Glycoprotein assay based on the optimized immittance signal of a redox tagged and lectin-based receptive interface
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Publication Date: | 2016 |
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Format: | Article |
Language: | eng |
Source: | Repositório Institucional da UNESP |
Download full: | http://dx.doi.org/10.1016/j.bios.2016.04.043 http://hdl.handle.net/11449/161546 |
Summary: | Glycoproteins play important roles in biological systems such as in process related to cell binding, signaling and disease. Consequently, novel, potentially quantitative, and rapid electroanalytical approaches capable of detecting protein binding are welcome. Herein, we introduce a methodology that is both fast and sensitive, and capable of quantification of the binding affinity in glycoprotein-lectin molecular models. The proposed methodology is based on the electrochemical impedance spectroscopy technique focused on the immittance function approach, wherein a library of analytical parameters can be computed from the raw impedance data obtained, and automatically processed in a label-free, quantifiable and very sensitive assay platform. This approach also avoids redox probe pre-doping of the analytical sample. Avoiding redox pre-doping of the analytical sample is achievable designing an appropriate redox-tagging monolayer containing lectin interface (a carbohydrate binding protein, herein ArtinM) as the bio-receptor, endowing high sensitivity of electrochemical signal when specifically detecting glycoproteins of interest (presently horseradish peroxidase, HRP, a mannose glycoprotein) as the biochemical target for ArtinM. The electroanalytical curves demonstrated that the binding affinity constant could be evaluated as equivalent for all library (immittance function) parameters, allowing optimized single frequency (or a range of frequencies) assessment with high sensitivity. In other words, binding affinity constants between ArtinM and HRP for each of the parameters in the immittance function library at given optimized frequencies were similar, independently of the parameter. Thus, the feasibility of using this immittance function approach for electroanalytical glycoarrays by accessing bio-recognition processes on a rapid (optimized) single frequency and highly multiplexable platform was demonstrated. (C) 2016 Elsevier B.V. All rights reserved. |
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Glycoprotein assay based on the optimized immittance signal of a redox tagged and lectin-based receptive interfaceElectroanalysisElectrochemical impedance spectroscopyGlycoproteinLectinImmittance functionsGlycoproteins play important roles in biological systems such as in process related to cell binding, signaling and disease. Consequently, novel, potentially quantitative, and rapid electroanalytical approaches capable of detecting protein binding are welcome. Herein, we introduce a methodology that is both fast and sensitive, and capable of quantification of the binding affinity in glycoprotein-lectin molecular models. The proposed methodology is based on the electrochemical impedance spectroscopy technique focused on the immittance function approach, wherein a library of analytical parameters can be computed from the raw impedance data obtained, and automatically processed in a label-free, quantifiable and very sensitive assay platform. This approach also avoids redox probe pre-doping of the analytical sample. Avoiding redox pre-doping of the analytical sample is achievable designing an appropriate redox-tagging monolayer containing lectin interface (a carbohydrate binding protein, herein ArtinM) as the bio-receptor, endowing high sensitivity of electrochemical signal when specifically detecting glycoproteins of interest (presently horseradish peroxidase, HRP, a mannose glycoprotein) as the biochemical target for ArtinM. The electroanalytical curves demonstrated that the binding affinity constant could be evaluated as equivalent for all library (immittance function) parameters, allowing optimized single frequency (or a range of frequencies) assessment with high sensitivity. In other words, binding affinity constants between ArtinM and HRP for each of the parameters in the immittance function library at given optimized frequencies were similar, independently of the parameter. Thus, the feasibility of using this immittance function approach for electroanalytical glycoarrays by accessing bio-recognition processes on a rapid (optimized) single frequency and highly multiplexable platform was demonstrated. (C) 2016 Elsevier B.V. All rights reserved.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Royal SocietyNewton FundSao Paulo State Univ, Univ Estadual Paulista Julio de Mesquita Filho, Inst Chem, Phys Chem Dept,Nanobion Grp, 55 Prof Francisco Degni St, BR-14800060 Sao Paulo, BrazilSao Paulo State Univ, Univ Estadual Paulista Julio de Mesquita Filho, Inst Chem, Phys Chem Dept,Nanobion Grp, 55 Prof Francisco Degni St, BR-14800060 Sao Paulo, BrazilElsevier B.V.Universidade Estadual Paulista (Unesp)Santos, Adriano [UNESP]Bueno, Paulo R. [UNESP]2018-11-26T16:33:11Z2018-11-26T16:33:11Z2016-09-15info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article368-378application/pdfhttp://dx.doi.org/10.1016/j.bios.2016.04.043Biosensors & Bioelectronics. Oxford: Elsevier Advanced Technology, v. 83, p. 368-378, 2016.0956-5663http://hdl.handle.net/11449/16154610.1016/j.bios.2016.04.043WOS:000376802300052WOS000376802300052.pdfWeb of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBiosensors & Bioelectronics2,373info:eu-repo/semantics/openAccess2024-01-01T06:18:12Zoai:repositorio.unesp.br:11449/161546Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-01-01T06:18:12Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Glycoprotein assay based on the optimized immittance signal of a redox tagged and lectin-based receptive interface |
