Research Article
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Year 2025, Volume: 9 Issue: 1, 13 - 24, 24.06.2025
https://doi.org/10.32571/ijct.1648820

Abstract

Project Number

FAB-2022-10562

References

  • 1. Hesse M. Alkaloids: Nature’s Curse or Blessing; Wiley-VCH: Zürich, Switzerland, 2002; pp. 14–27.
  • 2. Laine, A.E.; Lood, C.; Koskinen, A.M. Molecules. 2014, 19(2),1544-1567.
  • 3. Saxton, J.E. Monoterpenoid Indole Alkaloids: Supplement to Part. 4.; Wiley: Chichester, UK,1994;162–176, 719–725.
  • 4. Davis, R.A.; Duffy, S.; Avery, V.M.; Camp, D.; Hooper, J.N. Tetrahedron Lett. 2010, 51(4),583-585.
  • 5. Chan, S.T.; Pearce, A.N.; Page, M.J.; Kaiser, M.; Copp, B.R. J Nat Prod. 2011, 74(9),1972-1979.
  • 6. Gellis, A.; Dumètre, A.; Hutter, S.; Ollivier, E.; Vanelle, P.; Azas, N. Biomed Pharmacother. 2012, 66(5),339-347.
  • 7. Ashok, P.; Ganguly, S.; Murugesan, S. Drug Discov. Today. 2014, 19(11),1781-1791.
  • 8. Azas, N.; Laurencin, N.; Delmas, F.; Di Giorgio, C.; Gasquet, M.; Laget, M.; et al. Parasitol Res. 2002, 88, 165–71.
  • 9. Fiot, J.; Sanon, S.; Azas, N.; Mahiou, V.; Jansen, O.; Angenot, L.; et al. J Ethnopharmacol. 2006, 106, 173–8.
  • 10. Daugan, A.; Grondin, P.; Ruault, C.; le Monnier, D.G.; Coste, H.; Kirilovsky, J.; Hyafil, F.; Labaudiniere, R. J. Med. Chem. 2003, 46, 4525–4532.
  • 11. Davis, R.A.; Duffy, S.; Avery, V.M.; Camp, D.; Hooper, J.N.A. Tetrahedron Lett. 2010, 51, 583–585.
  • 12. Chan, S.T.S.; Pearce, A.N.; Page, M.J.; Kaiser, M.; Copp, B.R. J. Nat. Prod. 2011, 74, 1972–1979.
  • 13. Gellis, A.; Dumètre, A.; Lanzada, G.; Hutter, S.; Ollivier, E.; Vanelle, P.; Azas, N. Biomed. Pharmacother. 2012, 66, 339–347.
  • 14. Van Maarseveen, J.H.; Hermkens, P.H.H.; de Clercq, E.; Balzarini, J.; Scheeren, H.W.; Kruse, C.G. J. Med. Chem. 1992, 35, 3223–3230.
  • 15. Miller, J.F.; Turner, E.M.; Sherrill, R.G.; Gudmundsson, K.; Spaltenstein, A.; Sethna, P.; Brown, K.W.; Harvey, R.; Romines, K.R.; Golden, P. Bioorg. Med. Chem. Lett. 2010, 20, 256–259.
  • 16. Shen, Y.; Chang, Y.; Lin, C.; Liaw, C.; Kuo, Y.H.; Tu, L.; Yeh, S.F.; Chern, J. Mar. Drugs. 2011, 9, 256–277.
  • 17. Skouta, R.; Hayano, M.; Shimada, K.; Stockwell, B.R. Bioorg. Med. Chem. Lett. 2012, 22, 5707–5713.
  • 18. Hotha, S.; Yarrow, J.C.; Yang, J.G.; Garrett, S.; Renduchintala, K.V.; Mayer, T.U.; Kapoor, T.M. Angew. Chem. 2003, 115, 2481–2484.
  • 19. Serafini, P.; Meckel, K.; Kelso, M.; Noonan, K.; Califano, J.; Koch, W.; Dolcetti, L.; Bronte, V.; Borrello, I. J. Exp. Med. 2006, 203, 2691–2702.
  • 20. Wamelink, M.; Struys, E.; Jakobs, C. JIMD: Official Journal of the Society for the Study of Inborn Errors of Metabolism. 2008, 31(6), 703-717.
  • 21. del Campo, J.S.M.; Patiño, R. Thermochim. Acta. 2011, 517(1-2), 40-44. 22. Kaplan, M.; Hammerman. Paper presented at the Seminars in Fetal and Neonatal Medicine. 2010.
  • 23. Ulusu, N.N.; Kus, M.S.; Acan, N.L.; Tezcan, E.F. IJBCB. 1999, 31(7), 787-796.
  • 24. Winiarska, K.; Węgrzynowicz, M.; Jagielski, A.K.; Bryła, J. Metabolism, 2003, 52(6), 739-746.
  • 25. Riganti, C.; Gazzano, E.; Polimeni, M.; Aldieri, E.; Ghigo, D. Free Radic Biol Med. 2012, 53(3), 421-436.
  • 26. Tsouko, E.; Khan, A.S.; White, M.A.; Han, J.J.; Shi, Y.; Merchant, F.A.; ... & Frigo, D.E. Oncogenesis. 2014, 3(5), e103-e103.
  • 27. Furukawa, T.; Tabata, S.; Minami, K.; Yamamoto, M.; Kawahara, K.; Tanimoto, A. BBA-Gen Subjects. 2023, 1867(3), 130301.
  • 28. Atamna, H.; Pascarmona, G.; Ginsburg, H. Mol Biochem Parasit, 1994, 67(1), 79-89.
  • 29. López, C.; Saravia, C.; Gomez, A.; Hoebeke, J.; Patarroyo, M.A. Gene. 2010, 467(1-2), 1-12.
  • 30. Wolach, B.; Ashkenazi, M.; Grossmann, R.; Gavrieli, R.; Friedman, Z.; Bashan, N. Pediatr Res. 2004, 55, 807–813.
  • 31. Elyassi, A.R.; Rowshan, H.H. Anesth Prog. 2009, 56, 86–91.
  • 32. Wu, Y.H.; Tseng, C.P.; Cheng, M.L.; Ho, H.Y.; Shih, S.R.; Chiu, D.T. J Infect Dis. 2008, 197, 812–816.
