Selenocarbamates As a Prodrug‐Based Approach to Carbonic Anhydrase Inhibition

A study on the activity of selenocarbamates as a novel chemotype acting as carbonic anhydrase (CA, EC 4.2.1.1) inhibitors is reported. Undergoing CA‐mediated hydrolysis, selenocarbamates release selenolates behaving as zinc binding groups and effectively inhibiting CAs. A series of selenocarbamates...

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Detalles Bibliográficos
Autores principales: Angeli, Andrea, Ferraroni, Marta, Capperucci, Antonella, Tanini, Damiano, Costantino, Gabriele, Supuran, Claudiu T.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2022
Materias:
Research Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9310613/
https://www.ncbi.nlm.nih.gov/pubmed/35238480
http://dx.doi.org/10.1002/cmdc.202200085
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author Angeli, Andrea
Ferraroni, Marta
Capperucci, Antonella
Tanini, Damiano
Costantino, Gabriele
Supuran, Claudiu T.
author_facet Angeli, Andrea
Ferraroni, Marta
Capperucci, Antonella
Tanini, Damiano
Costantino, Gabriele
Supuran, Claudiu T.
author_sort Angeli, Andrea
collection PubMed
description A study on the activity of selenocarbamates as a novel chemotype acting as carbonic anhydrase (CA, EC 4.2.1.1) inhibitors is reported. Undergoing CA‐mediated hydrolysis, selenocarbamates release selenolates behaving as zinc binding groups and effectively inhibiting CAs. A series of selenocarbamates characterised by high molecular diversity and complexity have been studied against different human CA isoforms such as hCA I, II, IX and XII. Selenocarbamates behave as masked selenols with potential biological applications as prodrugs for CAs inhibition‐based strategies. X‐ray studies provided insights into the binding mode of this novel class of CA inhibitors.
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spelling pubmed-93106132022-07-29 Selenocarbamates As a Prodrug‐Based Approach to Carbonic Anhydrase Inhibition Angeli, Andrea Ferraroni, Marta Capperucci, Antonella Tanini, Damiano Costantino, Gabriele Supuran, Claudiu T. ChemMedChem Research Articles A study on the activity of selenocarbamates as a novel chemotype acting as carbonic anhydrase (CA, EC 4.2.1.1) inhibitors is reported. Undergoing CA‐mediated hydrolysis, selenocarbamates release selenolates behaving as zinc binding groups and effectively inhibiting CAs. A series of selenocarbamates characterised by high molecular diversity and complexity have been studied against different human CA isoforms such as hCA I, II, IX and XII. Selenocarbamates behave as masked selenols with potential biological applications as prodrugs for CAs inhibition‐based strategies. X‐ray studies provided insights into the binding mode of this novel class of CA inhibitors. John Wiley and Sons Inc. 2022-03-23 2022-06-03 /pmc/articles/PMC9310613/ /pubmed/35238480 http://dx.doi.org/10.1002/cmdc.202200085 Text en © 2022 The Authors. ChemMedChem published by Wiley-VCH GmbH https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Angeli, Andrea
Ferraroni, Marta
Capperucci, Antonella
Tanini, Damiano
Costantino, Gabriele
Supuran, Claudiu T.
Selenocarbamates As a Prodrug‐Based Approach to Carbonic Anhydrase Inhibition
title Selenocarbamates As a Prodrug‐Based Approach to Carbonic Anhydrase Inhibition
title_full Selenocarbamates As a Prodrug‐Based Approach to Carbonic Anhydrase Inhibition
title_fullStr Selenocarbamates As a Prodrug‐Based Approach to Carbonic Anhydrase Inhibition
title_full_unstemmed Selenocarbamates As a Prodrug‐Based Approach to Carbonic Anhydrase Inhibition
title_short Selenocarbamates As a Prodrug‐Based Approach to Carbonic Anhydrase Inhibition
title_sort selenocarbamates as a prodrug‐based approach to carbonic anhydrase inhibition
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9310613/
https://www.ncbi.nlm.nih.gov/pubmed/35238480
http://dx.doi.org/10.1002/cmdc.202200085
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