Tianeptine Esters Derivatives: A Study of Protein-Drug Interaction Performed by Fluorescence Quenching and Molecular Docking
Autor(a) principal: | |
---|---|
Data de Publicação: | 2019 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Journal of the Brazilian Chemical Society (Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532019001002125 |
Resumo: | The nature of binding between bovine serum albumin (BSA) and the antidepressant tianeptine and a new series of esters derivatives were studied in this paper. The interactions with BSA were investigated by UV-Vis and fluorescence spectroscopy at three different temperatures. The fluorescence quenching experiments showed that BSA interactions with tianeptine could be dynamic while to its esters a static mechanism was observed. The results showed that tianeptine quenches the intrinsic fluorescence of BSA more efficiently than its esters due to the presence of the free acid portion. The number of binding sites determined by fluorescence spectroscopy is approximately equal to 1 indicating that there is one binding site between BSA tianeptine esters, but the presence of a second interaction site for tianeptine at higher temperatures could be not ruled out. Molecular docking calculations point out a strong affinity of tianeptine and its esters to the site IIA of protein, supporting the hypothesis of a static quenching mechanism. |
id |
SBQ-2_bd7740d8ba3e7ed336b02ebd2dffec91 |
---|---|
oai_identifier_str |
oai:scielo:S0103-50532019001002125 |
network_acronym_str |
SBQ-2 |
network_name_str |
Journal of the Brazilian Chemical Society (Online) |
repository_id_str |
|
spelling |
Tianeptine Esters Derivatives: A Study of Protein-Drug Interaction Performed by Fluorescence Quenching and Molecular Dockingtianeptineprotein interactionfluorescence quenchingStern-VolmerdockingThe nature of binding between bovine serum albumin (BSA) and the antidepressant tianeptine and a new series of esters derivatives were studied in this paper. The interactions with BSA were investigated by UV-Vis and fluorescence spectroscopy at three different temperatures. The fluorescence quenching experiments showed that BSA interactions with tianeptine could be dynamic while to its esters a static mechanism was observed. The results showed that tianeptine quenches the intrinsic fluorescence of BSA more efficiently than its esters due to the presence of the free acid portion. The number of binding sites determined by fluorescence spectroscopy is approximately equal to 1 indicating that there is one binding site between BSA tianeptine esters, but the presence of a second interaction site for tianeptine at higher temperatures could be not ruled out. Molecular docking calculations point out a strong affinity of tianeptine and its esters to the site IIA of protein, supporting the hypothesis of a static quenching mechanism.Sociedade Brasileira de Química2019-10-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532019001002125Journal of the Brazilian Chemical Society v.30 n.10 2019reponame:Journal of the Brazilian Chemical Society (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.21577/0103-5053.20190090info:eu-repo/semantics/openAccessSoares,Franciela A.Ceschi,Marco A.Franceschini,Daniel B.Canto,Vanessa P. doNetz,Paulo A.Campo,Leandra F.eng2019-10-17T00:00:00Zoai:scielo:S0103-50532019001002125Revistahttp://jbcs.sbq.org.brONGhttps://old.scielo.br/oai/scielo-oai.php||office@jbcs.sbq.org.br1678-47900103-5053opendoar:2019-10-17T00:00Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)false |
dc.title.none.fl_str_mv |
Tianeptine Esters Derivatives: A Study of Protein-Drug Interaction Performed by Fluorescence Quenching and Molecular Docking |
title |
Tianeptine Esters Derivatives: A Study of Protein-Drug Interaction Performed by Fluorescence Quenching and Molecular Docking |
spellingShingle |
Tianeptine Esters Derivatives: A Study of Protein-Drug Interaction Performed by Fluorescence Quenching and Molecular Docking Soares,Franciela A. tianeptine protein interaction fluorescence quenching Stern-Volmer docking |
title_short |
Tianeptine Esters Derivatives: A Study of Protein-Drug Interaction Performed by Fluorescence Quenching and Molecular Docking |
title_full |
Tianeptine Esters Derivatives: A Study of Protein-Drug Interaction Performed by Fluorescence Quenching and Molecular Docking |
title_fullStr |
Tianeptine Esters Derivatives: A Study of Protein-Drug Interaction Performed by Fluorescence Quenching and Molecular Docking |
title_full_unstemmed |
Tianeptine Esters Derivatives: A Study of Protein-Drug Interaction Performed by Fluorescence Quenching and Molecular Docking |
title_sort |
Tianeptine Esters Derivatives: A Study of Protein-Drug Interaction Performed by Fluorescence Quenching and Molecular Docking |
author |
Soares,Franciela A. |
author_facet |
Soares,Franciela A. Ceschi,Marco A. Franceschini,Daniel B. Canto,Vanessa P. do Netz,Paulo A. Campo,Leandra F. |
author_role |
author |
author2 |
Ceschi,Marco A. Franceschini,Daniel B. Canto,Vanessa P. do Netz,Paulo A. Campo,Leandra F. |
author2_role |
author author author author author |
dc.contributor.author.fl_str_mv |
Soares,Franciela A. Ceschi,Marco A. Franceschini,Daniel B. Canto,Vanessa P. do Netz,Paulo A. Campo,Leandra F. |
dc.subject.por.fl_str_mv |
tianeptine protein interaction fluorescence quenching Stern-Volmer docking |
topic |
tianeptine protein interaction fluorescence quenching Stern-Volmer docking |
description |
The nature of binding between bovine serum albumin (BSA) and the antidepressant tianeptine and a new series of esters derivatives were studied in this paper. The interactions with BSA were investigated by UV-Vis and fluorescence spectroscopy at three different temperatures. The fluorescence quenching experiments showed that BSA interactions with tianeptine could be dynamic while to its esters a static mechanism was observed. The results showed that tianeptine quenches the intrinsic fluorescence of BSA more efficiently than its esters due to the presence of the free acid portion. The number of binding sites determined by fluorescence spectroscopy is approximately equal to 1 indicating that there is one binding site between BSA tianeptine esters, but the presence of a second interaction site for tianeptine at higher temperatures could be not ruled out. Molecular docking calculations point out a strong affinity of tianeptine and its esters to the site IIA of protein, supporting the hypothesis of a static quenching mechanism. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-10-01 |
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=S0103-50532019001002125 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532019001002125 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.21577/0103-5053.20190090 |
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 |
Sociedade Brasileira de Química |
publisher.none.fl_str_mv |
Sociedade Brasileira de Química |
dc.source.none.fl_str_mv |
Journal of the Brazilian Chemical Society v.30 n.10 2019 reponame:Journal of the Brazilian Chemical Society (Online) instname:Sociedade Brasileira de Química (SBQ) instacron:SBQ |
instname_str |
Sociedade Brasileira de Química (SBQ) |
instacron_str |
SBQ |
institution |
SBQ |
reponame_str |
Journal of the Brazilian Chemical Society (Online) |
collection |
Journal of the Brazilian Chemical Society (Online) |
repository.name.fl_str_mv |
Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ) |
repository.mail.fl_str_mv |
||office@jbcs.sbq.org.br |
_version_ |
1750318182171672576 |