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Synthesis and Biological Evaluation of Novel Dihydro [2,3D] Pyridine Substituted Enaminosulfonamide Compounds as Potent Human Erythrocyte Carbonic Anhydrase II (hCAII)

Year 2021, Volume: 25 Issue: 1, 200 - 211, 01.02.2021
https://doi.org/10.16984/saufenbilder.688414

Abstract

Dihydro [2,3D] pyridine substituted enaminosulfonamide compounds have been synthesized and their effects on carbonic anhydrase II (hCAII) have been evaluated. Pyrido [2,3 d] pyrimidines were synthesized from barbituric acid derivatives, malonanitrile, aldehyde derivatives in basic condition and then hydrolyzed with hydrochloric acid. The targeted compounds were syn-thesized from amino sulfanilamide, dihydro [2,3D] pyridine compounds, and triethylorthoformate. 1H NMR, 13C NMR, FT-IR and elemental analysis were used for the structural analysis of the compounds. The half maximal inhibitory concentration (IC50) values of the compounds were determined to be between 27.03 and 104.39 μM for hCA II and 19.85-76.64 μM for Ki.

Supporting Institution

Sakarya University Scientific Research Projects Coordination Unit

Project Number

2012-02-04-033/2016-50-02-002.

Thanks

Duzce University Scientific and Technological Research Laboratory

References

  • [1] M. Conrad and M. Guthzeit, “Ueber Barbitursäurederivate,” Berichte der Dtsch. Chem. Gesellschaft, vol. 15, no. 2, pp. 2844–2850, Jul. 1882.
  • [2] J. T. Mason, J. W. Baker, and F. Pilcher, “Sodium amytal in surgical management,” Am. J. Surg., vol. 9, no. 1, pp. 9–15, Jul. 1930.
  • [3] N. Moussier, L. Bruche, F. Viani, and M. Zanda, “Fluorinated Barbituric Acid Derivatives: Synthesis and Bio-activity,” Curr. Org. Chem., vol. 7, no. 11, pp. 1071–1080, Jul. 2003.
  • [4] A. Barakat et al., “New Diethyl Ammonium Salt of Thiobarbituric Acid Derivative: Synthesis, Molecular Structure Investigations and Docking Studies,” Molecules, vol. 20, no. 11, pp. 20642–20658, Nov. 2015.
  • [5] H. R. Bourne, Y. Weinstein, K. L. Melmon, L. M. Lichtenstein, C. S. Henney, and G. M. Shearer, “Modulation of Inflammation and Immunity by Cyclic AMP,” Science (80-. )., vol. 184, no. 4132, pp. 19–28, Apr. 1974.
  • [6] P. M. Epstein and R. Hachisu, “Cyclic nucleotide phosphodiesterase in normal and leukemic human lymphocytes and lymphoblasts.,” Adv. Cyclic Nucleotide Protein Phosphorylation Res., vol. 16, pp. 303–24, 1984.
  • [7] M. D. Leibowitz et al., “A Novel Insulin Secretagogue Is a Phosphodiesterase Inhibitor,” Diabetes, vol. 44, pp. 68–74, 1995.
  • [8] E. M. Grivsky, S. Lee, C. W. Sigel, D. S. Duch, and C. A. Nichol, “Synthesis and antitumor activity of 2,4-diamino-6-(2,5-dimethoxybenzyl)-5-methylpyrido[2,3-d]pyrimidine,” J. Med. Chem., vol. 23, no. 3, pp. 327–329, Mar. 1980.
  • [9] Y. Hamamoto and N. Yamamoto, “Anti-Fas monoclonal antibody is cytocidal to human,” Proc. Nati. Acad. Sci., vol. 87, no. December, pp. 2–6, 1990.
  • [10] L. K. Wathen, “Method Of Preventing Or Treating Atherosclerosis Or Restenosis,” US 2004/0067947 A1, 2004.
