Furosemide blocks the anion channel caused by Staphylococcus aureus α-hemolysin

Detalhes bibliográficos
Autor(a) principal: Teixeira, Luciana
Data de Publicação: 2022
Outros Autores: Silva Júnior, Janilson, Vieira, Pedro, Canto, Marcus, Figueirêdo, Anne Gabryelle, Machado, Dijanah, Silva, Joelmir
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Anais da Faculdade de Medicina de Olinda (Online)
Texto Completo: https://afmo.emnuvens.com.br/afmo/article/view/192
Resumo: To investigate the effect of furosemide on Staphylococcus aureus α-hemolysin (α-HL) channel in planar lipid bilayers by electrophysiological characterization and molecular docking studies. Planar lipid bilayer membranes were prepared and α-HL (0.07 mg/mL) was added to the standard solution in cis compartment of the experimental chamber. All experiments were performed at room temperature using an Axopatch 200A amplifier in the voltage clamp mode. At pH 7.5, α-HL channels were usually in a high conductance ~4 nS and rarely switch to low conductance states. After the ion channel was incorporated in bilayer membrane, the furosemide was also added to the standard solution to the cis compartment. To docking studies, atomics coordinates for the α-HL heptameric channel was retrieved from PDB ID (7AHL) and the structure of furosemide was removed from the PubChem, their coordinates were built and minimized with Avogadro software. The molecular docking experiments were performed using the Dockthor online. The furosemide inhibited (P<0.05) conductance α-HL channel and it was a voltage-dependent manner. The two best docking solutions and the α-HL channel were evaluated, it was observed the connection mode with the highest affinity of interaction has a greater number of hydrogen bonding. The residues were 113 and 147 that form the remainders of the constriction α-HL channel. In conclusion, furosemide blocks ion currents in the constriction of channel caused by Staphylococcus aureus α-hemolysin.
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spelling Furosemide blocks the anion channel caused by Staphylococcus aureus α-hemolysin Furosemida bloqueia canal aniônico formado pela α-hemolisina de Staphylococcus aureus.FurosemidaStaphylococcus aureusCanal iônicoFator de virulênciaAgente AntimicrobianoFurosemideStaphylococcus aureusIon channelVirulence factorsAnti-bacterial agentTo investigate the effect of furosemide on Staphylococcus aureus α-hemolysin (α-HL) channel in planar lipid bilayers by electrophysiological characterization and molecular docking studies. Planar lipid bilayer membranes were prepared and α-HL (0.07 mg/mL) was added to the standard solution in cis compartment of the experimental chamber. All experiments were performed at room temperature using an Axopatch 200A amplifier in the voltage clamp mode. At pH 7.5, α-HL channels were usually in a high conductance ~4 nS and rarely switch to low conductance states. After the ion channel was incorporated in bilayer membrane, the furosemide was also added to the standard solution to the cis compartment. To docking studies, atomics coordinates for the α-HL heptameric channel was retrieved from PDB ID (7AHL) and the structure of furosemide was removed from the PubChem, their coordinates were built and minimized with Avogadro software. The molecular docking experiments were performed using the Dockthor