Docking de herbicidas na glutationa transferase tau4-4 de soja (Glycine max)
Ano de defesa: | 2011 |
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Autor(a) principal: | |
Orientador(a): | |
Banca de defesa: | |
Tipo de documento: | Dissertação |
Tipo de acesso: | Acesso aberto |
Idioma: | por |
Instituição de defesa: |
Universidade Federal de São Carlos
|
Programa de Pós-Graduação: |
Programa de Pós-Graduação em Biotecnologia - PPGBiotec
|
Departamento: |
Não Informado pela instituição
|
País: |
BR
|
Palavras-chave em Português: | |
Palavras-chave em Inglês: | |
Área do conhecimento CNPq: | |
Link de acesso: | https://repositorio.ufscar.br/handle/ufscar/6974 |
Resumo: | This study, based on molecular docking, describes the search for the most favorable conformations when complexes between herbicides, used in soybean cultivation, and an enzyme involved in the detoxification process are formed and based on these results some guidelines for the developing of new compounds are proposed. The glutathione transferase Tau, GmGSTU4-4, from soybean was the target protein, and diclofop, fluazifop, Clethodim, clomazone, diquat, paraquat, atrazine, diuron, bentazone, acifluorofem, fomesafem, sulfentrazone, glyphosate and clorimurom, the 14 herbicides studied. These last ones were chosen based on the list of those that are used in soybean crops and are registered with the Ministry of Agriculture and Supply of Brasil. For all of them the GmGSTU4-4-herbicide complexes were obtained. The protein binding site, analyzed by molecular visualization, presents an almost cylindrical shape, open and exposed to the solvent and is composed of two sites G and H. Three water molecules were observed in the G-site in that participate in molecular interactions with several of the studied herbicides, This finding suggests that new compounds that could, and should, be developed need to have in their structure chemical groups capable of interacting with the water, both as donors and acceptors of hydrogen bonds. Another interesting finding was that the largest herbicides may occupy both the G and H sites, and seem to be most promising in the activity of detoxification. |
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Mendes, Josiane EnevinaSchpector, Júlio Zukermanhttp://lattes.cnpq.br/4252331837170383http://lattes.cnpq.br/709004889934018214939005-3515-4e35-a752-f333e0e42b4c2016-08-17T18:39:37Z2011-05-262016-08-17T18:39:37Z2011-03-30MENDES, Josiane Enevina. Docking de herbicidas na glutationa transferase TAU4-4 de soja (Glycine Max). 2011. 104 f. Dissertação (Mestrado em Multidisciplinar) - Universidade Federal de São Carlos, São Carlos, 2011.https://repositorio.ufscar.br/handle/ufscar/6974This study, based on molecular docking, describes the search for the most favorable conformations when complexes between herbicides, used in soybean cultivation, and an enzyme involved in the detoxification process are formed and based on these results some guidelines for the developing of new compounds are proposed. The glutathione transferase Tau, GmGSTU4-4, from soybean was the target protein, and diclofop, fluazifop, Clethodim, clomazone, diquat, paraquat, atrazine, diuron, bentazone, acifluorofem, fomesafem, sulfentrazone, glyphosate and clorimurom, the 14 herbicides studied. These last ones were chosen based on the list of those that are used in soybean crops and are registered with the Ministry of Agriculture and Supply of Brasil. For all of them the GmGSTU4-4-herbicide complexes were obtained. The protein binding site, analyzed by molecular visualization, presents an almost cylindrical shape, open and exposed to the solvent and is composed of two sites G and H. Three water molecules were observed in the G-site in that participate in molecular interactions with several of the studied herbicides, This finding suggests that new compounds that could, and should, be developed need to have in their structure chemical groups capable of interacting with the water, both as donors and acceptors of hydrogen bonds. Another interesting finding was