  • [11] W. B. Schwartz, “The Effect of Sulfanilamide on Salt and Water Excretion in Congestive Heart Failure,” N. Engl. J. Med., vol. 240, no. 5, pp. 173–177, Feb. 1949.
  • [12] C. C. L. Quianzon and I. E. Cheikh, “History of current non-insulin medications for diabetes mellitus,” J. Community Hosp. Intern. Med. Perspect., vol. 2, no. 3, pp. 19081, Jan. 2012.
  • [13] N. K. Terrett, A. S. Bell, D. Brown, and P. Ellis, “Sildenafil (VIAGRATM), a potent and selective inhibitor of type 5 cGMP phosphodiesterase with utility for the treatment of male erectile dysfunction,” Bioorg. Med. Chem. Lett., vol. 6, no. 15, pp. 1819–1824, Aug. 1996.
  • [14] C. R. Fischer, Jnos; Ganellin, Analogue-based Drug Discoveryا. 2006.
  • [15] S. Dadiboyena and A. T. Hamme II, “Synthesis of Celecoxib and Structural Analogs- A Review,” Curr. Org. Chem., vol. 16, no. 11, pp. 1390–1407, May 2012.
  • [16] J. B. Baell, A. G. Holloway. “New Subst ructure Filters for Removal of Pan Assay Interference Compounds (PAINS) from Screening Libraries and for Their Exclu sion in Bioassays” Journal Of Medıcınal Chemıstry, vol. 53, no.7, pp. 2719-2740, Apr 8, 2010.
  • [17] S. Batra, Y. A. Sabnis, P. J. Rosenthal et al. “Structure-based approach to falci-pain- 2 inhibitors: Synthesis and biological eva luation of 1,6,7-trisubstituted dihydroi soquinolines and isoquinolines,” Bioorga nic&Medıcınal Chemıstry, vol.11, no.3, pp. 2293-2299, May 15, 2003.
  • [18] N. Berber, M. Arslan, C. Bilen et al. “Synthesis and evaluation of new phthala zine substituted beta-lactam derivatives as carbonic anhydrase inhibitors,” Russian Journal of Bioorganic Chemistry, vol. 41, no. 4, pp. 414-420, Jul, 2015.
  • [19] M. Kalaycı, C. Türkeş, M. Arslan, Y. De mir, S. Beydemir “Novel benzoic acid de rivatives: Synthesis and biological evalua tion as multitarget acetylcholinesterase and carbonic anhydrase inhibitors,” Arch Pharm., e2000282, 2020. https://doi.org/10.1002/ardp.202000282
  • [20] B. Sever, C. Türkes, M. D. Altıntop, Y. Demir, S. Beydemir “Thiazolyl- pyrazo- line derivatives: In vitro and in silico eva luation as potential acetylcholinesterase and carbonic anhydrase inhibitors,” Inter national Journal of Biological Macromo lecules, vol. 163, pp. 1970-1988, 2020.
  • [21] A. Topal, M. Atamanalp, E. Oruç, Y. De mir, S. Beydemir, A. Işık “In vivo chan-ges in carbonic anhydrase activity and histo pathology of gill and liver tissues after acute exposure to chlorpyrifos in rainbow trout,” Archives of Industrial Hygiene and Toxicology, vol. 65, no. 4, pp. 377-385, 2014.
  • [22] I. Gulcin, S. Beydemir “Phenolic Compo unds as Antioxidants: Carbonic Anhyd rase Isoenzymes Inhibitors,” Mini Re views in Medicinal Chemistry, vol. 13, no. 3, pp. 408-430, 2013.
  • [23] M. Tugrak, H. I. Gul, Y. Demir, I. Gulcin “Synthesis of benzamide derivatives with thiourea‐substituted benzenesulfonamides as carbonic anhydrase inhibitors,” Arch Pharm., e2000230, 2020. https://doi.org/10.1002/ardp.202000230
