Rhenium(I) Polypyridine Complexes as Luminescence-Based Sensors for the BSA Protein
Autor(a) principal: | |
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Data de Publicação: | 2016 |
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=S0103-50532016000100179 |
Resumo: | The binding interaction of rhenium(I) complexes fac-[Re(CO)3(NN)(py)]+, py = pyridine and NN = 1,10-phenanthroline (phen), 4,7-diphenyl-1,10-phenanthroline (ph2phen) or 4,7-dichloro-1,10-phenanthroline (Cl2phen), and bovine serum albumin (BSA) was investigated at physiological pH using emission intensity variation and circular dichroism (CD) spectroscopy. The photophysical investigations showed that in the presence of BSA, the metal-to-ligand-charge transfer (3MLCT) emission of the rhenium(I) complexes was quenched due to entrapment of the complex within the protein environment. Additionally, high Stern-Volmer (KSV) and binding (Kb) constants were determined from luminescence data, revealing the occurrence of a strong interaction and/or association. The differences in KSV values can be tentatively associated with an electron-withdrawing constant (σ) defined by Hammett equation. The CD results showed that the extent of α-helicity of the BSA decreased upon the addition of rhenium complexes, which provided further support for the interaction of rhenium(I) complexes and the protein. |
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Rhenium(I) Polypyridine Complexes as Luminescence-Based Sensors for the BSA Proteinrhenium(I) polypyridine complexesBSAluminescence-based sensorThe binding interaction of rhenium(I) complexes fac-[Re(CO)3(NN)(py)]+, py = pyridine and NN = 1,10-phenanthroline (phen), 4,7-diphenyl-1,10-phenanthroline (ph2phen) or 4,7-dichloro-1,10-phenanthroline (Cl2phen), and bovine serum albumin (BSA) was investigated at physiological pH using emission intensity variation and circular dichroism (CD) spectroscopy. The photophysical investigations showed that in the presence of BSA, the metal-to-ligand-charge transfer (3MLCT) emission of the rhenium(I) complexes was quenched due to entrapment of the complex within the protein environment. Additionally, high Stern-Volmer (KSV) and binding (Kb) constants were determined from luminescence data, revealing the occurrence of a strong interaction and/or association. The differences in KSV values can be tentatively associated with an electron-withdrawing constant (σ) defined by Hammett equation. The CD results showed that the extent of α-helicity of the BSA decreased upon the addition of rhenium complexes, which provided further support for the interaction of rhenium(I) complexes and the protein.Sociedade Brasileira de Química2016-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532016000100179Journal of the Brazilian Chemical Society v.27 n.1 2016reponame:Journal of the Brazilian Chemical Society (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.5935/0103-5053.20150268info:eu-repo/semantics/openAccessFrin,Karina P. M.Nascimento,Verônica M.eng2016-03-09T00:00:00Zoai:scielo:S0103-50532016000100179Revistahttp://jbcs.sbq.org.brONGhttps://old.scielo.br/oai/scielo-oai.php||office@jbcs.sbq.org.br1678-47900103-5053opendoar:2016-03-09T00:00Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)false |
dc.title.none.fl_str_mv |
Rhenium(I) Polypyridine Complexes as Luminescence-Based Sensors for the BSA Protein |
title |
Rhenium(I) Polypyridine Complexes as Luminescence-Based Sensors for the BSA Protein |
spellingShingle |
Rhenium(I) Polypyridine Complexes as Luminescence-Based Sensors for the BSA Protein Frin,Karina P. M. rhenium(I) polypyridine complexes BSA luminescence-based sensor |
title_short |
Rhenium(I) Polypyridine Complexes as Luminescence-Based Sensors for the BSA Protein |
title_full |
Rhenium(I) Polypyridine Complexes as Luminescence-Based Sensors for the BSA Protein |
title_fullStr |
Rhenium(I) Polypyridine Complexes as Luminescence-Based Sensors for the BSA Protein |
title_full_unstemmed |
Rhenium(I) Polypyridine Complexes as Luminescence-Based Sensors for the BSA Protein |
title_sort |
Rhenium(I) Polypyridine Complexes as Luminescence-Based Sensors for the BSA Protein |
author |
Frin,Karina P. M. |
author_facet |
Frin,Karina P. M. Nascimento,Verônica M. |
author_role |
author |
author2 |
Nascimento,Verônica M. |
author2_role |
author |
dc.contributor.author.fl_str_mv |
Frin,Karina P. M. Nascimento,Verônica M. |
dc.subject.por.fl_str_mv |
rhenium(I) polypyridine complexes BSA luminescence-based sensor |
topic |
rhenium(I) polypyridine complexes BSA luminescence-based sensor |
description |
The binding interaction of rhenium(I) complexes fac-[Re(CO)3(NN)(py)]+, py = pyridine and NN = 1,10-phenanthroline (phen), 4,7-diphenyl-1,10-phenanthroline (ph2phen) or 4,7-dichloro-1,10-phenanthroline (Cl2phen), and bovine serum albumin (BSA) was investigated at physiological pH using emission intensity variation and circular dichroism (CD) spectroscopy. The photophysical investigations showed that in the presence of BSA, the metal-to-ligand-charge transfer (3MLCT) emission of the rhenium(I) complexes was quenched due to entrapment of the complex within the protein environment. Additionally, high Stern-Volmer (KSV) and binding (Kb) constants were determined from luminescence data, revealing the occurrence of a strong interaction and/or association. The differences in KSV values can be tentatively associated with an electron-withdrawing constant (σ) defined by Hammett equation. The CD results showed that the extent of α-helicity of the BSA decreased upon the addition of rhenium complexes, which provided further support for the interaction of rhenium(I) complexes and the protein. |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016-01-01 |
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=S0103-50532016000100179 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532016000100179 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.5935/0103-5053.20150268 |
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.27 n.1 2016 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_ |
1750318177917599744 |