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Ultrafast Biomarker Quantification through Reagentless Capacitive Kinetics

[Image: see text] We introduce a facile assessment of binding kinetics at bioreceptive redox-active interfaces as a means of quantifying target proteins. This is achieved by monitoring the redox capacitance (C(r)) of a receptor-modified conductive polymer interface under continuous flow. Exemplified...

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Autores principales: Kang, Shaoyu, Sharafeldin, Mohamed, Patrick, Sophie C., Chen, Xuanxiao, Davis, Jason J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2023
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10018454/
https://www.ncbi.nlm.nih.gov/pubmed/36856747
http://dx.doi.org/10.1021/acs.analchem.2c05398
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author Kang, Shaoyu
Sharafeldin, Mohamed
Patrick, Sophie C.
Chen, Xuanxiao
Davis, Jason J.
author_facet Kang, Shaoyu
Sharafeldin, Mohamed
Patrick, Sophie C.
Chen, Xuanxiao
Davis, Jason J.
author_sort Kang, Shaoyu
collection PubMed
description [Image: see text] We introduce a facile assessment of binding kinetics at bioreceptive redox-active interfaces as a means of quantifying target proteins. This is achieved by monitoring the redox capacitance (C(r)) of a receptor-modified conductive polymer interface under continuous flow. Exemplified with the quantification of C-reactive protein (CRP), capacitance analyses resolve both the association and dissociation regimes in real-time. Significantly, the rate of electrochemical signal change within the association regime is a sensitive function of target concentration, enabling marker assaying down to picomolar levels, comparable to end-point assays, in 15 s. This reagentless proof-of-principle methodology is envisioned to be widely applicable to the facile quantification of a range of other pertinent, clinically relevant targets.
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spelling pubmed-100184542023-03-17 Ultrafast Biomarker Quantification through Reagentless Capacitive Kinetics Kang, Shaoyu Sharafeldin, Mohamed Patrick, Sophie C. Chen, Xuanxiao Davis, Jason J. Anal Chem [Image: see text] We introduce a facile assessment of binding kinetics at bioreceptive redox-active interfaces as a means of quantifying target proteins. This is achieved by monitoring the redox capacitance (C(r)) of a receptor-modified conductive polymer interface under continuous flow. Exemplified with the quantification of C-reactive protein (CRP), capacitance analyses resolve both the association and dissociation regimes in real-time. Significantly, the rate of electrochemical signal change within the association regime is a sensitive function of target concentration, enabling marker assaying down to picomolar levels, comparable to end-point assays, in 15 s. This reagentless proof-of-principle methodology is envisioned to be widely applicable to the facile quantification of a range of other pertinent, clinically relevant targets. American Chemical Society 2023-03-01 /pmc/articles/PMC10018454/ /pubmed/36856747 http://dx.doi.org/10.1021/acs.analchem.2c05398 Text en © 2023 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Kang, Shaoyu
Sharafeldin, Mohamed
Patrick, Sophie C.
Chen, Xuanxiao
Davis, Jason J.
Ultrafast Biomarker Quantification through Reagentless Capacitive Kinetics
title Ultrafast Biomarker Quantification through Reagentless Capacitive Kinetics
title_full Ultrafast Biomarker Quantification through Reagentless Capacitive Kinetics
title_fullStr Ultrafast Biomarker Quantification through Reagentless Capacitive Kinetics
title_full_unstemmed Ultrafast Biomarker Quantification through Reagentless Capacitive Kinetics
title_short Ultrafast Biomarker Quantification through Reagentless Capacitive Kinetics
title_sort ultrafast biomarker quantification through reagentless capacitive kinetics
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10018454/
https://www.ncbi.nlm.nih.gov/pubmed/36856747
http://dx.doi.org/10.1021/acs.analchem.2c05398
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