INTERAÇÕES COMPETITIVAS DE COMPLEXOS DE RUTÊNIO CONTENDO DIMETILSULFÓXIDO E LIGANTES N-HETEROCÍCLICOS COM ALBUMINA DE SORO HUMANO
Autor(a) principal: | |
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Data de Publicação: | 2020 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | por |
Título da fonte: | Química Nova (Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422020000300261 |
Resumo: | Two ruthenium complexes of the type [RuCl(dmso)(L)2]Cl {L = 4,4’-dimethyl-2,2’-bipyridine (dmbpy); 4,4’-dinonyl-2,2’-bipyridine (dnbpy)} have been synthesized and characterized by elemental analysis, 1H NMR, FTIR, electronic spectra, and molar conductivity. The IR spectral studies revealed that the DMSO molecule is S-bound ( νSO= 1100 cm-1; 1079 cm-1). For complexes, MLCT bands were observed around 390 nm and 440 nm. The measurements of conductivity revealed the presence of 1:1 electrolyte. Interactions of ruthenium complexes with human serum albumin were examined by fluorescence spectroscopy. The results revealed a combined quenching mechanism of HSA fluorescence by [RuCl(dmso)(dmbpy)2]Cl, with binding constant of 5.82 ± 0.08 x 105 mol-1 L (297 K), 5.29 ± 0.06 x 105 mol-1 L (303 K), and 4.68 ± 0.06 x 105 mol-1 L (313 K), whereas the [RuCl(dmso)(dnbpy)2]Cl caused static quenching predominantly, with binding constant of 9.87 ± 0.05 x 105 mol-1 L (297 K), 3.41 ± 0.04 x 105 mol-1 L (303 K), and 0.89 ± 0.05 x 105 mol-1 L (313 K). The binding process occurred spontaneously and was mainly driven by enthalpy, as evidenced by thermodynamic parameters. Site marker competitive experiment showed that ruthenium complexes bind to the warfarin binding site in subdomain IIA of HSA. |
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Química Nova (Online) |
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INTERAÇÕES COMPETITIVAS DE COMPLEXOS DE RUTÊNIO CONTENDO DIMETILSULFÓXIDO E LIGANTES N-HETEROCÍCLICOS COM ALBUMINA DE SORO HUMANOfluorescencequenchingbinding constantsite probesvan der Waals forcesTwo ruthenium complexes of the type [RuCl(dmso)(L)2]Cl {L = 4,4’-dimethyl-2,2’-bipyridine (dmbpy); 4,4’-dinonyl-2,2’-bipyridine (dnbpy)} have been synthesized and characterized by elemental analysis, 1H NMR, FTIR, electronic spectra, and molar conductivity. The IR spectral studies revealed that the DMSO molecule is S-bound ( νSO= 1100 cm-1; 1079 cm-1). For complexes, MLCT bands were observed around 390 nm and 440 nm. The measurements of conductivity revealed the presence of 1:1 electrolyte. Interactions of ruthenium complexes with human serum albumin were examined by fluorescence spectroscopy. The results revealed a combined quenching mechanism of HSA fluorescence by [RuCl(dmso)(dmbpy)2]Cl, with binding constant of 5.82 ± 0.08 x 105 mol-1 L (297 K), 5.29 ± 0.06 x 105 mol-1 L (303 K), and 4.68 ± 0.06 x 105 mol-1 L (313 K), whereas the [RuCl(dmso)(dnbpy)2]Cl caused static quenching predominantly, with binding constant of 9.87 ± 0.05 x 105 mol-1 L (297 K), 3.41 ± 0.04 x 105 mol-1 L (303 K), and 0.89 ± 0.05 x 105 mol-1 L (313 K). The binding process occurred spontaneously and was mainly driven by enthalpy, as evidenced by thermodynamic parameters. Site marker competitive experiment showed that ruthenium complexes bind to the warfarin binding site in subdomain IIA of HSA.Sociedade Brasileira de Química2020-03-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422020000300261Química Nova v.43 n.3 2020reponame:Química Nova (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.21577/0100-4042.20170488info:eu-repo/semantics/openAccessB. Neto,Guilherme LuizBaptista,Eduardo Alexandre M.Becca,Gabriel Hideki S.Nakatani,Helena S.Souza,Vagner R. depor2020-05-28T00:00:00Zoai:scielo:S0100-40422020000300261Revistahttps://www.scielo.br/j/qn/ONGhttps://old.scielo.br/oai/scielo-oai.phpquimicanova@sbq.org.br1678-70640100-4042opendoar:2020-05-28T00:00Química Nova (Online) - Sociedade Brasileira de Química (SBQ)false |
dc.title.none.fl_str_mv |
