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      Fluoroenesulphonamides: N-sulphonylurea isosteres showing nanomolar selective cancer-related transmembrane human carbonic anhydrase inhibition

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          Abstract

          After hydrofluorination of ynesulphonamides in superacid or in the presence of hydrofluoric acid/base reagents, a series of α-fluoroenamides has been synthesised and tested for the inhibition of carbonic anhydrase (CA, EC 4.2.1.1) isoforms. This study reveals a new, highly selective family of cancer-related transmembrane human (h) CA IX/XII inhibitors. These original fluorinated ureido isosters do not inhibit the widespread cytosolic isoforms hCA I and II and selectively inhibit the transmembrane cancer-related hCA IX and XII, offering interesting new leads for future studies.

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          Ureido-substituted benzenesulfonamides potently inhibit carbonic anhydrase IX and show antimetastatic activity in a model of breast cancer metastasis.

          Daniela Vullo, Andrea Scozzafava, Shoukat Dedhar … (2011)
          A series of ureido-substituted benzenesulfonamides was prepared that showed a very interesting profile for the inhibition of several human carbonic anhydrases (hCAs, EC 4.2.1.1), such as hCAs I and II (cytosolic isoforms) and hCAs IX and XII (transmembrane, tumor-associated enzymes). Excellent inhibition of all these isoforms has been observed with various members of the series, depending on the substitution pattern of the urea moiety. Several low nanomolar CA IX/XII inhibitors also showing good selectivity for the transmembrane over the cytosolic isoforms have been discovered. One of them, 4-{[(3'-nitrophenyl)carbamoyl]amino}benzenesulfonamide, significantly inhibited the formation of metastases by the highly aggressive 4T1 mammary tumor cells at pharmacologic concentrations of 45 mg/kg, constituting an interesting candidate for the development of conceptually novel antimetastatic drugs.
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            The carbon dioxide hydration activity of carbonic anhydrase. I. Stop-flow kinetic studies on the native human isoenzymes B and C.

            R Khalifah (1971)
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              Inhibition of carbonic anhydrase IX targets primary tumors, metastases, and cancer stem cells: Three for the price of one

              Claudiu Supuran, Vincenzo Alterio, Anna Di Fiore … (2018)
              Human carbonic anhydrase (CA) IX is a tumor-associated protein, since it is scarcely present in normal tissues, but highly overexpressed in a large number of solid tumors, where it actively contributes to survival and metastatic spread of tumor cells. Due to these features, the characterization of its biochemical, structural, and functional features for drug design purposes has been extensively carried out, with consequent development of several highly selective small molecule inhibitors and monoclonal antibodies to be used for different purposes. Aim of this review is to provide a comprehensive state-of-the-art of studies performed on this enzyme, regarding structural, functional, and biomedical aspects, as well as the development of molecules with diagnostic and therapeutic applications for cancer treatment. A brief description of additional pharmacologic applications for CA IX inhibition in other diseases, such as arthritis and ischemia, is also provided.
              Article 0 comments Cited 73 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): J Enzyme Inhib Med Chem
                Journal ID (iso-abbrev): J Enzyme Inhib Med Chem
                Journal ID (publisher-id): IENZ
                Journal ID (publisher-id): ienz20
                Title: Journal of Enzyme Inhibition and Medicinal Chemistry
                Publisher: Taylor & Francis
                ISSN (Print): 1475-6366
                ISSN (Electronic): 1475-6374
                Publication date Collection: 2018
                Publication date (Electronic): 30 April 2018
                Volume: 33
                Issue: 1
                Pages: 804-808
                Affiliations
                [a ]IC2MP-UMR CNRS 7582, Superacid Group–Organic Synthesis Team, Université de Poitiers , Poitiers, France;
                [b ]Department NEUROFARBA–Pharmaceutical and Nutraceutical Chemistry Section, Università degli Studi di Firenze , Sesto Fiorentino, Florence, Italy;
                [c ]Institut Lavoisier de Versailles, UMR CNRS 8180, Universitée de Versailles Saint-Quentin-en-Yvelines , Versailles, France;
                [d ]Laboratoire de Chimie Organique, Service de Chimie et Physico Chimie Organiques, Université Libre de Bruxelles , Brussels, Belgium
                Author notes
                CONTACT Claudiu T. Supuran claudiu.supuran@ 123456unifi.it Department NEUROFARBA–Pharmaceutical and Nutraceutical Chemistry Section, Università degli Studi di Firenze , Sesto Fiorentino, Florence, Italy;
                Sebastien Thibaudeau sebastien.thibaudeau@ 123456univ-poitiers.fr IC2MP-UMR CNRS 7582, Superacid Group–Organic Synthesis Team, Université de Poitiers , Poitiers, France
                Article
                Publisher ID: 1461097
                DOI: 10.1080/14756366.2018.1461097
                PMC ID: 6009971
                PubMed ID: 29706097
                SO-VID: 3a4f3647-091a-493b-9953-1961f50e6bdb
                Copyright © © 2018 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.
                License:

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 07 March 2018
                Date revision received : 29 March 2018
                Date accepted : 02 April 2018
                Page count
                Pages: 5, Words: 4162
                Categories
                Subject: Short Communication

                ScienceOpen disciplines: Pharmaceutical chemistry
                Keywords: superacid,hydrofluorination,fluorinated isosters,carbonic anhydrase inhibitors,ureas
                Data availability:
                ScienceOpen disciplines: Pharmaceutical chemistry
                Keywords: superacid, hydrofluorination, fluorinated isosters, carbonic anhydrase inhibitors, ureas

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