Biorecognition of hydrogen peroxide using a novel electrochemical platform designed with Glossoscolex paulistus giant hemoglobin
Autor(a) principal: | |
---|---|
Data de Publicação: | 2022 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1007/s00216-022-04020-8 http://hdl.handle.net/11449/230650 |
Resumo: | The giant extracellular hemoglobin of the annelid Glossoscolex paulistus (HbGp; 3.6 MDa) is a valuable and underexplored supramolecular hemoprotein system for the biorecognition of reactive oxygen species. In this work, an efficient and simple electrochemical platform was designed for analyzing H2O2, using HbGp covalently immobilized on Nafion®-modified glassy carbon electrode, named as HbGp/Nafion/GCE. Voltammetric and spectroscopic studies revealed the importance of prior modification of the electrodic support with the conducting polymer to obtain satisfactory hemoglobin electroactivity, as well as a biocompatible microenvironment for its immobilization. In terms of biological activity, it was observed a greater reactivity of the biomolecule in acidic medium, enabling the detection of the analyte by a quasi-reversible mechanism, whose kinetics was limited by analyte diffusion. In the presence of H2O2, the native structure of hemoglobin (oxy-HbGp (Fe2+)) oxidizes to ferryl-HbGp (Fe4+) and this redox reaction can be monitored on HbGp/Nafion/GCE with a detection limit of 8.5 × 10‒7 mol L-1. In addition to high sensitivity, the electrochemical biosensor also provided reproducible, consistent, and accurate measurements. The electroanalytical method showed an appropriate performance to quantify different levels of H2O2 in milk samples, proving the potential of HbGp/Nafion/GCE for this purpose. Graphical abstract: [Figure not available: see fulltext.] |
id |
UNSP_c8fcbd0d76785c67d6edc1f511c4e2b7 |
---|---|
oai_identifier_str |
oai:repositorio.unesp.br:11449/230650 |
network_acronym_str |
UNSP |
network_name_str |
Repositório Institucional da UNESP |
repository_id_str |
2946 |
spelling |
Biorecognition of hydrogen peroxide using a novel electrochemical platform designed with Glossoscolex paulistus giant hemoglobinElectroanalysisElectrochemical biosensorsGiant hemoglobinsGlossoscolex paulistusH2O2The giant extracellular hemoglobin of the annelid Glossoscolex paulistus (HbGp; 3.6 MDa) is a valuable and underexplored supramolecular hemoprotein system for the biorecognition of reactive oxygen species. In this work, an efficient and simple electrochemical platform was designed for analyzing H2O2, using HbGp covalently immobilized on Nafion®-modified glassy carbon electrode, named as HbGp/Nafion/GCE. Voltammetric and spectroscopic studies revealed the importance of prior modification of the electrodic support with the conducting polymer to obtain satisfactory hemoglobin electroactivity, as well as a biocompatible microenvironment for its immobilization. In terms of biological activity, it was observed a greater reactivity of the biomolecule in acidic medium, enabling the detection of the analyte by a quasi-reversible mechanism, whose kinetics was limited by analyte diffusion. In the presence of H2O2, the native structure of hemoglobin (oxy-HbGp (Fe2+)) oxidizes to ferryl-HbGp (Fe4+) and this redox reaction can be monitored on HbGp/Nafion/GCE with a detection limit of 8.5 × 10‒7 mol L-1. In addition to high sensitivity, the electrochemical biosensor also provided reproducible, consistent, and accurate measurements. The electroanalytical method showed an appropriate performance to quantify different levels of H2O2 in milk samples, proving the potential of HbGp/Nafion/GCE for this purpose. Graphical abstract: [Figure not available: see fulltext.]Departamento de Química Universidade Federal de São Carlos, Rod. Washington Luís km 235, SPUniversidade Federal Do Sul E Sudeste Do Pará, Folha 17, Quadra 04, Lote Especial, PACentro de Ciência E Tecnologia Universidade Federal Do Cariri, Avenida Tenente Raimundo Rocha, 1639, Cidade Universitária, CEUniversidade Estadual Paulista Instituto Avançado de Estudos Do Mar, Campus de Registro, Av. Nelson Brihi Badur, 430 - Vila Tupy, SPUniversidade Estadual Paulista Instituto Avançado de Estudos Do Mar, Campus de Registro, Av. Nelson Brihi Badur, 430 - Vila Tupy, SPUniversidade Federal de São Carlos (UFSCar)Universidade Federal Do Sul E Sudeste Do ParáUniversidade Federal Do CaririUniversidade Estadual Paulista (UNESP)Nascimento, Evair D.Abrantes-Coutinho, Vanessa E.Oliveira, Thiago M. B. F.Santiago, Patrícia S. [UNESP]Carvalho, Francisco A. O.2022-04-29T08:41:22Z2022-04-29T08:41:22Z2022-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1007/s00216-022-04020-8Analytical and Bioanalytical Chemistry.1618-26501618-2642http://hdl.handle.net/11449/23065010.1007/s00216-022-04020-82-s2.0-85127288731Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengAnalytical and Bioanalytical Chemistryinfo:eu-repo/semantics/openAccess2024-05-03T13:20:09Zoai:repositorio.unesp.br:11449/230650Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T18:38:12.175302Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Biorecognition of hydrogen peroxide using a novel electrochemical platform designed with Glossoscolex paulistus giant hemoglobin |