INTERAÇÕES COMPETITIVAS DE COMPLEXOS DE RUTÊNIO CONTENDO DIMETILSULFÓXIDO E LIGANTES N-HETEROCÍCLICOS COM ALBUMINA DE SORO HUMANO |
title |
INTERAÇÕES COMPETITIVAS DE COMPLEXOS DE RUTÊNIO CONTENDO DIMETILSULFÓXIDO E LIGANTES N-HETEROCÍCLICOS COM ALBUMINA DE SORO HUMANO |
spellingShingle |
INTERAÇÕES COMPETITIVAS DE COMPLEXOS DE RUTÊNIO CONTENDO DIMETILSULFÓXIDO E LIGANTES N-HETEROCÍCLICOS COM ALBUMINA DE SORO HUMANO B. Neto,Guilherme Luiz fluorescence quenching binding constant site probes van der Waals forces |
title_short |
INTERAÇÕES COMPETITIVAS DE COMPLEXOS DE RUTÊNIO CONTENDO DIMETILSULFÓXIDO E LIGANTES N-HETEROCÍCLICOS COM ALBUMINA DE SORO HUMANO |
title_full |
INTERAÇÕES COMPETITIVAS DE COMPLEXOS DE RUTÊNIO CONTENDO DIMETILSULFÓXIDO E LIGANTES N-HETEROCÍCLICOS COM ALBUMINA DE SORO HUMANO |
title_fullStr |
INTERAÇÕES COMPETITIVAS DE COMPLEXOS DE RUTÊNIO CONTENDO DIMETILSULFÓXIDO E LIGANTES N-HETEROCÍCLICOS COM ALBUMINA DE SORO HUMANO |
title_full_unstemmed |
INTERAÇÕES COMPETITIVAS DE COMPLEXOS DE RUTÊNIO CONTENDO DIMETILSULFÓXIDO E LIGANTES N-HETEROCÍCLICOS COM ALBUMINA DE SORO HUMANO |
title_sort |
INTERAÇÕES COMPETITIVAS DE COMPLEXOS DE RUTÊNIO CONTENDO DIMETILSULFÓXIDO E LIGANTES N-HETEROCÍCLICOS COM ALBUMINA DE SORO HUMANO |
author |
B. Neto,Guilherme Luiz |
author_facet |
B. Neto,Guilherme Luiz Baptista,Eduardo Alexandre M. Becca,Gabriel Hideki S. Nakatani,Helena S. Souza,Vagner R. de |
author_role |
author |
author2 |
Baptista,Eduardo Alexandre M. Becca,Gabriel Hideki S. Nakatani,Helena S. Souza,Vagner R. de |
author2_role |
author author author author |
dc.contributor.author.fl_str_mv |
B. Neto,Guilherme Luiz Baptista,Eduardo Alexandre M. Becca,Gabriel Hideki S. Nakatani,Helena S. Souza,Vagner R. de |
dc.subject.por.fl_str_mv |
fluorescence quenching binding constant site probes van der Waals forces |
topic |
fluorescence quenching binding constant site probes van der Waals forces |
description |
Two ruthenium complexes of the type [RuCl(dmso)(L)2]Cl {L = 4,4’-dimethyl-2,2’-bipyridine (dmbpy); 4,4’-dinonyl-2,2’-bipyridine (dnbpy)} have been synthesized and characterized by elemental analysis, 1H NMR, FTIR, electronic spectra, and molar conductivity. The IR spectral studies revealed that the DMSO molecule is S-bound ( νSO= 1100 cm-1; 1079 cm-1). For complexes, MLCT bands were observed around 390 nm and 440 nm. The measurements of conductivity revealed the presence of 1:1 electrolyte. Interactions of ruthenium complexes with human serum albumin were examined by fluorescence spectroscopy. The results revealed a combined quenching mechanism of HSA fluorescence by [RuCl(dmso)(dmbpy)2]Cl, with binding constant of 5.82 ± 0.08 x 105 mol-1 L (297 K), 5.29 ± 0.06 x 105 mol-1 L (303 K), and 4.68 ± 0.06 x 105 mol-1 L (313 K), whereas the [RuCl(dmso)(dnbpy)2]Cl caused static quenching predominantly, with binding constant of 9.87 ± 0.05 x 105 mol-1 L (297 K), 3.41 ± 0.04 x 105 mol-1 L (303 K), and 0.89 ± 0.05 x 105 mol-1 L (313 K). The binding process occurred spontaneously and was mainly driven by enthalpy, as evidenced by thermodynamic parameters. Site marker competitive experiment showed that ruthenium complexes bind to the warfarin binding site in subdomain IIA of HSA. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-03-01 |
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=S0100-40422020000300261 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422020000300261 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.relation.none.fl_str_mv |
10.21577/0100-4042.20170488 |
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 |
Química Nova v.43 n.3 2020 reponame:Química Nova (Online) instname:Sociedade Brasileira de Química (SBQ) instacron:SBQ |
instname_str |
Sociedade Brasileira de Química (SBQ) |
instacron_str |
SBQ |
institution |
SBQ |
reponame_str |
Química Nova (Online) |
collection |
Química Nova (Online) |
repository.name.fl_str_mv |
Química Nova (Online) - Sociedade Brasileira de Química (SBQ) |
repository.mail.fl_str_mv |
quimicanova@sbq.org.br |
_version_ |
1750318120137916416 |