Calcium channel blockers: molecular docking and inhibition studies on carbonic anhydrase I and II isoenzymes
WOS: 000519177800001 PubMed: 32107977 Carbonic anhydrases (CAs) are potent dehydration of carbonic acid and catalyst of the reversible hydration of carbon dioxide. Here, CA I and CA II was purified from human erythrocytes using the simple chromatographic method and determined the interactions betwee...
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ftanadoluuniv:oai:earsiv.anadolu.edu.tr:11421/23981 2023-05-15T15:52:45+02:00 Calcium channel blockers: molecular docking and inhibition studies on carbonic anhydrase I and II isoenzymes Turkes, Cuneyt Demir, Yeliz Beydemir, Sukru Anadolu Üniversitesi 2020-07-09T20:58:42Z https://hdl.handle.net/11421/23981 https://doi.org/10.1080/07391102.2020.1736631 eng eng Taylor & Francis Inc 10.1080/07391102.2020.1736631 Journal of Biomolecular Structure & Dynamics Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı 0739-1102 1538-0254 https://doi.org/10.1080/07391102.2020.1736631 https://hdl.handle.net/11421/23981 info:eu-repo/semantics/closedAccess Carbonic anhydrase calcium channel blockers enzyme inhibition enzyme purification molecular docking article 2020 ftanadoluuniv https://doi.org/10.1080/07391102.2020.1736631 2020-10-21T11:16:13Z WOS: 000519177800001 PubMed: 32107977 Carbonic anhydrases (CAs) are potent dehydration of carbonic acid and catalyst of the reversible hydration of carbon dioxide. Here, CA I and CA II was purified from human erythrocytes using the simple chromatographic method and determined the interactions between some calcium channel blockers and the enzymes. Molecular docking studies were performed these compounds. It was found that calcium channel blockers (nimodipine, nilvadipine, nitrendipine, isradipine, and nifedipine) exhibit potential inhibitor properties for hCA I and hCA II. IC50 values of hCA I were in the range of 9.24-58.00 mu M, and K-i constants were in the range of 7.60 +/- 2.68-35.92 +/- 16.01 mu M. IC50 values of hCA II were in the range of 70.00-138.60 mu M, and K-i constants were in the range of 48.30 +/- 9.81-162.35 +/- 20.47 mu M. Nimodipine presented the highest docking score and had competitive inhibition, the benzene and pyridine rings were found to enter the cavity for hCA I. Nifedipine and isradipine did not affect hCA II. Among these drugs, nitrendipine was found to be the most potent inhibitor for hCA I and nimodipine for hCA II. These compounds may be useful for CA inhibitors. Communicated by Ramaswamy H. Sarma Article in Journal/Newspaper Carbonic acid Anadolu University Institutional Repository Journal of Biomolecular Structure and Dynamics 39 5 1672 1680 |
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Open Polar |
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Anadolu University Institutional Repository |
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ftanadoluuniv |
language |
English |
topic |
Carbonic anhydrase calcium channel blockers enzyme inhibition enzyme purification molecular docking |
spellingShingle |
Carbonic anhydrase calcium channel blockers enzyme inhibition enzyme purification molecular docking Turkes, Cuneyt Demir, Yeliz Beydemir, Sukru Calcium channel blockers: molecular docking and inhibition studies on carbonic anhydrase I and II isoenzymes |
topic_facet |
Carbonic anhydrase calcium channel blockers enzyme inhibition enzyme purification molecular docking |
description |
WOS: 000519177800001 PubMed: 32107977 Carbonic anhydrases (CAs) are potent dehydration of carbonic acid and catalyst of the reversible hydration of carbon dioxide. Here, CA I and CA II was purified from human erythrocytes using the simple chromatographic method and determined the interactions between some calcium channel blockers and the enzymes. Molecular docking studies were performed these compounds. It was found that calcium channel blockers (nimodipine, nilvadipine, nitrendipine, isradipine, and nifedipine) exhibit potential inhibitor properties for hCA I and hCA II. IC50 values of hCA I were in the range of 9.24-58.00 mu M, and K-i constants were in the range of 7.60 +/- 2.68-35.92 +/- 16.01 mu M. IC50 values of hCA II were in the range of 70.00-138.60 mu M, and K-i constants were in the range of 48.30 +/- 9.81-162.35 +/- 20.47 mu M. Nimodipine presented the highest docking score and had competitive inhibition, the benzene and pyridine rings were found to enter the cavity for hCA I. Nifedipine and isradipine did not affect hCA II. Among these drugs, nitrendipine was found to be the most potent inhibitor for hCA I and nimodipine for hCA II. These compounds may be useful for CA inhibitors. Communicated by Ramaswamy H. Sarma |
author2 |
Anadolu Üniversitesi |
format |
Article in Journal/Newspaper |
author |
Turkes, Cuneyt Demir, Yeliz Beydemir, Sukru |
author_facet |
Turkes, Cuneyt Demir, Yeliz Beydemir, Sukru |
author_sort |
Turkes, Cuneyt |
title |
Calcium channel blockers: molecular docking and inhibition studies on carbonic anhydrase I and II isoenzymes |
title_short |
Calcium channel blockers: molecular docking and inhibition studies on carbonic anhydrase I and II isoenzymes |
title_full |
Calcium channel blockers: molecular docking and inhibition studies on carbonic anhydrase I and II isoenzymes |
title_fullStr |
Calcium channel blockers: molecular docking and inhibition studies on carbonic anhydrase I and II isoenzymes |
title_full_unstemmed |
Calcium channel blockers: molecular docking and inhibition studies on carbonic anhydrase I and II isoenzymes |
title_sort |
calcium channel blockers: molecular docking and inhibition studies on carbonic anhydrase i and ii isoenzymes |
publisher |
Taylor & Francis Inc |
publishDate |
2020 |
url |
https://hdl.handle.net/11421/23981 https://doi.org/10.1080/07391102.2020.1736631 |
genre |
Carbonic acid |
genre_facet |
Carbonic acid |
op_relation |
10.1080/07391102.2020.1736631 Journal of Biomolecular Structure & Dynamics Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı 0739-1102 1538-0254 https://doi.org/10.1080/07391102.2020.1736631 https://hdl.handle.net/11421/23981 |
op_rights |
info:eu-repo/semantics/closedAccess |
op_doi |
https://doi.org/10.1080/07391102.2020.1736631 |
container_title |
Journal of Biomolecular Structure and Dynamics |
container_volume |
39 |
container_issue |
5 |
container_start_page |
1672 |
op_container_end_page |
1680 |
_version_ |
1766387857456365568 |