  • 33. Ninfali, P.; Orsenigo, I.; Baronciani, L.; Rapa, S. Prep Biochem. 1990, 20(3-4), 297-309.
  • 34. Adem, S.; Ciftci, M. Protein Expres Purif. 2012, 81(1), 1-4.
  • 35. Akkemik, E.; Budak, H.; Ciftci, M. J Enzym Inhıb Med Ch. 2010, 25(6), 871-875.
  • 36. Morelli, A.; Benatti, U.; Gaetani, G.; De Flora, A. Proceedings of the National Academy of Sciences, 1978, 75(4), 1979-1983.
  • 37. Beutler, E. Red cell metabolism. A manual of biochemical methods, 1975, 11-12.
  • 38. Akkemik, E.; Budak, H.; Ciftci, M. J Enzym Inhıb Med Ch. 2010, 25(4), 476-479.
  • 39. Mancuso, G.; Midiri, A.; Gerace, E.; Biondo, C. Pathogens 2021, 10(10), 1310.
  • 40. Kowalska-Krochmal, B.; Dudek-Wicher, R. Pathogens. 2021, 10(2), 165.
  • 41. Wiegand, I.; Hilpert, K.; Hancock, R.E.W. Nat. Protoc3. 2008, 163–175.
  • 42. Denev, P.; Kratchanova, M.; Ciz, M.; Lojek, A.; Vasicek, O.; Nedelcheva, P.; … Vojtek, L. Food Chem. 2014, 157, 37-44.
  • 43. CLSI, Clinical and Laboratory Standards Institute, CLSI Document no. M07, 2018. 11th ed., Wayne, Clinical and Laboratory Standards Institute.
  • 44. National Committee for Clinical Laboratory Standard, 1999.
  • 45. Trott, O.; Olson, A.J. J Comput Chem. 2010, 31(2), 455-461.
  • 46. Hwang, S.; Mruk, K.; Rahighi, S.; Raub, A.G.; Chen, C.H.; Dorn, L.E.; et al. Nat Commun. 2018, 9(1), 1-12.
  • 47. Mouilleron, S.; Badet-Denisot, M.A.; Golinelli-Pimpaneau, B. J Mol Biol. 2008, 377(4), 1174-1185.
  • 48. Caprari, S.; Brandi, V.; Pasquadibisceglie, A.; Polticelli, F. J. Biomol. Struct. Dyn. 2020, 38(15), 4508-4520.
  • 49. Stogios, P.J.; Kuhn, M.L.; Evdokimova, E.; Law, M.; Courvalin, P.; Savchenko, A. ACS Infect. Dis. 2017, 3(2), 132-143.
  • 50 Lipinski, C.A.; Lombardo, F.; Dominy, B.W.; Feeney, P.J. Adv Drug Delıver Rev. 1997, 23(1-3), 3-25.
  • 51. T. Martin. User’s guide for TEST (version4.2) (Toxicity Estimation Software Tool): a program to estimate toxicity from molecular structure. EPA/600/R-16/058.
  • 52. Ramírez-Nava, E.J.; Hernández-Ochoa, B.; Navarrete-Vázquez, G.; Arreguín-Espinosa, R.; Ortega-Cuellar, D.; González-Valdez, A.; ... & Gómez-Manzo, S. BBA-Gen Subjects. 2021, 1865(3), 129828.
  • 53. Konaté, K.; Mavoungou, J.F.; Lepengué, A.N.; Aworet-Samseny, R.R.; Hilou, A.; Souza, A.; ... M’Batchi, B. Ann Clin Microb Anti, 2012, 11, 1-12.
  • 54. Venkateswarulu, T.C.; Srirama, K.; Mikkili, I.; Dulla, J.B.; Alugunulla, V.N.; Sweety, D.; Karlapudi, A.P. Karbala Int. J. Mod. Sci. 2019, 5(4), 8.
  • 55. Berche, P.; Gaillard, J.L.; Simonet, M. Nosocomial Infections Caused by Bacteria and Their Prevention in Bacteriology. Ed Flammarion Medicine Sciences 1988, 64–71.
  • 56. Khan, M.A.; Göpel, Y.; Milewski, S.; Görke, B. Front Microbiol, 2016, 7, 208452.
  • 57. Begley, D.J.; Brightman, M.W. Basel: Birkhäuser Basel 2003, 39–78.
  • 58. Daina, A.; Zoete, V. ChemMedChem. 2016, 11(11), 1117-1121.
  • 59. Daina, A.; Michielin, O.; Zoete, V. Epub ahead of print. 2017.
  • 60. Selick, H.E.; Beresford, A.P.; Tarbit, M.H. Drug Discov. Today. 2002, 7, 109–116.
  • 61. Yenigun, S.; Basar, Y.; Gül, F.; Ipek, Y.; Gok, M.; Behcet, L.; ... & Demirtas, I. ChemistrySelect, 2024, 9(18), e202400919.
  • 62. Yenigun, S.; Basar, Y.; Ipek, Y.; Behcet, L.; Demirtas, I.; Ozen, T. J. Biol. Act. Prod. Nat, 2024, 14(3), 286-315.
  • 63. Yenigun, S.; Basar, Y.; Ipek, Y.; Gok, M.; Behcet, L.; Ozen, T.; Demirtas, I. Process Biochemistry, 2024, 143, 234-247.
  • 64. Chi, G. F.; Khan, S.; Başar, Y.; Kuete, J. R.; Matieta, V. Y.; Kuete, J. B.; ... & Shaheen, F. S. Afr. J. Bot., 2025, 180, 96-106.
  • 65. Yenigun, S.; Basar, Y.; Gul, F.; Marah, S.; Behcet, L.; Demirtas, I.; Ozen, T. ChemistrySelect, 2024, 9(18), e202400583.
  • 66. Başar, Y.; Yenigün, S.; Gül, F.; Ozen, T.; Demirtas, İ.; Alma, M. H.; Temel, S. IJCT, 2024, 8(1), 62-71.
  • 67. Burden, N.; Creton, S.; Weltje, L.; et al. Regul. Toxicol. Pharmacol., 2014, 70: 442–445.
  • 68. Griffiths, A.J; Miller, J.H; Suzuki, D.T; et al. In: Freeman WH (ed) An Introduction to Genetic Analysis. 2000.

