New Sulfanilamide Derivatives Incorporating Heterocyclic Carboxamide Moieties as Carbonic Anhydrase Inhibitors

Carbonic Anhydrases (CAs) are ubiquitous metalloenzymes involved in several disease conditions. There are 15 human CA (hCA) isoforms and their high homology represents a challenge for the discovery of potential drugs devoid of off-target side effects. For this reason, many synthetic and pharmacologi...

Full description

Bibliographic Details
Main Authors:	Andrea Angeli, Victor Kartsev, Anthi Petrou, Mariana Pinteala, Roman M. Vydzhak, Svitlana Y. Panchishin, Volodymyr Brovarets, Viviana De Luca, Clemente Capasso, Athina Geronikaki, Claudiu T. Supuran
Format:	Article
Language:	English
Published:	MDPI AG 2021-08-01
Series:	Pharmaceuticals
Subjects:	carbonic anhydrase metalloenzymes inhibitors molecular docking
Online Access:	https://www.mdpi.com/1424-8247/14/8/828

id	doaj-0d1ef5c1b80c463e9793bfa891279b9b
record_format	Article
spelling	doaj-0d1ef5c1b80c463e9793bfa891279b9b2021-08-26T14:12:33ZengMDPI AGPharmaceuticals1424-82472021-08-011482882810.3390/ph14080828New Sulfanilamide Derivatives Incorporating Heterocyclic Carboxamide Moieties as Carbonic Anhydrase InhibitorsAndrea Angeli0Victor Kartsev1Anthi Petrou2Mariana Pinteala3Roman M. Vydzhak4Svitlana Y. Panchishin5Volodymyr Brovarets6Viviana De Luca7Clemente Capasso8Athina Geronikaki9Claudiu T. Supuran10Department of Chemistry “Ugo Schiff”, University of Florence, Via della Lastruccia 3-13, 50019 Sesto Fiorentino, ItalyInterBioScreen, Chernogolovka, 142432 Chernogolovka, Moscow Region, RussiaDepartment of Pharmacy, School of Health, Aristotle University of Thessaloniki, 54124 Thessaloniki, GreeceCentre of Advanced Research in Bionanoconjugates and Biopolymers Department, “Petru Poni” Institute of Macromolecular Chemistry, 707410 Iasi, RomaniaDepartment of Chemistry of Bioactive Nitrogen-Containing Heterocyclic Bases, V.P. Kukhar Institute of Bioorganic Chemistry and Petrochemistry, NAS of Ukraine 1, Murmanska St, 02094 Kyiv, UkraineDepartment of Chemistry of Bioactive Nitrogen-Containing Heterocyclic Bases, V.P. Kukhar Institute of Bioorganic Chemistry and Petrochemistry, NAS of Ukraine 1, Murmanska St, 02094 Kyiv, UkraineDepartment of Chemistry of Bioactive Nitrogen-Containing Heterocyclic Bases, V.P. Kukhar Institute of Bioorganic Chemistry and Petrochemistry, NAS of Ukraine 1, Murmanska St, 02094 Kyiv, UkraineInstitute of Biosciences and Bioresources, CNR, Via Pietro Castellino 111, 80131 Napoli, ItalyInstitute of Biosciences and Bioresources, CNR, Via Pietro Castellino 111, 80131 Napoli, ItalyDepartment of Pharmacy, School of Health, Aristotle University of Thessaloniki, 54124 Thessaloniki, GreeceDepartment of Chemistry “Ugo Schiff”, University of Florence, Via della Lastruccia 3-13, 50019 Sesto Fiorentino, ItalyCarbonic Anhydrases (CAs) are ubiquitous metalloenzymes involved in several disease conditions. There are 15 human CA (hCA) isoforms and their high homology represents a challenge for the discovery of potential drugs devoid of off-target side effects. For this reason, many synthetic and pharmacologic research efforts are underway to achieve the full pharmacological potential of CA modulators of activity. We report here a novel series of sulfanilamide derivatives containing heterocyclic carboxamide moieties which were evaluated as CA inhibitors against the physiological relevant isoforms hCA I, II, IX, and XII. Some of them showed selectivity toward isoform hCA II and hCA XII. Molecular docking was performed for some of these compounds on isoforms hCA II and XII to understand the possible interaction with the active site amino acid residues, which rationalized the reported inhibitory activity.https://www.mdpi.com/1424-8247/14/8/828carbonic anhydrasemetalloenzymesinhibitorsmolecular docking
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Andrea Angeli Victor Kartsev Anthi Petrou Mariana Pinteala Roman M. Vydzhak Svitlana Y. Panchishin Volodymyr Brovarets Viviana De Luca Clemente Capasso Athina Geronikaki Claudiu T. Supuran