  • [24] T. Demirci, M. Arslan, Ç. Bilen, D. Demir, N. Gençer, and O. Arslan, “Synthesis and carbonic anhydrase inhibitory properties of 1,3-dicarbonyl derivatives of methylaminobenzene-sulfonamide,” J. Enzyme Inhib. Med. Chem., vol. 29, no. 1, pp. 132–136, 2014.
  • [25] J. A. Verpoorte, S. Mehta, and J. T. Edsall, “Esterase activities of human carbonic anhydrases B and C.,” J. Biol. Chem., vol. 242, no. 18, pp. 4221–9, Sep. 1967.
  • [26] H. Lineweaver and D. Burk, “The Determination of Enzyme Dissociation Constants,” J. Am. Chem. Soc., vol. 56, no. 3, pp. 658–666, Mar. 1934.
  • [27] C. Yung-Chi and W. H. Prusoff, “Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction,” Biochem. Pharmacol., vol. 22, no. 23, pp. 3099–3108, Dec. 1973.
  • [28] C. T. Supuran, A. S. A. Altamimi, and F. Carta, “Carbonic anhydrase inhibition and the management of glaucoma: a literature and patent review 2013-2019,” Expert Opin. Ther. Pat., vol. 29, no. 10, pp. 781–792, Oct. 2019.
  • [29] E. Masini, S. Sgambellone, and L. Lucarini, “Carbonic anhydrase inhibitors as ophthalmologic drugs for the treatment of glaucoma,” in Carbonic Anhydrases, Elsevier, 2019, pp. 269–285.
  • [30] S. Kalinin et al., “Highly hydrophilic 1,3-oxazol-5-yl benzenesulfonamide inhibitors of carbonic anhydrase II for reduction of glaucoma-related intraocular pressure,” Bioorganic Med. Chem., vol. 27, no. 21, p. 115086, 2019.
  • [31] E. Berrino and F. Carta, “Carbonic anhydrase inhibitors for the treatment of epilepsy and obesity,” in Carbonic Anhydrases, Elsevier, 2019, pp. 311–329.
  • [32] C. T. Supuran, “Carbonic anhydrase inhibitors as emerging agents for the treatment and imaging of hypoxic tumors,” Expert Opin. Investig. Drugs, vol. 27, no. 12, pp. 963–970, Dec. 2018.
  • [33] C. T. Supuran, “Carbonic Anhydrase Inhibition and the Management of Hypoxic Tumors,” Metabolites, vol. 7, no. 3, p. 48, Sep. 2017.
  • [34] Y. Zhou, R. B. Mokhtari, J. Pan, E. Cutz, and H. Yeger, “Carbonic Anhydrase II Mediates Malignant Behavior of Pulmonary Neuroendocrine Tumors,” Am. J. Respir. Cell Mol. Biol., vol. 52, no. 2, pp. 183–192, Feb. 2015.
  • [35] Z. Huyut, Ş. Beydemir, and İ. Gülçin, “Inhibition properties of some flavonoids on carbonic anhydrase I and II isoenzymes purified from human erythrocytes,” J. Biochem. Mol. Toxicol., vol. 31, no. 9, p. e21930, Sep. 2017.
  • [36] H. Göcer, A. Akıncıoğlu, S. Göksu, and İ. Gülçin, “Carbonic anhydrase inhibitory properties of phenolic sulfonamides derived from dopamine related compounds,” Arab. J. Chem., vol. 10, no. 3, pp. 398–402, 2017.
  • [37] T. Gokcen, M. Al, M. Topal, I. Gulcin, T. Ozturk, and A. C. Goren, “Synthesis of some natural sulphonamide derivatives as carbonic anhydrase inhibitors,” Org. Commun., vol. 10, no. 1, pp. 15–23, 2017.
  • [38] E. Garibov et al., “Synthesis of 4,5-disubstituted-2-thioxo-1,2,3,4-tetrahydropyrimidines and investigation of their acetylcholinesterase, butyrylcholinesterase, carbonic anhydrase I/II inhibitory and antioxidant activities,” J. Enzyme Inhib. Med. Chem., vol. 31, pp. 1–9, 2016.
Year 2021, Volume: 25 Issue: 1, 200 - 211, 01.02.2021
https://doi.org/10.16984/saufenbilder.688414