that the largest herbicides may occupy both the G and H sites, and seem to be most promising in the activity of detoxification.Este estudo, baseado em docking molecular, descreve a busca das conformações mais favoráveis para a formação dos complexos alvo-ligante com herbicidas utilizados no cultivo de soja e uma enzima envolvida no processo de desintoxicação, e baseado nestes resultados são propostas algumas diretrizes para o desenvolvimento de novos compostos. A proteína estudada foi a glutationa transferase Tau de soja, a GmGSTU4-4. Foram estudados 14 herbicidas: diclofope, fluazifope, cletodim, clomazona, diquate, paraquate, atrazina, diurom, bentazona, acifluorofem, fomesafem, sulfentrazona, clorimurom e glifosato. A escolha dos herbicidas se baseou na lista daqueles que são utilizados na cultura da soja e estão registrados no Ministério da Agricultura e Abastecimento do Brasil. Foram obtidos os complexos GmGSTU4-4-herbicidas. O sítio de ligação analisado por visualização molecular mostra uma forma quase cilíndrica, aberta e exposta ao solvente e composto de dois sítios G e H. No sítio G foram observadas três moléculas de água que participam de interações moleculares com vários dos herbicidas estudados o que sugere que novos compostos poderiam ser desenvolvidos observando a necessidade da presença de grupos químicos capazes de interagir com a água, tanto como doadores como aceptores de ligações de hidrogênio. Os herbicidas maiores podem ocupar os sítio G e H e parecem ser mais promissores na atividade de desintoxicação.Financiadora de Estudos e Projetosapplication/pdfporUniversidade Federal de São CarlosPrograma de Pós-Graduação em Biotecnologia - PPGBiotecUFSCarBRBiotecnologiaModelagem molecularDesintoxicação metabólicaDockingHerbicidasGlutationa transferase TauDockingMolecular ModelingHerbicidesGlutathione transferase TauOUTROSDocking de herbicidas na glutationa transferase tau4-4 de soja (Glycine max)Docking de herbicidas na glutationa transferase TAU4-4 de soja (Glycine Max)info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesis-1-1e0a7cf72-f4fb-48f4-93c2-3e7bc492b3cbinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UFSCARinstname:Universidade Federal de São Carlos (UFSCAR)instacron:UFSCARORIGINAL3640.pdfapplication/pdf5869617https://repositorio.ufscar.br/bitstream/ufscar/6974/1/3640.pdf4643e7ab6ff128afd74bd3d51d8588f3MD51TEXT3640.pdf.txt3640.pdf.txtExtracted texttext/plain166727https://repositorio.ufscar.br/bitstream/ufscar/6974/2/3640.pdf.txtbefb2e04e8d4691005baa0166c9e3ed3MD52THUMBNAIL3640.pdf.jpg3640.pdf.jpgIM Thumbnailimage/jpeg6155https://repositorio.ufscar.br/bitstream/ufscar/6974/3/3640.pdf.jpg7fec5df32a4f9516573954656f959d39MD53ufscar/69742023-09-18 18:30:33.597oai:repositorio.ufscar.br:ufscar/6974Repositório InstitucionalPUBhttps://repositorio.ufscar.br/oai/requestopendoar:43222023-09-18T18:30:33Repositório Institucional da UFSCAR - Universidade Federal de São Carlos (UFSCAR)false |
dc.title.por.fl_str_mv |
Docking de herbicidas na glutationa transferase tau4-4 de soja (Glycine max) |
dc.title.alternative.eng.fl_str_mv |
Docking de herbicidas na glutationa transferase TAU4-4 de soja (Glycine Max) |
title |
Docking de herbicidas na glutationa transferase tau4-4 de soja (Glycine max) |
spellingShingle |
Docking de herbicidas na glutationa transferase tau4-4 de soja (Glycine max) Mendes, Josiane Enevina Biotecnologia Modelagem molecular Desintoxicação metabólica Docking Herbicidas Glutationa transferase Tau Docking Molecular Modeling Herbicides Glutathione transferase Tau OUTROS |
title_short |
Docking de herbicidas na glutationa transferase tau4-4 de soja (Glycine max) |
title_full |
Docking de herbicidas na glutationa transferase tau4-4 de soja (Glycine max) |
title_fullStr |
Docking de herbicidas na glutationa transferase tau4-4 de soja (Glycine max) |
title_full_unstemmed |
Docking de herbicidas na glutationa transferase tau4-4 de soja (Glycine max) |
title_sort |
Docking de herbicidas na glutationa transferase tau4-4 de soja (Glycine max) |
author |
Mendes, Josiane Enevina |