Exploring the Antibacterial and Enzyme Inhibitory Potential of Selected β-Carboline Derivatives: In Vitro and In Silico Insights

Year 2025, Volume: 9 Issue: 1, 13 - 24, 24.06.2025
https://doi.org/10.32571/ijct.1648820

Abstract

β-Carboline derivatives have a wide range of biological effects such as antiviral, antitumor and antimalarial and are therefore important compounds for drug development. In this study, the effect of some β-carboline derivatives on glucose 6-phosphate dehydrogenase (G6PD), 6-phosphogluconate dehydrogenase (6PGD), and antibacterial activities were investigated. For this purpose, affinity chromatography was used to separate G6PD and 6PGD from human erythrocytes with a specific activity of 1.96 EU/ml protein and 4.569 EU/ml protein, respectively and then in vitro effects of compounds were assayed. It was found that only 1-Isopropyl-2,3,4,9-tetrahydro-1H-beta-carboline, among the selected β-Carboline derivatives, inhibited G6PD with an IC50 value of 31.2 µM. It was determined that other derivatives did not have any effect on G6PD and 6PGD activities. Besides antibacterial effects of compounds were examined and compounds were found effective against Escherichia coli, Klebsiella pneumoniae, and Acinetobacter haemolyticus. Molecular docking study of isopropyl-2,3,4,9-tetrahydro-1H-beta-carboline molecule to the hG6PD (6E08) receptor was performed and the estimated binding energy was determined as -6.97 kcal/mol. According to the results of antibacterial studies, compounds were docked into some specific proteins of microorganisms as well and possible interactions between receptors and derivatives were discussed.