Abstract

Project Number

2012-02-04-033/2016-50-02-002.

References

  • [1] M. Conrad and M. Guthzeit, “Ueber Barbitursäurederivate,” Berichte der Dtsch. Chem. Gesellschaft, vol. 15, no. 2, pp. 2844–2850, Jul. 1882.
  • [2] J. T. Mason, J. W. Baker, and F. Pilcher, “Sodium amytal in surgical management,” Am. J. Surg., vol. 9, no. 1, pp. 9–15, Jul. 1930.
  • [3] N. Moussier, L. Bruche, F. Viani, and M. Zanda, “Fluorinated Barbituric Acid Derivatives: Synthesis and Bio-activity,” Curr. Org. Chem., vol. 7, no. 11, pp. 1071–1080, Jul. 2003.
  • [4] A. Barakat et al., “New Diethyl Ammonium Salt of Thiobarbituric Acid Derivative: Synthesis, Molecular Structure Investigations and Docking Studies,” Molecules, vol. 20, no. 11, pp. 20642–20658, Nov. 2015.
  • [5] H. R. Bourne, Y. Weinstein, K. L. Melmon, L. M. Lichtenstein, C. S. Henney, and G. M. Shearer, “Modulation of Inflammation and Immunity by Cyclic AMP,” Science (80-. )., vol. 184, no. 4132, pp. 19–28, Apr. 1974.
  • [6] P. M. Epstein and R. Hachisu, “Cyclic nucleotide phosphodiesterase in normal and leukemic human lymphocytes and lymphoblasts.,” Adv. Cyclic Nucleotide Protein Phosphorylation Res., vol. 16, pp. 303–24, 1984.
  • [7] M. D. Leibowitz et al., “A Novel Insulin Secretagogue Is a Phosphodiesterase Inhibitor,” Diabetes, vol. 44, pp. 68–74, 1995.
  • [8] E. M. Grivsky, S. Lee, C. W. Sigel, D. S. Duch, and C. A. Nichol, “Synthesis and antitumor activity of 2,4-diamino-6-(2,5-dimethoxybenzyl)-5-methylpyrido[2,3-d]pyrimidine,” J. Med. Chem., vol. 23, no. 3, pp. 327–329, Mar. 1980.
  • [9] Y. Hamamoto and N. Yamamoto, “Anti-Fas monoclonal antibody is cytocidal to human,” Proc. Nati. Acad. Sci., vol. 87, no. December, pp. 2–6, 1990.
  • [10] L. K. Wathen, “Method Of Preventing Or Treating Atherosclerosis Or Restenosis,” US 2004/0067947 A1, 2004.
  • [11] W. B. Schwartz, “The Effect of Sulfanilamide on Salt and Water Excretion in Congestive Heart Failure,” N. Engl. J. Med., vol. 240, no. 5, pp. 173–177, Feb. 1949.
  • [12] C. C. L. Quianzon and I. E. Cheikh, “History of current non-insulin medications for diabetes mellitus,” J. Community Hosp. Intern. Med. Perspect., vol. 2, no. 3, pp. 19081, Jan. 2012.
  • [13] N. K. Terrett, A. S. Bell, D. Brown, and P. Ellis, “Sildenafil (VIAGRATM), a potent and selective inhibitor of type 5 cGMP phosphodiesterase with utility for the treatment of male erectile dysfunction,” Bioorg. Med. Chem. Lett., vol. 6, no. 15, pp. 1819–1824, Aug. 1996.
  • [14] C. R. Fischer, Jnos; Ganellin, Analogue-based Drug Discoveryا. 2006.
  • [15] S. Dadiboyena and A. T. Hamme II, “Synthesis of Celecoxib and Structural Analogs- A Review,” Curr. Org. Chem., vol. 16, no. 11, pp. 1390–1407, May 2012.
  • [16] J. B. Baell, A. G. Holloway. “New Subst ructure Filters for Removal of Pan Assay Interference Compounds (PAINS) from Screening Libraries and for Their Exclu sion in Bioassays” Journal Of Medıcınal Chemıstry, vol. 53, no.7, pp. 2719-2740, Apr 8, 2010.
  • [17] S. Batra, Y. A. Sabnis, P. J. Rosenthal et al. “Structure-based approach to falci-pain- 2 inhibitors: Synthesis and biological eva luation of 1,6,7-trisubstituted dihydroi soquinolines and isoquinolines,” Bioorga nic&Medıcınal Chemıstry, vol.11, no.3, pp. 2293-2299, May 15, 2003.
  • [18] N. Berber, M. Arslan, C. Bilen et al. “Synthesis and evaluation of new phthala zine substituted beta-lactam derivatives as carbonic anhydrase inhibitors,” Russian Journal of Bioorganic Chemistry, vol. 41, no. 4, pp. 414-420, Jul, 2015.
  • [19] M. Kalaycı, C. Türkeş, M. Arslan, Y. De mir, S. Beydemir “Novel benzoic acid de rivatives: Synthesis and biological evalua tion as multitarget acetylcholinesterase and carbonic anhydrase inhibitors,” Arch Pharm., e2000282, 2020. https://doi.org/10.1002/ardp.202000282
  • [20] B. Sever, C. Türkes, M. D. Altıntop, Y. Demir, S. Beydemir “Thiazolyl- pyrazo- line derivatives: In vitro and in silico eva luation as potential acetylcholinesterase and carbonic anhydrase inhibitors,” Inter national Journal of Biological Macromo lecules, vol. 163, pp. 1970-1988, 2020.
