From Sensors to Silencers: Quinoline- and Benzimidazole-Sulfonamides as Inhibitors for Zinc Proteases

[Image: see text] Derived from the extensive work in the area of small molecule zinc(II) ion sensors, chelating fragment libraries of quinoline- and benzimidazole-sulfonamides have been prepared and screened against several different zinc(II)-dependent matrix metalloproteinases (MMPs). The fragments...

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Autores principales: Rouffet, Matthieu, de Oliveira, César Augusto F., Udi, Yael, Agrawal, Arpita, Sagi, Irit, McCammon, J. Andrew, Cohen, Seth M.
Formato: Texto
Lenguaje:English
Publicado: American Chemical Society 2010
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2886603/
https://www.ncbi.nlm.nih.gov/pubmed/20507095
http://dx.doi.org/10.1021/ja101088j
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author Rouffet, Matthieu
de Oliveira, César Augusto F.
Udi, Yael
Agrawal, Arpita
Sagi, Irit
McCammon, J. Andrew
Cohen, Seth M.
author_facet Rouffet, Matthieu
de Oliveira, César Augusto F.
Udi, Yael
Agrawal, Arpita
Sagi, Irit
McCammon, J. Andrew
Cohen, Seth M.
author_sort Rouffet, Matthieu
collection PubMed
description [Image: see text] Derived from the extensive work in the area of small molecule zinc(II) ion sensors, chelating fragment libraries of quinoline- and benzimidazole-sulfonamides have been prepared and screened against several different zinc(II)-dependent matrix metalloproteinases (MMPs). The fragments show impressive inhibition of these metalloenzymes and preferences for different MMPs based on the nature of the chelating group. The findings show that focused chelator libraries are a powerful strategy for the discovery of lead fragments for metalloprotein inhibition.
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spelling pubmed-28866032010-06-16 From Sensors to Silencers: Quinoline- and Benzimidazole-Sulfonamides as Inhibitors for Zinc Proteases Rouffet, Matthieu de Oliveira, César Augusto F. Udi, Yael Agrawal, Arpita Sagi, Irit McCammon, J. Andrew Cohen, Seth M. J Am Chem Soc [Image: see text] Derived from the extensive work in the area of small molecule zinc(II) ion sensors, chelating fragment libraries of quinoline- and benzimidazole-sulfonamides have been prepared and screened against several different zinc(II)-dependent matrix metalloproteinases (MMPs). The fragments show impressive inhibition of these metalloenzymes and preferences for different MMPs based on the nature of the chelating group. The findings show that focused chelator libraries are a powerful strategy for the discovery of lead fragments for metalloprotein inhibition. American Chemical Society 2010-05-27 2010-06-23 /pmc/articles/PMC2886603/ /pubmed/20507095 http://dx.doi.org/10.1021/ja101088j Text en Copyright © 2010 American Chemical Society http://pubs.acs.org This is an open-access article distributed under the ACS AuthorChoice Terms & Conditions. Any use of this article, must conform to the terms of that license which are available at http://pubs.acs.org.
spellingShingle Rouffet, Matthieu
de Oliveira, César Augusto F.
Udi, Yael
Agrawal, Arpita
Sagi, Irit
McCammon, J. Andrew
Cohen, Seth M.
From Sensors to Silencers: Quinoline- and Benzimidazole-Sulfonamides as Inhibitors for Zinc Proteases
title From Sensors to Silencers: Quinoline- and Benzimidazole-Sulfonamides as Inhibitors for Zinc Proteases
title_full From Sensors to Silencers: Quinoline- and Benzimidazole-Sulfonamides as Inhibitors for Zinc Proteases
title_fullStr From Sensors to Silencers: Quinoline- and Benzimidazole-Sulfonamides as Inhibitors for Zinc Proteases
title_full_unstemmed From Sensors to Silencers: Quinoline- and Benzimidazole-Sulfonamides as Inhibitors for Zinc Proteases
title_short From Sensors to Silencers: Quinoline- and Benzimidazole-Sulfonamides as Inhibitors for Zinc Proteases
title_sort from sensors to silencers: quinoline- and benzimidazole-sulfonamides as inhibitors for zinc proteases
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2886603/
https://www.ncbi.nlm.nih.gov/pubmed/20507095
http://dx.doi.org/10.1021/ja101088j
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