Supporting Institution

Atatürk University-Scientific Research Projects

Project Number

FAB-2022-10562

References

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  • 2. Laine, A.E.; Lood, C.; Koskinen, A.M. Molecules. 2014, 19(2),1544-1567.
  • 3. Saxton, J.E. Monoterpenoid Indole Alkaloids: Supplement to Part. 4.; Wiley: Chichester, UK,1994;162–176, 719–725.
  • 4. Davis, R.A.; Duffy, S.; Avery, V.M.; Camp, D.; Hooper, J.N. Tetrahedron Lett. 2010, 51(4),583-585.
  • 5. Chan, S.T.; Pearce, A.N.; Page, M.J.; Kaiser, M.; Copp, B.R. J Nat Prod. 2011, 74(9),1972-1979.
  • 6. Gellis, A.; Dumètre, A.; Hutter, S.; Ollivier, E.; Vanelle, P.; Azas, N. Biomed Pharmacother. 2012, 66(5),339-347.
  • 7. Ashok, P.; Ganguly, S.; Murugesan, S. Drug Discov. Today. 2014, 19(11),1781-1791.
  • 8. Azas, N.; Laurencin, N.; Delmas, F.; Di Giorgio, C.; Gasquet, M.; Laget, M.; et al. Parasitol Res. 2002, 88, 165–71.
  • 9. Fiot, J.; Sanon, S.; Azas, N.; Mahiou, V.; Jansen, O.; Angenot, L.; et al. J Ethnopharmacol. 2006, 106, 173–8.
  • 10. Daugan, A.; Grondin, P.; Ruault, C.; le Monnier, D.G.; Coste, H.; Kirilovsky, J.; Hyafil, F.; Labaudiniere, R. J. Med. Chem. 2003, 46, 4525–4532.
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  • 18. Hotha, S.; Yarrow, J.C.; Yang, J.G.; Garrett, S.; Renduchintala, K.V.; Mayer, T.U.; Kapoor, T.M. Angew. Chem. 2003, 115, 2481–2484.
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  • 23. Ulusu, N.N.; Kus, M.S.; Acan, N.L.; Tezcan, E.F. IJBCB. 1999, 31(7), 787-796.
  • 24. Winiarska, K.; Węgrzynowicz, M.; Jagielski, A.K.; Bryła, J. Metabolism, 2003, 52(6), 739-746.
  • 25. Riganti, C.; Gazzano, E.; Polimeni, M.; Aldieri, E.; Ghigo, D. Free Radic Biol Med. 2012, 53(3), 421-436.
  • 26. Tsouko, E.; Khan, A.S.; White, M.A.; Han, J.J.; Shi, Y.; Merchant, F.A.; ... & Frigo, D.E. Oncogenesis. 2014, 3(5), e103-e103.
  • 27. Furukawa, T.; Tabata, S.; Minami, K.; Yamamoto, M.; Kawahara, K.; Tanimoto, A. BBA-Gen Subjects. 2023, 1867(3), 130301.
  • 28. Atamna, H.; Pascarmona, G.; Ginsburg, H. Mol Biochem Parasit, 1994, 67(1), 79-89.
  • 29. López, C.; Saravia, C.; Gomez, A.; Hoebeke, J.; Patarroyo, M.A. Gene. 2010, 467(1-2), 1-12.
  • 30. Wolach, B.; Ashkenazi, M.; Grossmann, R.; Gavrieli, R.; Friedman, Z.; Bashan, N. Pediatr Res. 2004, 55, 807–813.
  • 31. Elyassi, A.R.; Rowshan, H.H. Anesth Prog. 2009, 56, 86–91.
  • 32. Wu, Y.H.; Tseng, C.P.; Cheng, M.L.; Ho, H.Y.; Shih, S.R.; Chiu, D.T. J Infect Dis. 2008, 197, 812–816.
  • 33. Ninfali, P.; Orsenigo, I.; Baronciani, L.; Rapa, S. Prep Biochem. 1990, 20(3-4), 297-309.
  • 34. Adem, S.; Ciftci, M. Protein Expres Purif. 2012, 81(1), 1-4.
  • 35. Akkemik, E.; Budak, H.; Ciftci, M. J Enzym Inhıb Med Ch. 2010, 25(6), 871-875.
  • 36. Morelli, A.; Benatti, U.; Gaetani, G.; De Flora, A. Proceedings of the National Academy of Sciences, 1978, 75(4), 1979-1983.
  • 37. Beutler, E. Red cell metabolism. A manual of biochemical methods, 1975, 11-12.
  • 38. Akkemik, E.; Budak, H.; Ciftci, M. J Enzym Inhıb Med Ch. 2010, 25(4), 476-479.