author_facet |
Mendes, Josiane Enevina |
author_role |
author |
dc.contributor.authorlattes.por.fl_str_mv |
http://lattes.cnpq.br/7090048899340182 |
dc.contributor.author.fl_str_mv |
Mendes, Josiane Enevina |
dc.contributor.advisor1.fl_str_mv |
Schpector, Júlio Zukerman |
dc.contributor.advisor1Lattes.fl_str_mv |
http://lattes.cnpq.br/4252331837170383 |
dc.contributor.authorID.fl_str_mv |
14939005-3515-4e35-a752-f333e0e42b4c |
contributor_str_mv |
Schpector, Júlio Zukerman |
dc.subject.por.fl_str_mv |
Biotecnologia Modelagem molecular Desintoxicação metabólica Docking Herbicidas Glutationa transferase Tau |
topic |
Biotecnologia Modelagem molecular Desintoxicação metabólica Docking Herbicidas Glutationa transferase Tau Docking Molecular Modeling Herbicides Glutathione transferase Tau OUTROS |
dc.subject.eng.fl_str_mv |
Docking Molecular Modeling Herbicides Glutathione transferase Tau |
dc.subject.cnpq.fl_str_mv |
OUTROS |
description |
This study, based on molecular docking, describes the search for the most favorable conformations when complexes between herbicides, used in soybean cultivation, and an enzyme involved in the detoxification process are formed and based on these results some guidelines for the developing of new compounds are proposed. The glutathione transferase Tau, GmGSTU4-4, from soybean was the target protein, and diclofop, fluazifop, Clethodim, clomazone, diquat, paraquat, atrazine, diuron, bentazone, acifluorofem, fomesafem, sulfentrazone, glyphosate and clorimurom, the 14 herbicides studied. These last ones were chosen based on the list of those that are used in soybean crops and are registered with the Ministry of Agriculture and Supply of Brasil. For all of them the GmGSTU4-4-herbicide complexes were obtained. The protein binding site, analyzed by molecular visualization, presents an almost cylindrical shape, open and exposed to the solvent and is composed of two sites G and H. Three water molecules were observed in the G-site in that participate in molecular interactions with several of the studied herbicides, This finding suggests that new compounds that could, and should, be developed need to have in their structure chemical groups capable of interacting with the water, both as donors and acceptors of hydrogen bonds. Another interesting finding was that the largest herbicides may occupy both the G and H sites, and seem to be most promising in the activity of detoxification. |
publishDate |
2011 |
dc.date.available.fl_str_mv |
2011-05-26 2016-08-17T18:39:37Z |
dc.date.issued.fl_str_mv |
2011-03-30 |
dc.date.accessioned.fl_str_mv |
2016-08-17T18:39:37Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/masterThesis |
format |
masterThesis |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
MENDES, Josiane Enevina. Docking de herbicidas na glutationa transferase TAU4-4 de soja (Glycine Max). 2011. 104 f. Dissertação (Mestrado em Multidisciplinar) - Universidade Federal de São Carlos, São Carlos, 2011. |
dc.identifier.uri.fl_str_mv |
https://repositorio.ufscar.br/handle/ufscar/6974 |
identifier_str_mv |
MENDES, Josiane Enevina. Docking de herbicidas na glutationa transferase TAU4-4 de soja (Glycine Max). 2011. 104 f. Dissertação (Mestrado em Multidisciplinar) - Universidade Federal de São Carlos, São Carlos, 2011. |
url |
https://repositorio.ufscar.br/handle/ufscar/6974 |
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por |
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por |
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info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
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application/pdf |
dc.publisher.none.fl_str_mv |
Universidade Federal de São Carlos |
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Programa de Pós-Graduação em Biotecnologia - PPGBiotec |
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UFSCar |
dc.publisher.country.fl_str_mv |
BR |
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Universidade Federal de São Carlos |
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