauvomine B1
 contains cyclopropane ring incorporated in the 
unprecedented 6/5/6/6/3/5 hexacyclic structure ornate with six stereocenters, making this 
compound a challenging synthetic task. 
Our strategy for (+)-rauvomine B total synthesis proceeds via a key tetracyclic 
intermediate, which could be efficiently prepared from commercially available N-Boc-(S)-
tryptophan in 4 steps: 1) homologization to homotryptophan 2) aldol reaction 3) Pictet Spengler reaction 4) elimination. This efficient route also enabled several other members 
of macroline/sarpagine indole alkaloids to be synthesized from this common intermediate,
via unified strategy.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine",
title = "Sintetičke studije za dobijanje (+)-rauvomina B i drugih članova  makrolinske/sarpaginske grupe alkaloida, Synthetic studies towards (+)-rauvomine B and other  macroline/sarpagine alkaloids",
number = "58",
pages = "134-134",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5934"
}
Đurković, F. T., Ferjančić, Z.,& Bihelović, F.. (2022). Sintetičke studije za dobijanje (+)-rauvomina B i drugih članova  makrolinske/sarpaginske grupe alkaloida. in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine
Belgrade : Serbian Chemical Society.(58), 134-134.
https://hdl.handle.net/21.15107/rcub_cherry_5934
Đurković FT, Ferjančić Z, Bihelović F. Sintetičke studije za dobijanje (+)-rauvomina B i drugih članova  makrolinske/sarpaginske grupe alkaloida. in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine. 2022;(58):134-134.
https://hdl.handle.net/21.15107/rcub_cherry_5934 .
Đurković, Filip T., Ferjančić, Zorana, Bihelović, Filip, "Sintetičke studije za dobijanje (+)-rauvomina B i drugih članova  makrolinske/sarpaginske grupe alkaloida" in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine, no. 58 (2022):134-134,
https://hdl.handle.net/21.15107/rcub_cherry_5934 .

Izolovanje, aktivnost i bioinformatička analiza ficina 1c

Đurković, Filip T.

(2020) 

TY  - THES
AU  - Đurković, Filip T.
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4114
AB  - U okviru ovog završnog rada predstavljeno je izolovanje i karakterizacija bazne
izoforme ficina, proteaze pronaĎene u lateksu koji je sakupljen krajem juna iz ploda drveta smokve (Ficus carica) koja raste u Baru, u Crnoj Gori. Izolovanje je izvedeno primenom jonoizmenjivačke hromatografije, a čistoća dobijene frakcije je proverena reverzno-faznom hromatografijom i SDS-PAGE elektroforezom. U saradnji sa profesorom J. Lahom1 tripsinskim mapiranjem je na osnovu transkriptomske sekvence utvrđeno da je izolovana izofoma ficin 1c. Primenom infracrvene spektroskopije sa Furijeovom transformacijom (FTIR) određen je sadržaj sekundarnih struktura u ovoj izoformi. Modelovanje 3D strukture ficina 1c izvedeno je primenom Phyre2 servera, a slaganje sekvenci sa ostalim izoformama ficina izvedeno je uz pomoć MAFFT programa.
Na osnovu dobijenih rezultata modelovanja 3D strukture i sličnosti sekundarnih
struktura, zaključeno je da je obrazac uvijanja ficina 1c gotovo identičan uvijanju drugih izoformi ficina izolovanih iz različitih sorti smokve, kao i drugih biljnih cistein proteaza, kao što je papain. U prilog ovom zaključku govore i rezultati upoređivanja sekvenci, koji pokazuju evolutivnu konzerviranost cisteinskih ostataka, koji zbog katalitičke aktivnosti i izgradnje disulfidnih mostova imaju presudan uticaj na trodimenzionalnu strukturu proteina.
T1  - Izolovanje, aktivnost i bioinformatička analiza ficina 1c
SP  - 1
EP  - 36
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4114
ER  - 
@mastersthesis{
author = "Đurković, Filip T.",
year = "2020",
abstract = "U okviru ovog završnog rada predstavljeno je izolovanje i karakterizacija bazne
izoforme ficina, proteaze pronaĎene u lateksu koji je sakupljen krajem juna iz ploda drveta smokve (Ficus carica) koja raste u Baru, u Crnoj Gori. Izolovanje je izvedeno primenom jonoizmenjivačke hromatografije, a čistoća dobijene frakcije je proverena reverzno-faznom hromatografijom i SDS-PAGE elektroforezom. U saradnji sa profesorom J. Lahom1 tripsinskim mapiranjem je na osnovu transkriptomske sekvence utvrđeno da je izolovana izofoma ficin 1c. Primenom infracrvene spektroskopije sa Furijeovom transformacijom (FTIR) određen je sadržaj sekundarnih struktura u ovoj izoformi. Modelovanje 3D strukture ficina 1c izvedeno je primenom Phyre2 servera, a slaganje sekvenci sa ostalim izoformama ficina izvedeno je uz pomoć MAFFT programa.
Na osnovu dobijenih rezultata modelovanja 3D strukture i sličnosti sekundarnih
struktura, zaključeno je da je obrazac uvijanja ficina 1c gotovo identičan uvijanju drugih izoformi ficina izolovanih iz različitih sorti smokve, kao i drugih biljnih cistein proteaza, kao što je papain. U prilog ovom zaključku govore i rezultati upoređivanja sekvenci, koji pokazuju evolutivnu konzerviranost cisteinskih ostataka, koji zbog katalitičke aktivnosti i izgradnje disulfidnih mostova imaju presudan uticaj na trodimenzionalnu strukturu proteina.",
title = "Izolovanje, aktivnost i bioinformatička analiza ficina 1c",
pages = "1-36",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4114"
}
Đurković, F. T.. (2020). Izolovanje, aktivnost i bioinformatička analiza ficina 1c. , 1-36.
https://hdl.handle.net/21.15107/rcub_cherry_4114
Đurković FT. Izolovanje, aktivnost i bioinformatička analiza ficina 1c. 2020;:1-36.
https://hdl.handle.net/21.15107/rcub_cherry_4114 .
Đurković, Filip T., "Izolovanje, aktivnost i bioinformatička analiza ficina 1c" (2020):1-36,
https://hdl.handle.net/21.15107/rcub_cherry_4114 .