  • 39. Mancuso, G.; Midiri, A.; Gerace, E.; Biondo, C. Pathogens 2021, 10(10), 1310.
  • 40. Kowalska-Krochmal, B.; Dudek-Wicher, R. Pathogens. 2021, 10(2), 165.
  • 41. Wiegand, I.; Hilpert, K.; Hancock, R.E.W. Nat. Protoc3. 2008, 163–175.
  • 42. Denev, P.; Kratchanova, M.; Ciz, M.; Lojek, A.; Vasicek, O.; Nedelcheva, P.; … Vojtek, L. Food Chem. 2014, 157, 37-44.
  • 43. CLSI, Clinical and Laboratory Standards Institute, CLSI Document no. M07, 2018. 11th ed., Wayne, Clinical and Laboratory Standards Institute.
  • 44. National Committee for Clinical Laboratory Standard, 1999.
  • 45. Trott, O.; Olson, A.J. J Comput Chem. 2010, 31(2), 455-461.
  • 46. Hwang, S.; Mruk, K.; Rahighi, S.; Raub, A.G.; Chen, C.H.; Dorn, L.E.; et al. Nat Commun. 2018, 9(1), 1-12.
  • 47. Mouilleron, S.; Badet-Denisot, M.A.; Golinelli-Pimpaneau, B. J Mol Biol. 2008, 377(4), 1174-1185.
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  • 52. Ramírez-Nava, E.J.; Hernández-Ochoa, B.; Navarrete-Vázquez, G.; Arreguín-Espinosa, R.; Ortega-Cuellar, D.; González-Valdez, A.; ... & Gómez-Manzo, S. BBA-Gen Subjects. 2021, 1865(3), 129828.
  • 53. Konaté, K.; Mavoungou, J.F.; Lepengué, A.N.; Aworet-Samseny, R.R.; Hilou, A.; Souza, A.; ... M’Batchi, B. Ann Clin Microb Anti, 2012, 11, 1-12.
  • 54. Venkateswarulu, T.C.; Srirama, K.; Mikkili, I.; Dulla, J.B.; Alugunulla, V.N.; Sweety, D.; Karlapudi, A.P. Karbala Int. J. Mod. Sci. 2019, 5(4), 8.
  • 55. Berche, P.; Gaillard, J.L.; Simonet, M. Nosocomial Infections Caused by Bacteria and Their Prevention in Bacteriology. Ed Flammarion Medicine Sciences 1988, 64–71.
  • 56. Khan, M.A.; Göpel, Y.; Milewski, S.; Görke, B. Front Microbiol, 2016, 7, 208452.
  • 57. Begley, D.J.; Brightman, M.W. Basel: Birkhäuser Basel 2003, 39–78.
  • 58. Daina, A.; Zoete, V. ChemMedChem. 2016, 11(11), 1117-1121.
  • 59. Daina, A.; Michielin, O.; Zoete, V. Epub ahead of print. 2017.
  • 60. Selick, H.E.; Beresford, A.P.; Tarbit, M.H. Drug Discov. Today. 2002, 7, 109–116.
  • 61. Yenigun, S.; Basar, Y.; Gül, F.; Ipek, Y.; Gok, M.; Behcet, L.; ... & Demirtas, I. ChemistrySelect, 2024, 9(18), e202400919.
  • 62. Yenigun, S.; Basar, Y.; Ipek, Y.; Behcet, L.; Demirtas, I.; Ozen, T. J. Biol. Act. Prod. Nat, 2024, 14(3), 286-315.
  • 63. Yenigun, S.; Basar, Y.; Ipek, Y.; Gok, M.; Behcet, L.; Ozen, T.; Demirtas, I. Process Biochemistry, 2024, 143, 234-247.
  • 64. Chi, G. F.; Khan, S.; Başar, Y.; Kuete, J. R.; Matieta, V. Y.; Kuete, J. B.; ... & Shaheen, F. S. Afr. J. Bot., 2025, 180, 96-106.
  • 65. Yenigun, S.; Basar, Y.; Gul, F.; Marah, S.; Behcet, L.; Demirtas, I.; Ozen, T. ChemistrySelect, 2024, 9(18), e202400583.
  • 66. Başar, Y.; Yenigün, S.; Gül, F.; Ozen, T.; Demirtas, İ.; Alma, M. H.; Temel, S. IJCT, 2024, 8(1), 62-71.
  • 67. Burden, N.; Creton, S.; Weltje, L.; et al. Regul. Toxicol. Pharmacol., 2014, 70: 442–445.
  • 68. Griffiths, A.J; Miller, J.H; Suzuki, D.T; et al. In: Freeman WH (ed) An Introduction to Genetic Analysis. 2000.
There are 67 citations in total.

