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Impact of Silanization Parameters and Antibody Immobilization Strategy on Binding Capacity of Photonic Ring Resonators

Ring resonator-based biosensors have found widespread application as the transducing principle in “lab-on-a-chip” platforms due to their sensitivity, small size and support for multiplexed sensing. Their sensitivity is, however, not inherently selective towards biomarkers, and surface functionalizat...

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Autores principales: Arnfinnsdottir, Nina Bjørk, Chapman, Cole A., Bailey, Ryan C., Aksnes, Astrid, Stokke, Bjørn Torger
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7309079/
https://www.ncbi.nlm.nih.gov/pubmed/32498466
http://dx.doi.org/10.3390/s20113163
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author Arnfinnsdottir, Nina Bjørk
Chapman, Cole A.
Bailey, Ryan C.
Aksnes, Astrid
Stokke, Bjørn Torger
author_facet Arnfinnsdottir, Nina Bjørk
Chapman, Cole A.
Bailey, Ryan C.
Aksnes, Astrid
Stokke, Bjørn Torger
author_sort Arnfinnsdottir, Nina Bjørk
collection PubMed
description Ring resonator-based biosensors have found widespread application as the transducing principle in “lab-on-a-chip” platforms due to their sensitivity, small size and support for multiplexed sensing. Their sensitivity is, however, not inherently selective towards biomarkers, and surface functionalization of the sensors is key in transforming the sensitivity to be specific for a particular biomarker. There is currently no consensus on process parameters for optimized functionalization of these sensors. Moreover, the procedures are typically optimized on flat silicon oxide substrates as test systems prior to applying the procedure to the actual sensor. Here we present what is, to our knowledge, the first comparison of optimization of silanization on flat silicon oxide substrates to results of protein capture on sensors where all parameters of two conjugation protocols are tested on both platforms. The conjugation protocols differed in the chosen silanization solvents and protein immobilization strategy. The data show that selection of acetic acid as the solvent in the silanization step generally yields a higher protein binding capacity for C-reactive protein (CRP) onto anti-CRP functionalized ring resonator sensors than using ethanol as the solvent. Furthermore, using the BS3 linker resulted in more consistent protein binding capacity across the silanization parameters tested. Overall, the data indicate that selection of parameters in the silanization and immobilization protocols harbor potential for improved biosensor binding capacity and should therefore be included as an essential part of the biosensor development process.
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spelling pubmed-73090792020-06-25 Impact of Silanization Parameters and Antibody Immobilization Strategy on Binding Capacity of Photonic Ring Resonators Arnfinnsdottir, Nina Bjørk Chapman, Cole A. Bailey, Ryan C. Aksnes, Astrid Stokke, Bjørn Torger Sensors (Basel) Article Ring resonator-based biosensors have found widespread application as the transducing principle in “lab-on-a-chip” platforms due to their sensitivity, small size and support for multiplexed sensing. Their sensitivity is, however, not inherently selective towards biomarkers, and surface functionalization of the sensors is key in transforming the sensitivity to be specific for a particular biomarker. There is currently no consensus on process parameters for optimized functionalization of these sensors. Moreover, the procedures are typically optimized on flat silicon oxide substrates as test systems prior to applying the procedure to the actual sensor. Here we present what is, to our knowledge, the first comparison of optimization of silanization on flat silicon oxide substrates to results of protein capture on sensors where all parameters of two conjugation protocols are tested on both platforms. The conjugation protocols differed in the chosen silanization solvents and protein immobilization strategy. The data show that selection of acetic acid as the solvent in the silanization step generally yields a higher protein binding capacity for C-reactive protein (CRP) onto anti-CRP functionalized ring resonator sensors than using ethanol as the solvent. Furthermore, using the BS3 linker resulted in more consistent protein binding capacity across the silanization parameters tested. Overall, the data indicate that selection of parameters in the silanization and immobilization protocols harbor potential for improved biosensor binding capacity and should therefore be included as an essential part of the biosensor development process. MDPI 2020-06-02 /pmc/articles/PMC7309079/ /pubmed/32498466 http://dx.doi.org/10.3390/s20113163 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Arnfinnsdottir, Nina Bjørk
Chapman, Cole A.
Bailey, Ryan C.
Aksnes, Astrid
Stokke, Bjørn Torger
Impact of Silanization Parameters and Antibody Immobilization Strategy on Binding Capacity of Photonic Ring Resonators
title Impact of Silanization Parameters and Antibody Immobilization Strategy on Binding Capacity of Photonic Ring Resonators
title_full Impact of Silanization Parameters and Antibody Immobilization Strategy on Binding Capacity of Photonic Ring Resonators
title_fullStr Impact of Silanization Parameters and Antibody Immobilization Strategy on Binding Capacity of Photonic Ring Resonators
title_full_unstemmed Impact of Silanization Parameters and Antibody Immobilization Strategy on Binding Capacity of Photonic Ring Resonators
title_short Impact of Silanization Parameters and Antibody Immobilization Strategy on Binding Capacity of Photonic Ring Resonators
title_sort impact of silanization parameters and antibody immobilization strategy on binding capacity of photonic ring resonators
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7309079/
https://www.ncbi.nlm.nih.gov/pubmed/32498466
http://dx.doi.org/10.3390/s20113163
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