Isolation, identification, and stability of Ficin 1c isoform from fig latex

Milošević, Jelica; Vrhovac, Lidija; Đurković, Filip T.; Janković, Brankica; Malkov, Saša; Lah, Jurij; Polović, Natalija

(Royal Society of Chemistry, 2020) 

TY  - JOUR
AU  - Milošević, Jelica
AU  - Vrhovac, Lidija
AU  - Đurković, Filip T.
AU  - Janković, Brankica
AU  - Malkov, Saša
AU  - Lah, Jurij
AU  - Polović, Natalija
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4265
AB  - Latex of common fig (Ficus carica) is a rich protein source with a high level of proteolytic activity contributing to its defensive role. The divergent group of cysteine proteases known as ficin (EC 3.4.22.3) represents the majority of latex protein content and shows activity towards fig parasites. Both classical and novel biochemical techniques suggest the intricate pattern of ficin expression and activity profiles. Even though structurally related, different ficin isoforms show some differences in pI values enabling their separation using ion-exchangers. A single alkaline isoform was purified and identified based on the available transcriptomic data as Ficin 1c. This isoform shows both general proteolytic and gelatinolytic activity suggesting a biological role in the degradation of a broad range of natural substrates. The insight into the Ficin 1c structure also provided some functional clues. The secondary structure content and the overall fold are similar to related proteases of the same and other plant sources resulting in similar unfolding routes. Stability assessment of Ficin 1c in comparison to ficin isoform mixture showed that isoform diversity might lead to increased protease stability.
PB  - Royal Society of Chemistry
T2  - New Journal of Chemistry
T1  - Isolation, identification, and stability of Ficin 1c isoform from fig latex
VL  - 44
IS  - 36
SP  - 15716
EP  - 15723
DO  - 10.1039/D0NJ02938F
ER  - 
@article{
author = "Milošević, Jelica and Vrhovac, Lidija and Đurković, Filip T. and Janković, Brankica and Malkov, Saša and Lah, Jurij and Polović, Natalija",
year = "2020",
abstract = "Latex of common fig (Ficus carica) is a rich protein source with a high level of proteolytic activity contributing to its defensive role. The divergent group of cysteine proteases known as ficin (EC 3.4.22.3) represents the majority of latex protein content and shows activity towards fig parasites. Both classical and novel biochemical techniques suggest the intricate pattern of ficin expression and activity profiles. Even though structurally related, different ficin isoforms show some differences in pI values enabling their separation using ion-exchangers. A single alkaline isoform was purified and identified based on the available transcriptomic data as Ficin 1c. This isoform shows both general proteolytic and gelatinolytic activity suggesting a biological role in the degradation of a broad range of natural substrates. The insight into the Ficin 1c structure also provided some functional clues. The secondary structure content and the overall fold are similar to related proteases of the same and other plant sources resulting in similar unfolding routes. Stability assessment of Ficin 1c in comparison to ficin isoform mixture showed that isoform diversity might lead to increased protease stability.",
publisher = "Royal Society of Chemistry",
journal = "New Journal of Chemistry",
title = "Isolation, identification, and stability of Ficin 1c isoform from fig latex",
volume = "44",
number = "36",
pages = "15716-15723",
doi = "10.1039/D0NJ02938F"
}
Milošević, J., Vrhovac, L., Đurković, F. T., Janković, B., Malkov, S., Lah, J.,& Polović, N.. (2020). Isolation, identification, and stability of Ficin 1c isoform from fig latex. in New Journal of Chemistry
Royal Society of Chemistry., 44(36), 15716-15723.
https://doi.org/10.1039/D0NJ02938F
Milošević J, Vrhovac L, Đurković FT, Janković B, Malkov S, Lah J, Polović N. Isolation, identification, and stability of Ficin 1c isoform from fig latex. in New Journal of Chemistry. 2020;44(36):15716-15723.
doi:10.1039/D0NJ02938F .
Milošević, Jelica, Vrhovac, Lidija, Đurković, Filip T., Janković, Brankica, Malkov, Saša, Lah, Jurij, Polović, Natalija, "Isolation, identification, and stability of Ficin 1c isoform from fig latex" in New Journal of Chemistry, 44, no. 36 (2020):15716-15723,
https://doi.org/10.1039/D0NJ02938F . .
11
2
8
10