title |
Biorecognition of hydrogen peroxide using a novel electrochemical platform designed with Glossoscolex paulistus giant hemoglobin |
spellingShingle |
Biorecognition of hydrogen peroxide using a novel electrochemical platform designed with Glossoscolex paulistus giant hemoglobin Nascimento, Evair D. Electroanalysis Electrochemical biosensors Giant hemoglobins Glossoscolex paulistus H2O2 |
title_short |
Biorecognition of hydrogen peroxide using a novel electrochemical platform designed with Glossoscolex paulistus giant hemoglobin |
title_full |
Biorecognition of hydrogen peroxide using a novel electrochemical platform designed with Glossoscolex paulistus giant hemoglobin |
title_fullStr |
Biorecognition of hydrogen peroxide using a novel electrochemical platform designed with Glossoscolex paulistus giant hemoglobin |
title_full_unstemmed |
Biorecognition of hydrogen peroxide using a novel electrochemical platform designed with Glossoscolex paulistus giant hemoglobin |
title_sort |
Biorecognition of hydrogen peroxide using a novel electrochemical platform designed with Glossoscolex paulistus giant hemoglobin |
author |
Nascimento, Evair D. |
author_facet |
Nascimento, Evair D. Abrantes-Coutinho, Vanessa E. Oliveira, Thiago M. B. F. Santiago, Patrícia S. [UNESP] Carvalho, Francisco A. O. |
author_role |
author |
author2 |
Abrantes-Coutinho, Vanessa E. Oliveira, Thiago M. B. F. Santiago, Patrícia S. [UNESP] Carvalho, Francisco A. O. |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Universidade Federal de São Carlos (UFSCar) Universidade Federal Do Sul E Sudeste Do Pará Universidade Federal Do Cariri Universidade Estadual Paulista (UNESP) |
dc.contributor.author.fl_str_mv |
Nascimento, Evair D. Abrantes-Coutinho, Vanessa E. Oliveira, Thiago M. B. F. Santiago, Patrícia S. [UNESP] Carvalho, Francisco A. O. |
dc.subject.por.fl_str_mv |
Electroanalysis Electrochemical biosensors Giant hemoglobins Glossoscolex paulistus H2O2 |
topic |
Electroanalysis Electrochemical biosensors Giant hemoglobins Glossoscolex paulistus H2O2 |
description |
The giant extracellular hemoglobin of the annelid Glossoscolex paulistus (HbGp; 3.6 MDa) is a valuable and underexplored supramolecular hemoprotein system for the biorecognition of reactive oxygen species. In this work, an efficient and simple electrochemical platform was designed for analyzing H2O2, using HbGp covalently immobilized on Nafion®-modified glassy carbon electrode, named as HbGp/Nafion/GCE. Voltammetric and spectroscopic studies revealed the importance of prior modification of the electrodic support with the conducting polymer to obtain satisfactory hemoglobin electroactivity, as well as a biocompatible microenvironment for its immobilization. In terms of biological activity, it was observed a greater reactivity of the biomolecule in acidic medium, enabling the detection of the analyte by a quasi-reversible mechanism, whose kinetics was limited by analyte diffusion. In the presence of H2O2, the native structure of hemoglobin (oxy-HbGp (Fe2+)) oxidizes to ferryl-HbGp (Fe4+) and this redox reaction can be monitored on HbGp/Nafion/GCE with a detection limit of 8.5 × 10‒7 mol L-1. In addition to high sensitivity, the electrochemical biosensor also provided reproducible, consistent, and accurate measurements. The electroanalytical method showed an appropriate performance to quantify different levels of H2O2 in milk samples, proving the potential of HbGp/Nafion/GCE for this purpose. Graphical abstract: [Figure not available: see fulltext.] |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022-04-29T08:41:22Z 2022-04-29T08:41:22Z 2022-01-01 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1007/s00216-022-04020-8 Analytical and Bioanalytical Chemistry. 1618-2650 1618-2642 http://hdl.handle.net/11449/230650 10.1007/s00216-022-04020-8 2-s2.0-85127288731 |
url |
http://dx.doi.org/10.1007/s00216-022-04020-8 http://hdl.handle.net/11449/230650 |
identifier_str_mv |
Analytical and Bioanalytical Chemistry. 1618-2650 1618-2642 10.1007/s00216-022-04020-8 2-s2.0-85127288731 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Analytical and Bioanalytical Chemistry |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808128957760929792 |