title |
Glycoprotein assay based on the optimized immittance signal of a redox tagged and lectin-based receptive interface |
spellingShingle |
Glycoprotein assay based on the optimized immittance signal of a redox tagged and lectin-based receptive interface Santos, Adriano [UNESP] Electroanalysis Electrochemical impedance spectroscopy Glycoprotein Lectin Immittance functions |
title_short |
Glycoprotein assay based on the optimized immittance signal of a redox tagged and lectin-based receptive interface |
title_full |
Glycoprotein assay based on the optimized immittance signal of a redox tagged and lectin-based receptive interface |
title_fullStr |
Glycoprotein assay based on the optimized immittance signal of a redox tagged and lectin-based receptive interface |
title_full_unstemmed |
Glycoprotein assay based on the optimized immittance signal of a redox tagged and lectin-based receptive interface |
title_sort |
Glycoprotein assay based on the optimized immittance signal of a redox tagged and lectin-based receptive interface |
author |
Santos, Adriano [UNESP] |
author_facet |
Santos, Adriano [UNESP] Bueno, Paulo R. [UNESP] |
author_role |
author |
author2 |
Bueno, Paulo R. [UNESP] |
author2_role |
author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) |
dc.contributor.author.fl_str_mv |
Santos, Adriano [UNESP] Bueno, Paulo R. [UNESP] |
dc.subject.por.fl_str_mv |
Electroanalysis Electrochemical impedance spectroscopy Glycoprotein Lectin Immittance functions |
topic |
Electroanalysis Electrochemical impedance spectroscopy Glycoprotein Lectin Immittance functions |
description |
Glycoproteins play important roles in biological systems such as in process related to cell binding, signaling and disease. Consequently, novel, potentially quantitative, and rapid electroanalytical approaches capable of detecting protein binding are welcome. Herein, we introduce a methodology that is both fast and sensitive, and capable of quantification of the binding affinity in glycoprotein-lectin molecular models. The proposed methodology is based on the electrochemical impedance spectroscopy technique focused on the immittance function approach, wherein a library of analytical parameters can be computed from the raw impedance data obtained, and automatically processed in a label-free, quantifiable and very sensitive assay platform. This approach also avoids redox probe pre-doping of the analytical sample. Avoiding redox pre-doping of the analytical sample is achievable designing an appropriate redox-tagging monolayer containing lectin interface (a carbohydrate binding protein, herein ArtinM) as the bio-receptor, endowing high sensitivity of electrochemical signal when specifically detecting glycoproteins of interest (presently horseradish peroxidase, HRP, a mannose glycoprotein) as the biochemical target for ArtinM. The electroanalytical curves demonstrated that the binding affinity constant could be evaluated as equivalent for all library (immittance function) parameters, allowing optimized single frequency (or a range of frequencies) assessment with high sensitivity. In other words, binding affinity constants between ArtinM and HRP for each of the parameters in the immittance function library at given optimized frequencies were similar, independently of the parameter. Thus, the feasibility of using this immittance function approach for electroanalytical glycoarrays by accessing bio-recognition processes on a rapid (optimized) single frequency and highly multiplexable platform was demonstrated. (C) 2016 Elsevier B.V. All rights reserved. |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016-09-15 2018-11-26T16:33:11Z 2018-11-26T16:33:11Z |
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/10.1016/j.bios.2016.04.043 Biosensors & Bioelectronics. Oxford: Elsevier Advanced Technology, v. 83, p. 368-378, 2016. 0956-5663 http://hdl.handle.net/11449/161546 10.1016/j.bios.2016.04.043 WOS:000376802300052 WOS000376802300052.pdf |
url |
http://dx.doi.org/10.1016/j.bios.2016.04.043 http://hdl.handle.net/11449/161546 |
identifier_str_mv |
Biosensors & Bioelectronics. Oxford: Elsevier Advanced Technology, v. 83, p. 368-378, 2016. 0956-5663 10.1016/j.bios.2016.04.043 WOS:000376802300052 WOS000376802300052.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Biosensors & Bioelectronics 2,373 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
368-378 application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier B.V. |
publisher.none.fl_str_mv |
Elsevier B.V. |
dc.source.none.fl_str_mv |
Web of Science 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 |
|
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1799965477270716416 |