Glycoprotein assay based on the optimized immittance signal of a redox tagged and lectin-based receptive interface

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dc.contributor.authorSantos, Adriano [UNESP]
dc.contributor.authorBueno, Paulo R. [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2018-11-26T16:33:11Z
dc.date.available2018-11-26T16:33:11Z
dc.date.issued2016-09-15
dc.description.abstractGlycoproteins 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.en
dc.description.affiliationSao 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, Brazil
dc.description.affiliationUnespSao 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, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipRoyal Society
dc.description.sponsorshipNewton Fund
dc.format.extent368-378
dc.identifierhttp://dx.doi.org/10.1016/j.bios.2016.04.043
dc.identifier.citationBiosensors & Bioelectronics. Oxford: Elsevier Advanced Technology, v. 83, p. 368-378, 2016.
dc.identifier.doi10.1016/j.bios.2016.04.043
dc.identifier.fileWOS000376802300052.pdf
dc.identifier.issn0956-5663
dc.identifier.urihttp://hdl.handle.net/11449/161546
dc.identifier.wosWOS:000376802300052
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiosensors & Bioelectronics
dc.relation.ispartofsjr2,373
dc.rights.accessRightsAcesso aberto
dc.sourceWeb of Science
dc.subjectElectroanalysis
dc.subjectElectrochemical impedance spectroscopy
dc.subjectGlycoprotein
dc.subjectLectin
dc.subjectImmittance functions
dc.titleGlycoprotein assay based on the optimized immittance signal of a redox tagged and lectin-based receptive interfaceen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.

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