Identification of novel chemical scaffolds Inhibiting trypanothione synthetase from pathogenic trypanosomatids

The search for novel chemical entities targeting essential and parasite-specific pathways is considered a priority for neglected diseases such as trypanosomiasis and leishmaniasis. The thiol-dependent redox metabolism of trypanosomatids relies on bis-glutathionylspermidine [trypanothione, T(SH)2],...

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Autores principales: Benítez, Diego, Medeiros, Andrea, Fiestas, Lucía, Panozzo Zénere, Esteban Andrés, Maiwald, Franziska, Prousis, Kyriakos C., Roussaki, Marina, Calogeropoulou, Theodora, Detsi, Anastasia, Jaeger, Timo, Šarlauskas, Jonas, Peterlin Mašič, Lucíja, Kunick, Conrad, Labadie, Guillermo Roberto, Flohé, Leopold, Comini, Marcelo A.
Formato: article artículo publishedVersion
Lenguaje:Inglés
Publicado: Public Library of Science (PLOS) 2020
Materias:
Acceso en línea:http://hdl.handle.net/2133/19536
http://hdl.handle.net/2133/19536
Aporte de:
id I15-R121-2133-19536
record_format dspace
institution Universidad Nacional de Rosario
institution_str I-15
repository_str R-121
collection Repositorio Hipermedial de la Universidad Nacional de Rosario (UNR)
language Inglés
orig_language_str_mv eng
topic Neglected Diseases
Trypanothione Synthetase Inhibitors
Pathogenic Trypanosomatids
Leishmania
Trypanosoma
spellingShingle Neglected Diseases
Trypanothione Synthetase Inhibitors
Pathogenic Trypanosomatids
Leishmania
Trypanosoma
Benítez, Diego
Medeiros, Andrea
Fiestas, Lucía
Panozzo Zénere, Esteban Andrés
Maiwald, Franziska
Prousis, Kyriakos C.
Roussaki, Marina
Calogeropoulou, Theodora
Detsi, Anastasia
Jaeger, Timo
Šarlauskas, Jonas
Peterlin Mašič, Lucíja
Kunick, Conrad
Labadie, Guillermo Roberto
Flohé, Leopold
Comini, Marcelo A.
Identification of novel chemical scaffolds Inhibiting trypanothione synthetase from pathogenic trypanosomatids
topic_facet Neglected Diseases
Trypanothione Synthetase Inhibitors
Pathogenic Trypanosomatids
Leishmania
Trypanosoma
description The search for novel chemical entities targeting essential and parasite-specific pathways is considered a priority for neglected diseases such as trypanosomiasis and leishmaniasis. The thiol-dependent redox metabolism of trypanosomatids relies on bis-glutathionylspermidine [trypanothione, T(SH)2], a low molecular mass cosubstrate absent in the host. In pathogenic trypanosomatids, a single enzyme, trypanothione synthetase (TryS), catalyzes trypanothione biosynthesis, which is indispensable for parasite survival. Thus, TryS qualifies as an attractive drug target candidate.
format article
artículo
publishedVersion
author Benítez, Diego
Medeiros, Andrea
Fiestas, Lucía
Panozzo Zénere, Esteban Andrés
Maiwald, Franziska
Prousis, Kyriakos C.
Roussaki, Marina
Calogeropoulou, Theodora
Detsi, Anastasia
Jaeger, Timo
Šarlauskas, Jonas
Peterlin Mašič, Lucíja
Kunick, Conrad
Labadie, Guillermo Roberto
Flohé, Leopold
Comini, Marcelo A.
author_facet Benítez, Diego
Medeiros, Andrea
Fiestas, Lucía
Panozzo Zénere, Esteban Andrés
Maiwald, Franziska
Prousis, Kyriakos C.
Roussaki, Marina
Calogeropoulou, Theodora
Detsi, Anastasia
Jaeger, Timo
Šarlauskas, Jonas
Peterlin Mašič, Lucíja
Kunick, Conrad
Labadie, Guillermo Roberto
Flohé, Leopold
Comini, Marcelo A.
author_sort Benítez, Diego
title Identification of novel chemical scaffolds Inhibiting trypanothione synthetase from pathogenic trypanosomatids
title_short Identification of novel chemical scaffolds Inhibiting trypanothione synthetase from pathogenic trypanosomatids
title_full Identification of novel chemical scaffolds Inhibiting trypanothione synthetase from pathogenic trypanosomatids
title_fullStr Identification of novel chemical scaffolds Inhibiting trypanothione synthetase from pathogenic trypanosomatids
title_full_unstemmed Identification of novel chemical scaffolds Inhibiting trypanothione synthetase from pathogenic trypanosomatids
title_sort identification of novel chemical scaffolds inhibiting trypanothione synthetase from pathogenic trypanosomatids
publisher Public Library of Science (PLOS)
publishDate 2020
url http://hdl.handle.net/2133/19536
http://hdl.handle.net/2133/19536
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