online. The furosemide inhibited (P<0.05) conductance α-HL channel and it was a voltage-dependent manner. The two best docking solutions and the α-HL channel were evaluated, it was observed the connection mode with the highest affinity of interaction has a greater number of hydrogen bonding. The residues were 113 and 147 that form the remainders of the constriction α-HL channel. In conclusion, furosemide blocks ion currents in the constriction of channel caused by Staphylococcus aureus α-hemolysin.Investigar o efeito de furosemida no canal α-hemolisina (α-HL) de Staphylococcus aureus em bicamadas lipídicas planares por caracterização eletrofisiológica e estudos de docking molecular. As membranas planares de bicamada lipídica foram preparadas e α-HL (0,07 mg/mL) foi adicionada à solução padrão no compartimento cis da câmara experimental. Todos os experimentos foram realizados em temperatura ambiente usando um amplificador Axopatch 200A no modo voltage clamp. Em pH 7,5, os canais α-HL estavam geralmente em uma alta condutância ~ 4 nS e raramente mudam para estados de baixa condutância. Após a incorporação do canal iônico na membrana bicamada, a furosemida também foi adicionada à solução padrão no compartimento cis. Para os estudos de docking, as coordenadas atômicas para o canal heptamérico α-HL foram recuperadas do PDB ID (7AHL) e a estrutura de furosemida foi obtida do PubChem, suas coordenadas foram elaboradas e minimizadas com o software Avogadro. Os experimentos de docking molecular foram realizados usando o Dockthor online. A furosemida inibiu (P<0,05) a condutância do canal α-HL de maneira voltagem-dependente. Foram avaliadas as duas melhores soluções de docking e o canal α-HL, observou-se que o modo de conexão com maior afinidade de interação possui maior número de ligações de hidrogênio. Os resíduos de ligação foram o 113 e o 147, que formam os remanescentes de constrição do canal α-HL. Em conclusão, a furosemida bloqueia as correntes iônicas na constrição do canal causado pela α-hemolisina de Staphylococcus aureus.Faculdade de Medicina de Olinda2022-12-22info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://afmo.emnuvens.com.br/afmo/article/view/19210.56102/afmo.2022.192ANNALS OF OLINDA MEDICAL SCHOOL; Vol. 1 No. 7 (2022); 19-23Anais da Faculdade de Medicina de Olinda; v. 1 n. 7 (2022); 19-232674-84872595-1734reponame:Anais da Faculdade de Medicina de Olinda (Online)instname:Faculdade de Medicina de Olinda (FMO)instacron:FMOenghttps://afmo.emnuvens.com.br/afmo/article/view/192/109Copyright (c) 2022 Luciana Teixeira, Janilson Silva Júnior, Pedro Vieira, Marcus Canto, Anne Gabryelle Figueirêdo, Dijanah Machado, Joelmir Silvahttps://creativecommons.org/licenses/by/4.0info:eu-repo/semantics/openAccessTeixeira, LucianaSilva Júnior, JanilsonVieira, Pedro Canto, Marcus Figueirêdo, Anne GabryelleMachado, DijanahSilva, Joelmir2022-12-22T19:56:55Zoai:ojs.afmo.emnuvens.com.br:article/192Revistahttps://afmo.emnuvens.com.br/afmoPUBhttps://afmo.emnuvens.com.br/afmo/oaianaisfmo@fmo.edu.br2674-84872595-1734opendoar:2022-12-22T19:56:55Anais da Faculdade de Medicina de Olinda (Online) - Faculdade de Medicina de Olinda (FMO)false
dc.title.none.fl_str_mv Furosemide blocks the anion channel caused by Staphylococcus aureus α-hemolysin
Furosemida bloqueia canal aniônico formado pela α-hemolisina de Staphylococcus aureus.
