Kinetic studies of HRP adsorption on ds-DNA immobilized on gold electrode surface by EIS and SPR
Autor(a) principal: | |
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Data de Publicação: | 2010 |
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=S0103-50532010000900008 |
Resumo: | This paper describes the construction of a multicomponent film via layer-by-layer (LbL) method and the kinetic analysis of the interaction between horseradish peroxidase (HRP) enzyme on calf thymus double-stranded DNA layer on a modified gold surface. Surface plasmon resonance (SPR) and electrochemical impedance spectroscopy (EIS) are used to characterize the successful construction of the film on the gold surface. Surface plasmon resonance provided essential information for the study and characterization of protein and nucleic acid interaction and this method is label-free and monitors the interactions in real time. The kinetic studies determined by SPR of the horseradish peroxidase film formation on ds-DNA layer showed values of 24.7 L mol-1 s-1 and 1.2×10-3 s-1 for k a and k d, respectively. The Gibbs free energy obtained for the system was -23.1 kJ mol-1. The results obtained show that the interaction of the enzymes molecules on ds-DNA is kinetically and thermodynamically favourable and the interaction among the layers probably occurs mainly by attraction of opposite charges. |
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Journal of the Brazilian Chemical Society (Online) |
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Kinetic studies of HRP adsorption on ds-DNA immobilized on gold electrode surface by EIS and SPRSPREISkinetic adsorptionDNAHRPprotein-DNA interactionThis paper describes the construction of a multicomponent film via layer-by-layer (LbL) method and the kinetic analysis of the interaction between horseradish peroxidase (HRP) enzyme on calf thymus double-stranded DNA layer on a modified gold surface. Surface plasmon resonance (SPR) and electrochemical impedance spectroscopy (EIS) are used to characterize the successful construction of the film on the gold surface. Surface plasmon resonance provided essential information for the study and characterization of protein and nucleic acid interaction and this method is label-free and monitors the interactions in real time. The kinetic studies determined by SPR of the horseradish peroxidase film formation on ds-DNA layer showed values of 24.7 L mol-1 s-1 and 1.2×10-3 s-1 for k a and k d, respectively. The Gibbs free energy obtained for the system was -23.1 kJ mol-1. The results obtained show that the interaction of the enzymes molecules on ds-DNA is kinetically and thermodynamically favourable and the interaction among the layers probably occurs mainly by attraction of opposite charges.Sociedade Brasileira de Química2010-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532010000900008Journal of the Brazilian Chemical Society v.21 n.9 2010reponame:Journal of the Brazilian Chemical Society (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.1590/S0103-50532010000900008info:eu-repo/semantics/openAccessFerreira,Danielle C. MMendes,Renata KKubota,Lauro Teng2010-09-13T00:00:00Zoai:scielo:S0103-50532010000900008Revistahttp://jbcs.sbq.org.brONGhttps://old.scielo.br/oai/scielo-oai.php||office@jbcs.sbq.org.br1678-47900103-5053opendoar:2010-09-13T00:00Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)false |
dc.title.none.fl_str_mv |
Kinetic studies of HRP adsorption on ds-DNA immobilized on gold electrode surface by EIS and SPR |
title |
Kinetic studies of HRP adsorption on ds-DNA immobilized on gold electrode surface by EIS and SPR |
spellingShingle |
Kinetic studies of HRP adsorption on ds-DNA immobilized on gold electrode surface by EIS and SPR Ferreira,Danielle C. M SPR EIS kinetic adsorption DNA HRP protein-DNA interaction |
title_short |
Kinetic studies of HRP adsorption on ds-DNA immobilized on gold electrode surface by EIS and SPR |
title_full |
Kinetic studies of HRP adsorption on ds-DNA immobilized on gold electrode surface by EIS and SPR |
title_fullStr |
Kinetic studies of HRP adsorption on ds-DNA immobilized on gold electrode surface by EIS and SPR |
title_full_unstemmed |
Kinetic studies of HRP adsorption on ds-DNA immobilized on gold electrode surface by EIS and SPR |
title_sort |
Kinetic studies of HRP adsorption on ds-DNA immobilized on gold electrode surface by EIS and SPR |
author |
Ferreira,Danielle C. M |
author_facet |
Ferreira,Danielle C. M Mendes,Renata K Kubota,Lauro T |
author_role |
author |
author2 |
Mendes,Renata K Kubota,Lauro T |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
Ferreira,Danielle C. M Mendes,Renata K Kubota,Lauro T |
dc.subject.por.fl_str_mv |
SPR EIS kinetic adsorption DNA HRP protein-DNA interaction |
topic |
SPR EIS kinetic adsorption DNA HRP protein-DNA interaction |
description |
This paper describes the construction of a multicomponent film via layer-by-layer (LbL) method and the kinetic analysis of the interaction between horseradish peroxidase (HRP) enzyme on calf thymus double-stranded DNA layer on a modified gold surface. Surface plasmon resonance (SPR) and electrochemical impedance spectroscopy (EIS) are used to characterize the successful construction of the film on the gold surface. Surface plasmon resonance provided essential information for the study and characterization of protein and nucleic acid interaction and this method is label-free and monitors the interactions in real time. The kinetic studies determined by SPR of the horseradish peroxidase film formation on ds-DNA layer showed values of 24.7 L mol-1 s-1 and 1.2×10-3 s-1 for k a and k d, respectively. The Gibbs free energy obtained for the system was -23.1 kJ mol-1. The results obtained show that the interaction of the enzymes molecules on ds-DNA is kinetically and thermodynamically favourable and the interaction among the layers probably occurs mainly by attraction of opposite charges. |
publishDate |
2010 |
dc.date.none.fl_str_mv |
2010-01-01 |
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=S0103-50532010000900008 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532010000900008 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0103-50532010000900008 |
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.21 n.9 2010 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_ |
1750318171409088512 |