Furosemide blocks the anion channel caused by Staphylococcus aureus α-hemolysin
Autor(a) principal: | |
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Data de Publicação: | 2022 |
Outros Autores: | , , , , , |
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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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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1796798260557381632 |