title Furosemide blocks the anion channel caused by Staphylococcus aureus α-hemolysin
spellingShingle Furosemide blocks the anion channel caused by Staphylococcus aureus α-hemolysin
Teixeira, Luciana
Furosemida
Staphylococcus aureus
Canal iônico
Fator de virulência
Agente Antimicrobiano
Furosemide
Staphylococcus aureus
Ion channel
Virulence factors
Anti-bacterial agent
title_short Furosemide blocks the anion channel caused by Staphylococcus aureus α-hemolysin
title_full Furosemide blocks the anion channel caused by Staphylococcus aureus α-hemolysin
title_fullStr Furosemide blocks the anion channel caused by Staphylococcus aureus α-hemolysin
title_full_unstemmed Furosemide blocks the anion channel caused by Staphylococcus aureus α-hemolysin
title_sort Furosemide blocks the anion channel caused by Staphylococcus aureus α-hemolysin
author Teixeira, Luciana
author_facet Teixeira, Luciana
Silva Júnior, Janilson
Vieira, Pedro
Canto, Marcus
Figueirêdo, Anne Gabryelle
Machado, Dijanah
Silva, Joelmir
author_role author
author2 Silva Júnior, Janilson
Vieira, Pedro
Canto, Marcus
Figueirêdo, Anne Gabryelle
Machado, Dijanah
Silva, Joelmir
author2_role author
author
author
author
author
author
dc.contributor.author.fl_str_mv Teixeira, Luciana
Silva Júnior, Janilson
Vieira, Pedro
Canto, Marcus
Figueirêdo, Anne Gabryelle
Machado, Dijanah
Silva, Joelmir
dc.subject.por.fl_str_mv Furosemida
Staphylococcus aureus
Canal iônico
Fator de virulência
Agente Antimicrobiano
Furosemide
Staphylococcus aureus
Ion channel
Virulence factors
Anti-bacterial agent
topic Furosemida
Staphylococcus aureus
Canal iônico
Fator de virulência
Agente Antimicrobiano
Furosemide
Staphylococcus aureus
Ion channel
Virulence factors
Anti-bacterial agent
description To investigate the effect of furosemide on Staphylococcus aureus α-hemolysin (α-HL) channel in planar lipid bilayers by electrophysiological characterization and molecular docking studies. Planar lipid bilayer membranes were prepared and α-HL (0.07 mg/mL) was added to the standard solution in cis compartment of the experimental chamber. All experiments were performed at room temperature using an Axopatch 200A amplifier in the voltage clamp mode. At pH 7.5, α-HL channels were usually in a high conductance ~4 nS and rarely switch to low conductance states. After the ion channel was incorporated in bilayer membrane, the furosemide was also added to the standard solution to the cis compartment. To docking studies, atomics coordinates for the α-HL heptameric channel was retrieved from PDB ID (7AHL) and the structure of furosemide was removed from the PubChem, their coordinates were built and minimized with Avogadro software. The molecular docking experiments were performed using the Dockthor online. The furosemide inhibited (P<0.05) conductance α-HL channel and it was a voltage-dependent manner. The two best docking solutions and the α-HL channel were evaluated, it was observed the connection mode with the highest affinity of interaction has a greater number of hydrogen bonding. The residues were 113 and 147 that form the remainders of the constriction α-HL channel. In conclusion, furosemide blocks ion currents in the constriction of channel caused by Staphylococcus aureus α-hemolysin.
publishDate 2022
dc.date.none.fl_str_mv 2022-12-22
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://afmo.emnuvens.com.br/afmo/article/view/192
10.56102/afmo.2022.192
url https://afmo.emnuvens.com.br/afmo/article/view/192
identifier_str_mv 10.56102/afmo.2022.192
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv https://afmo.emnuvens.com.br/afmo/article/view/192/109
dc.rights.driver.fl_str_mv https://creativecommons.org/licenses/by/4.0
info:eu-repo/semantics/openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/4.0
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Faculdade de Medicina de Olinda
publisher.none.fl_str_mv Faculdade de Medicina de Olinda
dc.source.none.fl_str_mv ANNALS OF OLINDA MEDICAL SCHOOL; Vol. 1 No. 7 (2022); 19-23
Anais da Faculdade de Medicina de Olinda; v. 1 n. 7 (2022); 19-23
2674-8487
2595-1734
reponame:Anais da Faculdade de Medicina de Olinda (Online)
instname:Faculdade de Medicina de Olinda (FMO)
instacron:FMO
instname_str Faculdade de Medicina de Olinda (FMO)
instacron_str FMO
institution FMO
reponame_str Anais da Faculdade de Medicina de Olinda (Online)
collection Anais da Faculdade de Medicina de Olinda (Online)
repository.name.fl_str_mv Anais da Faculdade de Medicina de Olinda (Online) - Faculdade de Medicina de Olinda (FMO)
repository.mail.fl_str_mv anaisfmo@fmo.edu.br
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