  • [21] A. Topal, M. Atamanalp, E. Oruç, Y. De mir, S. Beydemir, A. Işık “In vivo chan-ges in carbonic anhydrase activity and histo pathology of gill and liver tissues after acute exposure to chlorpyrifos in rainbow trout,” Archives of Industrial Hygiene and Toxicology, vol. 65, no. 4, pp. 377-385, 2014.
  • [22] I. Gulcin, S. Beydemir “Phenolic Compo unds as Antioxidants: Carbonic Anhyd rase Isoenzymes Inhibitors,” Mini Re views in Medicinal Chemistry, vol. 13, no. 3, pp. 408-430, 2013.
  • [23] M. Tugrak, H. I. Gul, Y. Demir, I. Gulcin “Synthesis of benzamide derivatives with thiourea‐substituted benzenesulfonamides as carbonic anhydrase inhibitors,” Arch Pharm., e2000230, 2020. https://doi.org/10.1002/ardp.202000230
  • [24] T. Demirci, M. Arslan, Ç. Bilen, D. Demir, N. Gençer, and O. Arslan, “Synthesis and carbonic anhydrase inhibitory properties of 1,3-dicarbonyl derivatives of methylaminobenzene-sulfonamide,” J. Enzyme Inhib. Med. Chem., vol. 29, no. 1, pp. 132–136, 2014.
  • [25] J. A. Verpoorte, S. Mehta, and J. T. Edsall, “Esterase activities of human carbonic anhydrases B and C.,” J. Biol. Chem., vol. 242, no. 18, pp. 4221–9, Sep. 1967.
  • [26] H. Lineweaver and D. Burk, “The Determination of Enzyme Dissociation Constants,” J. Am. Chem. Soc., vol. 56, no. 3, pp. 658–666, Mar. 1934.
  • [27] C. Yung-Chi and W. H. Prusoff, “Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction,” Biochem. Pharmacol., vol. 22, no. 23, pp. 3099–3108, Dec. 1973.
  • [28] C. T. Supuran, A. S. A. Altamimi, and F. Carta, “Carbonic anhydrase inhibition and the management of glaucoma: a literature and patent review 2013-2019,” Expert Opin. Ther. Pat., vol. 29, no. 10, pp. 781–792, Oct. 2019.
  • [29] E. Masini, S. Sgambellone, and L. Lucarini, “Carbonic anhydrase inhibitors as ophthalmologic drugs for the treatment of glaucoma,” in Carbonic Anhydrases, Elsevier, 2019, pp. 269–285.
  • [30] S. Kalinin et al., “Highly hydrophilic 1,3-oxazol-5-yl benzenesulfonamide inhibitors of carbonic anhydrase II for reduction of glaucoma-related intraocular pressure,” Bioorganic Med. Chem., vol. 27, no. 21, p. 115086, 2019.
  • [31] E. Berrino and F. Carta, “Carbonic anhydrase inhibitors for the treatment of epilepsy and obesity,” in Carbonic Anhydrases, Elsevier, 2019, pp. 311–329.
  • [32] C. T. Supuran, “Carbonic anhydrase inhibitors as emerging agents for the treatment and imaging of hypoxic tumors,” Expert Opin. Investig. Drugs, vol. 27, no. 12, pp. 963–970, Dec. 2018.
  • [33] C. T. Supuran, “Carbonic Anhydrase Inhibition and the Management of Hypoxic Tumors,” Metabolites, vol. 7, no. 3, p. 48, Sep. 2017.
  • [34] Y. Zhou, R. B. Mokhtari, J. Pan, E. Cutz, and H. Yeger, “Carbonic Anhydrase II Mediates Malignant Behavior of Pulmonary Neuroendocrine Tumors,” Am. J. Respir. Cell Mol. Biol., vol. 52, no. 2, pp. 183–192, Feb. 2015.
  • [35] Z. Huyut, Ş. Beydemir, and İ. Gülçin, “Inhibition properties of some flavonoids on carbonic anhydrase I and II isoenzymes purified from human erythrocytes,” J. Biochem. Mol. Toxicol., vol. 31, no. 9, p. e21930, Sep. 2017.
  • [36] H. Göcer, A. Akıncıoğlu, S. Göksu, and İ. Gülçin, “Carbonic anhydrase inhibitory properties of phenolic sulfonamides derived from dopamine related compounds,” Arab. J. Chem., vol. 10, no. 3, pp. 398–402, 2017.
  • [37] T. Gokcen, M. Al, M. Topal, I. Gulcin, T. Ozturk, and A. C. Goren, “Synthesis of some natural sulphonamide derivatives as carbonic anhydrase inhibitors,” Org. Commun., vol. 10, no. 1, pp. 15–23, 2017.
  • [38] E. Garibov et al., “Synthesis of 4,5-disubstituted-2-thioxo-1,2,3,4-tetrahydropyrimidines and investigation of their acetylcholinesterase, butyrylcholinesterase, carbonic anhydrase I/II inhibitory and antioxidant activities,” J. Enzyme Inhib. Med. Chem., vol. 31, pp. 1–9, 2016.
There are 38 citations in total.

