Review of the article „POM Analyses of Carbacylamidophosphates and Sulfanylamidophosphates Tested as New Carbonic Anhydrase Inhibitors“, verified by Publons, Web of Science
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Abstract: Six representatives of the amidophosphate derivatives (L1-L6) were synthesized and evaluated for their biological activities against carbonic anhydrase enzyme. Out of the six derivatives, L1 (IC50 = 12.5 ± 1.35 μM), and L2 (IC50 = 3.12 ± 0.45 μM) showed potent activity against BCA-II, whereas (L3, L4 and L5) showed weak inhibitory activity with the IC50 value of 24.5 ± 2.25, 24.5 ± 2.25, 55.5± 1.60, and 75.5 ± 1.25 μM respectively. They were found to be weak inhibitors of carbonic anhydrase as compared to acetazolamide (IC50 =0.12 ± 0.03 μM) which was used as standard inhibitor. All physic-chemical parameters were derived from the computational Petra/Osiris/Molinspiration/DFT (POM/DFT) model. They govern the bioactivity amidophosphate derivatives (L1-L6) which contain O,Opharmacophore site. The six compounds (L1-L6) analyzed here were previously screened experimentally and now screened virtually for their anti-carbonic anhydrase activity. The highest anti-carbonic anhydrase a...ctivity was obtained for compound L2 which exhibited excellent bioactivity (% inhibition = 95%) when compared to acetazolamide (% inhibition = 89%). The compound L3 represents an increased activity as compared to its analogues (L4- L6). The increase of bioactivity from L3 to L4-L6 could be attributed to the existence of minimum steric effect of substituents of P=O moiety which plays a crucial template role in the organization of anti-carbonic anhydrase O,O-phramacophore sites. Moreover, it is cheap, leading to fewer side effects and is possible to be included in selective anti-carbonic anhydrase agents design.
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Medicinal Chemistry, 2019, 1/BMS-MC-2019-29-24Collections
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Mašinski fakultetTY - JOUR AU - Jovanović, Tamara PY - 2019 UR - https://machinery.mas.bg.ac.rs/handle/123456789/5914 AB - Abstract: Six representatives of the amidophosphate derivatives (L1-L6) were synthesized and evaluated for their biological activities against carbonic anhydrase enzyme. Out of the six derivatives, L1 (IC50 = 12.5 ± 1.35 μM), and L2 (IC50 = 3.12 ± 0.45 μM) showed potent activity against BCA-II, whereas (L3, L4 and L5) showed weak inhibitory activity with the IC50 value of 24.5 ± 2.25, 24.5 ± 2.25, 55.5± 1.60, and 75.5 ± 1.25 μM respectively. They were found to be weak inhibitors of carbonic anhydrase as compared to acetazolamide (IC50 =0.12 ± 0.03 μM) which was used as standard inhibitor. All physic-chemical parameters were derived from the computational Petra/Osiris/Molinspiration/DFT (POM/DFT) model. They govern the bioactivity amidophosphate derivatives (L1-L6) which contain O,Opharmacophore site. The six compounds (L1-L6) analyzed here were previously screened experimentally and now screened virtually for their anti-carbonic anhydrase activity. The highest anti-carbonic anhydrase activity was obtained for compound L2 which exhibited excellent bioactivity (% inhibition = 95%) when compared to acetazolamide (% inhibition = 89%). The compound L3 represents an increased activity as compared to its analogues (L4- L6). The increase of bioactivity from L3 to L4-L6 could be attributed to the existence of minimum steric effect of substituents of P=O moiety which plays a crucial template role in the organization of anti-carbonic anhydrase O,O-phramacophore sites. Moreover, it is cheap, leading to fewer side effects and is possible to be included in selective anti-carbonic anhydrase agents design. T2 - Medicinal Chemistry T1 - Review of the article „POM Analyses of Carbacylamidophosphates and Sulfanylamidophosphates Tested as New Carbonic Anhydrase Inhibitors“, verified by Publons, Web of Science EP - 24 SP - 1/BMS-MC-2019-29 UR - https://hdl.handle.net/21.15107/rcub_machinery_5914 ER -
@article{ author = "Jovanović, Tamara", year = "2019", abstract = "Abstract: Six representatives of the amidophosphate derivatives (L1-L6) were synthesized and evaluated for their biological activities against carbonic anhydrase enzyme. Out of the six derivatives, L1 (IC50 = 12.5 ± 1.35 μM), and L2 (IC50 = 3.12 ± 0.45 μM) showed potent activity against BCA-II, whereas (L3, L4 and L5) showed weak inhibitory activity with the IC50 value of 24.5 ± 2.25, 24.5 ± 2.25, 55.5± 1.60, and 75.5 ± 1.25 μM respectively. They were found to be weak inhibitors of carbonic anhydrase as compared to acetazolamide (IC50 =0.12 ± 0.03 μM) which was used as standard inhibitor. All physic-chemical parameters were derived from the computational Petra/Osiris/Molinspiration/DFT (POM/DFT) model. They govern the bioactivity amidophosphate derivatives (L1-L6) which contain O,Opharmacophore site. The six compounds (L1-L6) analyzed here were previously screened experimentally and now screened virtually for their anti-carbonic anhydrase activity. The highest anti-carbonic anhydrase activity was obtained for compound L2 which exhibited excellent bioactivity (% inhibition = 95%) when compared to acetazolamide (% inhibition = 89%). The compound L3 represents an increased activity as compared to its analogues (L4- L6). The increase of bioactivity from L3 to L4-L6 could be attributed to the existence of minimum steric effect of substituents of P=O moiety which plays a crucial template role in the organization of anti-carbonic anhydrase O,O-phramacophore sites. Moreover, it is cheap, leading to fewer side effects and is possible to be included in selective anti-carbonic anhydrase agents design.", journal = "Medicinal Chemistry", title = "Review of the article „POM Analyses of Carbacylamidophosphates and Sulfanylamidophosphates Tested as New Carbonic Anhydrase Inhibitors“, verified by Publons, Web of Science", pages = "24-1/BMS-MC-2019-29", url = "https://hdl.handle.net/21.15107/rcub_machinery_5914" }
Jovanović, T.. (2019). Review of the article „POM Analyses of Carbacylamidophosphates and Sulfanylamidophosphates Tested as New Carbonic Anhydrase Inhibitors“, verified by Publons, Web of Science. in Medicinal Chemistry, 1/BMS-MC-2019-29-24. https://hdl.handle.net/21.15107/rcub_machinery_5914
Jovanović T. Review of the article „POM Analyses of Carbacylamidophosphates and Sulfanylamidophosphates Tested as New Carbonic Anhydrase Inhibitors“, verified by Publons, Web of Science. in Medicinal Chemistry. 2019;:1/BMS-MC-2019-29-24. https://hdl.handle.net/21.15107/rcub_machinery_5914 .
Jovanović, Tamara, "Review of the article „POM Analyses of Carbacylamidophosphates and Sulfanylamidophosphates Tested as New Carbonic Anhydrase Inhibitors“, verified by Publons, Web of Science" in Medicinal Chemistry (2019):1/BMS-MC-2019-29-24, https://hdl.handle.net/21.15107/rcub_machinery_5914 .