Isolation, identification, and stability of Ficin 1c isoform from fig latex

Milošević, Jelica; Vrhovac, Lidija; Đurković, Filip T.; Janković, Brankica; Malkov, Saša; Lah, Jurij; Polović, Natalija

(Royal Society of Chemistry, 2020) 

TY  - JOUR
AU  - Milošević, Jelica
AU  - Vrhovac, Lidija
AU  - Đurković, Filip T.
AU  - Janković, Brankica
AU  - Malkov, Saša
AU  - Lah, Jurij
AU  - Polović, Natalija
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4264
AB  - Latex of common fig (Ficus carica) is a rich protein source with a high level of proteolytic activity contributing to its defensive role. The divergent group of cysteine proteases known as ficin (EC 3.4.22.3) represents the majority of latex protein content and shows activity towards fig parasites. Both classical and novel biochemical techniques suggest the intricate pattern of ficin expression and activity profiles. Even though structurally related, different ficin isoforms show some differences in pI values enabling their separation using ion-exchangers. A single alkaline isoform was purified and identified based on the available transcriptomic data as Ficin 1c. This isoform shows both general proteolytic and gelatinolytic activity suggesting a biological role in the degradation of a broad range of natural substrates. The insight into the Ficin 1c structure also provided some functional clues. The secondary structure content and the overall fold are similar to related proteases of the same and other plant sources resulting in similar unfolding routes. Stability assessment of Ficin 1c in comparison to ficin isoform mixture showed that isoform diversity might lead to increased protease stability.
PB  - Royal Society of Chemistry
T2  - New Journal of Chemistry
T1  - Isolation, identification, and stability of Ficin 1c isoform from fig latex
VL  - 44
IS  - 36
SP  - 15716
EP  - 15723
DO  - 10.1039/D0NJ02938F
ER  - 
@article{
author = "Milošević, Jelica and Vrhovac, Lidija and Đurković, Filip T. and Janković, Brankica and Malkov, Saša and Lah, Jurij and Polović, Natalija",
year = "2020",
abstract = "Latex of common fig (Ficus carica) is a rich protein source with a high level of proteolytic activity contributing to its defensive role. The divergent group of cysteine proteases known as ficin (EC 3.4.22.3) represents the majority of latex protein content and shows activity towards fig parasites. Both classical and novel biochemical techniques suggest the intricate pattern of ficin expression and activity profiles. Even though structurally related, different ficin isoforms show some differences in pI values enabling their separation using ion-exchangers. A single alkaline isoform was purified and identified based on the available transcriptomic data as Ficin 1c. This isoform shows both general proteolytic and gelatinolytic activity suggesting a biological role in the degradation of a broad range of natural substrates. The insight into the Ficin 1c structure also provided some functional clues. The secondary structure content and the overall fold are similar to related proteases of the same and other plant sources resulting in similar unfolding routes. Stability assessment of Ficin 1c in comparison to ficin isoform mixture showed that isoform diversity might lead to increased protease stability.",
publisher = "Royal Society of Chemistry",
journal = "New Journal of Chemistry",
title = "Isolation, identification, and stability of Ficin 1c isoform from fig latex",
volume = "44",
number = "36",
pages = "15716-15723",
doi = "10.1039/D0NJ02938F"
}
Milošević, J., Vrhovac, L., Đurković, F. T., Janković, B., Malkov, S., Lah, J.,& Polović, N.. (2020). Isolation, identification, and stability of Ficin 1c isoform from fig latex. in New Journal of Chemistry
Royal Society of Chemistry., 44(36), 15716-15723.
https://doi.org/10.1039/D0NJ02938F
Milošević J, Vrhovac L, Đurković FT, Janković B, Malkov S, Lah J, Polović N. Isolation, identification, and stability of Ficin 1c isoform from fig latex. in New Journal of Chemistry. 2020;44(36):15716-15723.
doi:10.1039/D0NJ02938F .
Milošević, Jelica, Vrhovac, Lidija, Đurković, Filip T., Janković, Brankica, Malkov, Saša, Lah, Jurij, Polović, Natalija, "Isolation, identification, and stability of Ficin 1c isoform from fig latex" in New Journal of Chemistry, 44, no. 36 (2020):15716-15723,
https://doi.org/10.1039/D0NJ02938F . .
11
2
8
10