Details

Primary Language English
Subjects Chemical Engineering
Journal Section Research Articles
Authors

Tuna Demirci 0000-0001-8933-4944

Oğuzhan Özdemir 0000-0002-9588-3285

Mustafa Oğuzhan Kaya 0000-0002-8592-1567

Mustafa Arslan 0000-0003-0796-4374

Project Number 2012-02-04-033/2016-50-02-002.
Publication Date February 1, 2021
Submission Date February 13, 2020
Acceptance Date December 24, 2020
Published in Issue Year 2021 Volume: 25 Issue: 1

Cite

APA Demirci, T., Özdemir, O., Kaya, M. O., Arslan, M. (2021). Synthesis and Biological Evaluation of Novel Dihydro [2,3D] Pyridine Substituted Enaminosulfonamide Compounds as Potent Human Erythrocyte Carbonic Anhydrase II (hCAII). Sakarya University Journal of Science, 25(1), 200-211. https://doi.org/10.16984/saufenbilder.688414
AMA Demirci T, Özdemir O, Kaya MO, Arslan M. Synthesis and Biological Evaluation of Novel Dihydro [2,3D] Pyridine Substituted Enaminosulfonamide Compounds as Potent Human Erythrocyte Carbonic Anhydrase II (hCAII). SAUJS. February 2021;25(1):200-211. doi:10.16984/saufenbilder.688414
Chicago Demirci, Tuna, Oğuzhan Özdemir, Mustafa Oğuzhan Kaya, and Mustafa Arslan. “Synthesis and Biological Evaluation of Novel Dihydro [2,3D] Pyridine Substituted Enaminosulfonamide Compounds As Potent Human Erythrocyte Carbonic Anhydrase II (hCAII)”. Sakarya University Journal of Science 25, no. 1 (February 2021): 200-211. https://doi.org/10.16984/saufenbilder.688414.
EndNote Demirci T, Özdemir O, Kaya MO, Arslan M (February 1, 2021) Synthesis and Biological Evaluation of Novel Dihydro [2,3D] Pyridine Substituted Enaminosulfonamide Compounds as Potent Human Erythrocyte Carbonic Anhydrase II (hCAII). Sakarya University Journal of Science 25 1 200–211.
IEEE T. Demirci, O. Özdemir, M. O. Kaya, and M. Arslan, “Synthesis and Biological Evaluation of Novel Dihydro [2,3D] Pyridine Substituted Enaminosulfonamide Compounds as Potent Human Erythrocyte Carbonic Anhydrase II (hCAII)”, SAUJS, vol. 25, no. 1, pp. 200–211, 2021, doi: 10.16984/saufenbilder.688414.
ISNAD Demirci, Tuna et al. “Synthesis and Biological Evaluation of Novel Dihydro [2,3D] Pyridine Substituted Enaminosulfonamide Compounds As Potent Human Erythrocyte Carbonic Anhydrase II (hCAII)”. Sakarya University Journal of Science 25/1 (February 2021), 200-211. https://doi.org/10.16984/saufenbilder.688414.
JAMA Demirci T, Özdemir O, Kaya MO, Arslan M. Synthesis and Biological Evaluation of Novel Dihydro [2,3D] Pyridine Substituted Enaminosulfonamide Compounds as Potent Human Erythrocyte Carbonic Anhydrase II (hCAII). SAUJS. 2021;25:200–211.
MLA Demirci, Tuna et al. “Synthesis and Biological Evaluation of Novel Dihydro [2,3D] Pyridine Substituted Enaminosulfonamide Compounds As Potent Human Erythrocyte Carbonic Anhydrase II (hCAII)”. Sakarya University Journal of Science, vol. 25, no. 1, 2021, pp. 200-11, doi:10.16984/saufenbilder.688414.
Vancouver Demirci T, Özdemir O, Kaya MO, Arslan M. Synthesis and Biological Evaluation of Novel Dihydro [2,3D] Pyridine Substituted Enaminosulfonamide Compounds as Potent Human Erythrocyte Carbonic Anhydrase II (hCAII). SAUJS. 2021;25(1):200-11.