In silico molecular modeling and docking studies on the leishmanial tryparedoxin peroxidase

Detalhes bibliográficos
Autor(a) principal: Mutlu,Ozal
Data de Publicação: 2014
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Archives of Biology and Technology
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132014000200013
Resumo: Leishmaniasis is one of the most common form of neglected parasitic disease that affects about 350 million people worldwide. Leishmanias have a trypanothione mediated hydroperoxide metabolism to eliminate endogenous or exogenous oxidative agents. Both of 2-Cys peroxiredoxin (Prx) and glutathione peroxidase type tryparedoxin peroxidase (Px) are the terminal enzymes in the trypanothione dependent detoxification system. Therefore absence of trypanothione redox system in mammals and the sensitivity of trypanosomatids against oxidative stress, enzymes of this pathway are drug targets candidates. In this study, 3D structure of tryparedoxin peroxidase (2-Cys peroxiredoxin type) from Leishmania donovani (LdTXNPx) was described by homology modeling method based on the template of tryparedoxin peroxidase from Crithidia fasciculata and selected compounds were docked to the active site pocket. The quality of the 3D structure of the model was confirmed by various web based validation programs. When compared secondary and tertiary structure of the model, it showed a typical thioredoxin fold containing a central beta-sheet and three alpha-helices. Docking study showed that the selected compound 2 (CID 16073813) interacted with the active site amino acids and binding energy was -118.675 kcal/mol.
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spelling In silico molecular modeling and docking studies on the leishmanial tryparedoxin peroxidaseHomology modelingdockingLeishmania donovanitryparedoxin peroxidasehydroperoxide metabolismLeishmaniasis is one of the most common form of neglected parasitic disease that affects about 350 million people worldwide. Leishmanias have a trypanothione mediated hydroperoxide metabolism to eliminate endogenous or exogenous oxidative agents. Both of 2-Cys peroxiredoxin (Prx) and glutathione peroxidase type tryparedoxin peroxidase (Px) are the terminal enzymes in the trypanothione dependent detoxification system. Therefore absence of trypanothione redox system in mammals and the sensitivity of trypanosomatids against oxidative stress, enzymes of this pathway are drug targets candidates. In this study, 3D structure of tryparedoxin peroxidase (2-Cys peroxiredoxin type) from Leishmania donovani (LdTXNPx) was described by homology modeling method based on the template of tryparedoxin peroxidase from Crithidia fasciculata and selected compounds were docked to the active site pocket. The quality of the 3D structure of the model was confirmed by various web based validation programs. When compared secondary and tertiary structure of the model, it showed a typical thioredoxin fold containing a central beta-sheet and three alpha-helices. Docking study showed that the selected compound 2 (CID 16073813) interacted with the active site amino acids and binding energy was -118.675 kcal/mol.Instituto de Tecnologia do Paraná - Tecpar2014-04-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132014000200013Brazilian Archives of Biology and Technology v.57 n.2 2014reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/S1516-89132014000200013info:eu-repo/semantics/openAccessMutlu,Ozaleng2014-04-04T00:00:00Zoai:scielo:S1516-89132014000200013Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2014-04-04T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false
dc.title.none.fl_str_mv In silico molecular modeling and docking studies on the leishmanial tryparedoxin peroxidase
title In silico molecular modeling and docking studies on the leishmanial tryparedoxin peroxidase
spellingShingle In silico molecular modeling and docking studies on the leishmanial tryparedoxin peroxidase
Mutlu,Ozal
Homology modeling
docking
Leishmania donovani
tryparedoxin peroxidase
hydroperoxide metabolism
title_short In silico molecular modeling and docking studies on the leishmanial tryparedoxin peroxidase
title_full In silico molecular modeling and docking studies on the leishmanial tryparedoxin peroxidase
title_fullStr In silico molecular modeling and docking studies on the leishmanial tryparedoxin peroxidase
title_full_unstemmed In silico molecular modeling and docking studies on the leishmanial tryparedoxin peroxidase
title_sort In silico molecular modeling and docking studies on the leishmanial tryparedoxin peroxidase
author Mutlu,Ozal
author_facet Mutlu,Ozal
author_role author
dc.contributor.author.fl_str_mv Mutlu,Ozal
dc.subject.por.fl_str_mv Homology modeling
docking
Leishmania donovani
tryparedoxin peroxidase
hydroperoxide metabolism
topic Homology modeling
docking
Leishmania donovani
tryparedoxin peroxidase
hydroperoxide metabolism
description Leishmaniasis is one of the most common form of neglected parasitic disease that affects about 350 million people worldwide. Leishmanias have a trypanothione mediated hydroperoxide metabolism to eliminate endogenous or exogenous oxidative agents. Both of 2-Cys peroxiredoxin (Prx) and glutathione peroxidase type tryparedoxin peroxidase (Px) are the terminal enzymes in the trypanothione dependent detoxification system. Therefore absence of trypanothione redox system in mammals and the sensitivity of trypanosomatids against oxidative stress, enzymes of this pathway are drug targets candidates. In this study, 3D structure of tryparedoxin peroxidase (2-Cys peroxiredoxin type) from Leishmania donovani (LdTXNPx) was described by homology modeling method based on the template of tryparedoxin peroxidase from Crithidia fasciculata and selected compounds were docked to the active site pocket. The quality of the 3D structure of the model was confirmed by various web based validation programs. When compared secondary and tertiary structure of the model, it showed a typical thioredoxin fold containing a central beta-sheet and three alpha-helices. Docking study showed that the selected compound 2 (CID 16073813) interacted with the active site amino acids and binding energy was -118.675 kcal/mol.
publishDate 2014
dc.date.none.fl_str_mv 2014-04-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132014000200013
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132014000200013
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S1516-89132014000200013
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Instituto de Tecnologia do Paraná - Tecpar
publisher.none.fl_str_mv Instituto de Tecnologia do Paraná - Tecpar
dc.source.none.fl_str_mv Brazilian Archives of Biology and Technology v.57 n.2 2014
reponame:Brazilian Archives of Biology and Technology
instname:Instituto de Tecnologia do Paraná (Tecpar)
instacron:TECPAR
instname_str Instituto de Tecnologia do Paraná (Tecpar)
instacron_str TECPAR
institution TECPAR
reponame_str Brazilian Archives of Biology and Technology
collection Brazilian Archives of Biology and Technology
repository.name.fl_str_mv Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)
repository.mail.fl_str_mv babt@tecpar.br||babt@tecpar.br
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