Non-invasive control of protein-surface interactions for repeated electrochemical immunosensor use

Although most immunosensors which have high affinity antigen-antibody interactions can perform highly specific and sensitive detection, antibody-antigen bonds are typically too strong to allow for rapid reversibility. Therefore, creating a biosensor platform capable of non-invasive surface regenerat...

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Main Authors: Khoo, M.M., Rahim, Z., Darwish, N.T., Alias, Y., Khor, S.M.
Format: Article
Language:English
Published: 2016
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Online Access:http://eprints.um.edu.my/15517/1/Sensors_and_Actuators_B_Chemical_224%282016%29683-691_%28post-print_version%29.pdf
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http://www.sciencedirect.com/science/article/pii/S0925400515305517 http://ac.els-cdn.com/S0925400515305517/1-s2.0-S0925400515305517-main.pdf?tid=12ba379e-a7a1-11e5-ab92-00000aab0f26&acdnat=1450674775599c4957b60b3d1ca3619915c6369e87
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spelling my.um.eprints.155172016-01-12T02:22:59Z http://eprints.um.edu.my/15517/ Non-invasive control of protein-surface interactions for repeated electrochemical immunosensor use Khoo, M.M. Rahim, Z. Darwish, N.T. Alias, Y. Khor, S.M. QD Chemistry Although most immunosensors which have high affinity antigen-antibody interactions can perform highly specific and sensitive detection, antibody-antigen bonds are typically too strong to allow for rapid reversibility. Therefore, creating a biosensor platform capable of non-invasive surface regeneration is important for reducing costs and being able to perform multiple measurements without losing sensor sensitivity. A reusable electrochemical immunosensor was developed on which a glassy carbon plate was passivated with a mixed layer of 4-nitroaniline/p-phenylenediamine, attached with gold nanoparticles, followed by surface-bound epitope (sulfo-NHS-biotin) to which the monoclonal anti-biotin IgG antibody was complexed. Free biotin was detected when the antibody dissociated from the surface-bound epitope in the presence of free biotin during a displacement assay. The electrochemical impedance spectroscopy technique was used to monitor the protein-surface interactions. To ensure that the immunosensor could be used repeatedly, electrode polarization was used to remove as much surface-bound antibody as possible by applying a negative potential to the working electrode. Therefore, the antibody could bind to the surface-bound epitope again after the electrode was reincubated in the antibody solution, and hence, the displacement assay could be performed again for repeated sensor use. Comparisons between disposable and reusable biosensors are discussed in this paper. 2016 Article PeerReviewed application/pdf en http://eprints.um.edu.my/15517/1/Sensors_and_Actuators_B_Chemical_224%282016%29683-691_%28post-print_version%29.pdf Khoo, M.M. and Rahim, Z. and Darwish, N.T. and Alias, Y. and Khor, S.M. (2016) Non-invasive control of protein-surface interactions for repeated electrochemical immunosensor use. Sensors and Actuators B: Chemical, 224. pp. 683-691. http://www.sciencedirect.com/science/article/pii/S0925400515305517 http://ac.els-cdn.com/S0925400515305517/1-s2.0-S0925400515305517-main.pdf?tid=12ba379e-a7a1-11e5-ab92-00000aab0f26&acdnat=1450674775599c4957b60b3d1ca3619915c6369e87
institution Universiti Malaya
building UM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Malaya
content_source UM Research Repository
url_provider http://eprints.um.edu.my/
language English
topic QD Chemistry
spellingShingle QD Chemistry
Khoo, M.M.
Rahim, Z.
Darwish, N.T.
Alias, Y.
Khor, S.M.
Non-invasive control of protein-surface interactions for repeated electrochemical immunosensor use
description Although most immunosensors which have high affinity antigen-antibody interactions can perform highly specific and sensitive detection, antibody-antigen bonds are typically too strong to allow for rapid reversibility. Therefore, creating a biosensor platform capable of non-invasive surface regeneration is important for reducing costs and being able to perform multiple measurements without losing sensor sensitivity. A reusable electrochemical immunosensor was developed on which a glassy carbon plate was passivated with a mixed layer of 4-nitroaniline/p-phenylenediamine, attached with gold nanoparticles, followed by surface-bound epitope (sulfo-NHS-biotin) to which the monoclonal anti-biotin IgG antibody was complexed. Free biotin was detected when the antibody dissociated from the surface-bound epitope in the presence of free biotin during a displacement assay. The electrochemical impedance spectroscopy technique was used to monitor the protein-surface interactions. To ensure that the immunosensor could be used repeatedly, electrode polarization was used to remove as much surface-bound antibody as possible by applying a negative potential to the working electrode. Therefore, the antibody could bind to the surface-bound epitope again after the electrode was reincubated in the antibody solution, and hence, the displacement assay could be performed again for repeated sensor use. Comparisons between disposable and reusable biosensors are discussed in this paper.
format Article
author Khoo, M.M.
Rahim, Z.
Darwish, N.T.
Alias, Y.
Khor, S.M.
author_facet Khoo, M.M.
Rahim, Z.
Darwish, N.T.
Alias, Y.
Khor, S.M.
author_sort Khoo, M.M.
title Non-invasive control of protein-surface interactions for repeated electrochemical immunosensor use
title_short Non-invasive control of protein-surface interactions for repeated electrochemical immunosensor use
title_full Non-invasive control of protein-surface interactions for repeated electrochemical immunosensor use
title_fullStr Non-invasive control of protein-surface interactions for repeated electrochemical immunosensor use
title_full_unstemmed Non-invasive control of protein-surface interactions for repeated electrochemical immunosensor use
title_sort non-invasive control of protein-surface interactions for repeated electrochemical immunosensor use
publishDate 2016
url http://eprints.um.edu.my/15517/1/Sensors_and_Actuators_B_Chemical_224%282016%29683-691_%28post-print_version%29.pdf
http://eprints.um.edu.my/15517/
http://www.sciencedirect.com/science/article/pii/S0925400515305517 http://ac.els-cdn.com/S0925400515305517/1-s2.0-S0925400515305517-main.pdf?tid=12ba379e-a7a1-11e5-ab92-00000aab0f26&acdnat=1450674775599c4957b60b3d1ca3619915c6369e87
_version_ 1643690072281710592
score 13.211869