Details

Primary Language English
Subjects Structural Biology
Journal Section Research Articles
Authors

Behiye Taşer 0000-0002-7936-432X

Pınar Güller 0000-0001-8482-7889

Hakan Özkan 0000-0003-0048-8248

Project Number FAB-2022-10562
Early Pub Date June 2, 2025
Publication Date June 24, 2025
Submission Date February 28, 2025
Acceptance Date May 16, 2025
Published in Issue Year 2025 Volume: 9 Issue: 1

Cite

APA Taşer, B., Güller, P., & Özkan, H. (2025). Exploring the Antibacterial and Enzyme Inhibitory Potential of Selected β-Carboline Derivatives: In Vitro and In Silico Insights. International Journal of Chemistry and Technology, 9(1), 13-24. https://doi.org/10.32571/ijct.1648820
AMA Taşer B, Güller P, Özkan H. Exploring the Antibacterial and Enzyme Inhibitory Potential of Selected β-Carboline Derivatives: In Vitro and In Silico Insights. Int. J. Chem. Technol. June 2025;9(1):13-24. doi:10.32571/ijct.1648820
Chicago Taşer, Behiye, Pınar Güller, and Hakan Özkan. “Exploring the Antibacterial and Enzyme Inhibitory Potential of Selected β-Carboline Derivatives: In Vitro and In Silico Insights”. International Journal of Chemistry and Technology 9, no. 1 (June 2025): 13-24. https://doi.org/10.32571/ijct.1648820.
EndNote Taşer B, Güller P, Özkan H (June 1, 2025) Exploring the Antibacterial and Enzyme Inhibitory Potential of Selected β-Carboline Derivatives: In Vitro and In Silico Insights. International Journal of Chemistry and Technology 9 1 13–24.
IEEE B. Taşer, P. Güller, and H. Özkan, “Exploring the Antibacterial and Enzyme Inhibitory Potential of Selected β-Carboline Derivatives: In Vitro and In Silico Insights”, Int. J. Chem. Technol., vol. 9, no. 1, pp. 13–24, 2025, doi: 10.32571/ijct.1648820.
ISNAD Taşer, Behiye et al. “Exploring the Antibacterial and Enzyme Inhibitory Potential of Selected β-Carboline Derivatives: In Vitro and In Silico Insights”. International Journal of Chemistry and Technology 9/1 (June2025), 13-24. https://doi.org/10.32571/ijct.1648820.
JAMA Taşer B, Güller P, Özkan H. Exploring the Antibacterial and Enzyme Inhibitory Potential of Selected β-Carboline Derivatives: In Vitro and In Silico Insights. Int. J. Chem. Technol. 2025;9:13–24.
MLA Taşer, Behiye et al. “Exploring the Antibacterial and Enzyme Inhibitory Potential of Selected β-Carboline Derivatives: In Vitro and In Silico Insights”. International Journal of Chemistry and Technology, vol. 9, no. 1, 2025, pp. 13-24, doi:10.32571/ijct.1648820.
Vancouver Taşer B, Güller P, Özkan H. Exploring the Antibacterial and Enzyme Inhibitory Potential of Selected β-Carboline Derivatives: In Vitro and In Silico Insights. Int. J. Chem. Technol. 2025;9(1):13-24.