spellingShingle	Andrea Angeli Victor Kartsev Anthi Petrou Mariana Pinteala Roman M. Vydzhak Svitlana Y. Panchishin Volodymyr Brovarets Viviana De Luca Clemente Capasso Athina Geronikaki Claudiu T. Supuran New Sulfanilamide Derivatives Incorporating Heterocyclic Carboxamide Moieties as Carbonic Anhydrase Inhibitors Pharmaceuticals carbonic anhydrase metalloenzymes inhibitors molecular docking
author_facet	Andrea Angeli Victor Kartsev Anthi Petrou Mariana Pinteala Roman M. Vydzhak Svitlana Y. Panchishin Volodymyr Brovarets Viviana De Luca Clemente Capasso Athina Geronikaki Claudiu T. Supuran
author_sort	Andrea Angeli
title	New Sulfanilamide Derivatives Incorporating Heterocyclic Carboxamide Moieties as Carbonic Anhydrase Inhibitors
title_short	New Sulfanilamide Derivatives Incorporating Heterocyclic Carboxamide Moieties as Carbonic Anhydrase Inhibitors
title_full	New Sulfanilamide Derivatives Incorporating Heterocyclic Carboxamide Moieties as Carbonic Anhydrase Inhibitors
title_fullStr	New Sulfanilamide Derivatives Incorporating Heterocyclic Carboxamide Moieties as Carbonic Anhydrase Inhibitors
title_full_unstemmed	New Sulfanilamide Derivatives Incorporating Heterocyclic Carboxamide Moieties as Carbonic Anhydrase Inhibitors
title_sort	new sulfanilamide derivatives incorporating heterocyclic carboxamide moieties as carbonic anhydrase inhibitors
publisher	MDPI AG
series	Pharmaceuticals
issn	1424-8247
publishDate	2021-08-01
description	Carbonic Anhydrases (CAs) are ubiquitous metalloenzymes involved in several disease conditions. There are 15 human CA (hCA) isoforms and their high homology represents a challenge for the discovery of potential drugs devoid of off-target side effects. For this reason, many synthetic and pharmacologic research efforts are underway to achieve the full pharmacological potential of CA modulators of activity. We report here a novel series of sulfanilamide derivatives containing heterocyclic carboxamide moieties which were evaluated as CA inhibitors against the physiological relevant isoforms hCA I, II, IX, and XII. Some of them showed selectivity toward isoform hCA II and hCA XII. Molecular docking was performed for some of these compounds on isoforms hCA II and XII to understand the possible interaction with the active site amino acid residues, which rationalized the reported inhibitory activity.
topic	carbonic anhydrase metalloenzymes inhibitors molecular docking
url	https://www.mdpi.com/1424-8247/14/8/828
work_keys_str_mv	AT andreaangeli newsulfanilamidederivativesincorporatingheterocycliccarboxamidemoietiesascarbonicanhydraseinhibitors AT victorkartsev newsulfanilamidederivativesincorporatingheterocycliccarboxamidemoietiesascarbonicanhydraseinhibitors AT anthipetrou newsulfanilamidederivativesincorporatingheterocycliccarboxamidemoietiesascarbonicanhydraseinhibitors AT marianapinteala newsulfanilamidederivativesincorporatingheterocycliccarboxamidemoietiesascarbonicanhydraseinhibitors AT romanmvydzhak newsulfanilamidederivativesincorporatingheterocycliccarboxamidemoietiesascarbonicanhydraseinhibitors AT svitlanaypanchishin newsulfanilamidederivativesincorporatingheterocycliccarboxamidemoietiesascarbonicanhydraseinhibitors AT volodymyrbrovarets newsulfanilamidederivativesincorporatingheterocycliccarboxamidemoietiesascarbonicanhydraseinhibitors AT vivianadeluca newsulfanilamidederivativesincorporatingheterocycliccarboxamidemoietiesascarbonicanhydraseinhibitors AT clementecapasso newsulfanilamidederivativesincorporatingheterocycliccarboxamidemoietiesascarbonicanhydraseinhibitors AT athinageronikaki newsulfanilamidederivativesincorporatingheterocycliccarboxamidemoietiesascarbonicanhydraseinhibitors AT claudiutsupuran newsulfanilamidederivativesincorporatingheterocycliccarboxamidemoietiesascarbonicanhydraseinhibitors
_version_	1721190699270930432

New Sulfanilamide Derivatives Incorporating Heterocyclic Carboxamide Moieties as Carbonic Anhydrase Inhibitors

Similar Items