A new assay design for clinical diagnostics based on alternative recognition elements
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| Title: | A new assay design for clinical diagnostics based on alternative recognition elements |
|---|---|
| Authors: | Albrecht, Christiane1 christiane.albrecht@uni-tuebingen.de, Fechner, Peter1, Honcharenko, Dmytro2, Baltzer, Lars2, Gauglitz, Günter1 |
| Source: | Biosensors & Bioelectronics. Jun2010, Vol. 25 Issue 10, p2302-2308. 7p. |
| Subjects: | Biological assay, Polypeptides, Spectrum analysis, Chemical kinetics, Immunoassay, Biosensors, Immobilized antibodies, Molecular recognition |
| Abstract: | Abstract: Herein, we present a new sandwich assay design containing a high affinity polypeptide scaffold as immobilized capture element and an antibody for detection. These polypeptide scaffolds provide a good affinity towards one antigen and can be linked to biosensor surfaces without affecting their binding capabilities. Furthermore, the small peptides are very stable, which allows for regenerating the surface several hundreds of times and thus for reuse of the biosensor. Moreover, these receptors can be synthesized with different affinities towards one antigen, which has been proven by characterizing them using a label-free detection method RIfS (reflectometric interference spectroscopy) for collecting kinetic data. Polypeptide scaffolds with different affinities have been chosen and characterized. Upon these results, sandwich-type assays have been set-up using a fluorescently labelled antibody as detection element. Thereby could be shown, that the working range of the assay can be shifted according to the affinity of the used capturing polypeptide scaffold. The scaffolds with a higher affinity towards the antigen can detect lower concentration, and in contrary, scaffolds with lower affinities can detect higher concentrations. In consequence, using this new sandwich-type assay, we avoid the complex procedure to immobilize antibodies in correct orientation, but simultaneously keep this well-known recognition element in the assay for detection. Furthermore, in addition to all the acknowledged properties of immunoassays, we add the possibility of tuning the working range of assays in distinct manner according to request. [Copyright &y& Elsevier] |
| Copyright of Biosensors & Bioelectronics is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 50391671 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: A new assay design for clinical diagnostics based on alternative recognition elements – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Albrecht%2C+Christiane%22">Albrecht, Christiane</searchLink><relatesTo>1</relatesTo><i> christiane.albrecht@uni-tuebingen.de</i><br /><searchLink fieldCode="AR" term="%22Fechner%2C+Peter%22">Fechner, Peter</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Honcharenko%2C+Dmytro%22">Honcharenko, Dmytro</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Baltzer%2C+Lars%22">Baltzer, Lars</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Gauglitz%2C+Günter%22">Gauglitz, Günter</searchLink><relatesTo>1</relatesTo> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Biosensors+%26+Bioelectronics%22">Biosensors & Bioelectronics</searchLink>. Jun2010, Vol. 25 Issue 10, p2302-2308. 7p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Biological+assay%22">Biological assay</searchLink><br /><searchLink fieldCode="DE" term="%22Polypeptides%22">Polypeptides</searchLink><br /><searchLink fieldCode="DE" term="%22Spectrum+analysis%22">Spectrum analysis</searchLink><br /><searchLink fieldCode="DE" term="%22Chemical+kinetics%22">Chemical kinetics</searchLink><br /><searchLink fieldCode="DE" term="%22Immunoassay%22">Immunoassay</searchLink><br /><searchLink fieldCode="DE" term="%22Biosensors%22">Biosensors</searchLink><br /><searchLink fieldCode="DE" term="%22Immobilized+antibodies%22">Immobilized antibodies</searchLink><br /><searchLink fieldCode="DE" term="%22Molecular+recognition%22">Molecular recognition</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Abstract: Herein, we present a new sandwich assay design containing a high affinity polypeptide scaffold as immobilized capture element and an antibody for detection. These polypeptide scaffolds provide a good affinity towards one antigen and can be linked to biosensor surfaces without affecting their binding capabilities. Furthermore, the small peptides are very stable, which allows for regenerating the surface several hundreds of times and thus for reuse of the biosensor. Moreover, these receptors can be synthesized with different affinities towards one antigen, which has been proven by characterizing them using a label-free detection method RIfS (reflectometric interference spectroscopy) for collecting kinetic data. Polypeptide scaffolds with different affinities have been chosen and characterized. Upon these results, sandwich-type assays have been set-up using a fluorescently labelled antibody as detection element. Thereby could be shown, that the working range of the assay can be shifted according to the affinity of the used capturing polypeptide scaffold. The scaffolds with a higher affinity towards the antigen can detect lower concentration, and in contrary, scaffolds with lower affinities can detect higher concentrations. In consequence, using this new sandwich-type assay, we avoid the complex procedure to immobilize antibodies in correct orientation, but simultaneously keep this well-known recognition element in the assay for detection. Furthermore, in addition to all the acknowledged properties of immunoassays, we add the possibility of tuning the working range of assays in distinct manner according to request. [Copyright &y& Elsevier] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Biosensors & Bioelectronics is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1016/j.bios.2010.03.022 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 7 StartPage: 2302 Subjects: – SubjectFull: Biological assay Type: general – SubjectFull: Polypeptides Type: general – SubjectFull: Spectrum analysis Type: general – SubjectFull: Chemical kinetics Type: general – SubjectFull: Immunoassay Type: general – SubjectFull: Biosensors Type: general – SubjectFull: Immobilized antibodies Type: general – SubjectFull: Molecular recognition Type: general Titles: – TitleFull: A new assay design for clinical diagnostics based on alternative recognition elements Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Albrecht, Christiane – PersonEntity: Name: NameFull: Fechner, Peter – PersonEntity: Name: NameFull: Honcharenko, Dmytro – PersonEntity: Name: NameFull: Baltzer, Lars – PersonEntity: Name: NameFull: Gauglitz, Günter IsPartOfRelationships: – BibEntity: Dates: – D: 15 M: 06 Text: Jun2010 Type: published Y: 2010 Identifiers: – Type: issn-print Value: 09565663 Numbering: – Type: volume Value: 25 – Type: issue Value: 10 Titles: – TitleFull: Biosensors & Bioelectronics Type: main |
| ResultId | 1 |