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The impact of antibody/epitope affinity strength on the sensitivity of electrochemical immunosensors for detecting small molecules

A displacement immunoassay involves having a labelled analogue of the analyte (the epitope) already bound to the antibody. The presence of the analyte causes a competition for antibodies, and some of the antibodies dissociates from the epitope so that it can bind with the analyte. Herein, the i...

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Main Authors: Khor, S.M., Thordarson, P., Gooding, J.J.
Format: Article
Language:English
Published: Springer Verlag (Germany) 2013
Subjects:
QD Chemistry
Online Access:http://eprints.um.edu.my/15519/1/Analytical_and_Bioanalytical_Chemistry_405%282013%293889-3898_%28post-print_version%29.pdf
http://eprints.um.edu.my/15519/
http://dx.doi.org/10.1007/s00216-013-6782-8 http://download.springer.com/static/pdf/674/art253A10.1007252Fs00216-013-6782-8.pdf?originUrl=http3A2F2Flink.springer.com2Farticle2F10.10072Fs00216-013-6782-8&token2=exp=1450677127~acl=2Fstatic2Fpdf2F6742Fart252
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spelling my.um.eprints.155192016-01-12T02:46:10Z http://eprints.um.edu.my/15519/ The impact of antibody/epitope affinity strength on the sensitivity of electrochemical immunosensors for detecting small molecules Khor, S.M. Thordarson, P. Gooding, J.J. QD Chemistry A displacement immunoassay involves having a labelled analogue of the analyte (the epitope) already bound to the antibody. The presence of the analyte causes a competition for antibodies, and some of the antibodies dissociates from the epitope so that it can bind with the analyte. Herein, the influence of the affinity of the surface-bound epitope for the antibody on the sensitivity and selectivity of a displacement immunosensor is explored both theoretically and experimentally. An electrochemical immunosensor described previously [1], where the dissociation of antibodies from an electrode surface causes an increase in current from surface-bound ferrocene species, is used for this purpose. As expected, the ease and effectiveness of the bound antibody being displaced is inversely related to the affinity of the antibody to the surface-bound epitope relative to the analyte in solution as expected. However, if the affinity constant is too low, selectivity and/or sensitivity are compromised. Experimental results are qualitatively compared with a simple mass-action model. Springer Verlag (Germany) 2013 Article PeerReviewed application/pdf en http://eprints.um.edu.my/15519/1/Analytical_and_Bioanalytical_Chemistry_405%282013%293889-3898_%28post-print_version%29.pdf Khor, S.M. and Thordarson, P. and Gooding, J.J. (2013) The impact of antibody/epitope affinity strength on the sensitivity of electrochemical immunosensors for detecting small molecules. Analytical and Bioanalytical Chemistry, 405 (11). pp. 3889-3898. http://dx.doi.org/10.1007/s00216-013-6782-8 http://download.springer.com/static/pdf/674/art253A10.1007252Fs00216-013-6782-8.pdf?originUrl=http3A2F2Flink.springer.com2Farticle2F10.10072Fs00216-013-6782-8&token2=exp=1450677127~acl=2Fstatic2Fpdf2F6742Fart252
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
Khor, S.M.
Thordarson, P.
Gooding, J.J.
The impact of antibody/epitope affinity strength on the sensitivity of electrochemical immunosensors for detecting small molecules
description A displacement immunoassay involves having a labelled analogue of the analyte (the epitope) already bound to the antibody. The presence of the analyte causes a competition for antibodies, and some of the antibodies dissociates from the epitope so that it can bind with the analyte. Herein, the influence of the affinity of the surface-bound epitope for the antibody on the sensitivity and selectivity of a displacement immunosensor is explored both theoretically and experimentally. An electrochemical immunosensor described previously [1], where the dissociation of antibodies from an electrode surface causes an increase in current from surface-bound ferrocene species, is used for this purpose. As expected, the ease and effectiveness of the bound antibody being displaced is inversely related to the affinity of the antibody to the surface-bound epitope relative to the analyte in solution as expected. However, if the affinity constant is too low, selectivity and/or sensitivity are compromised. Experimental results are qualitatively compared with a simple mass-action model.
format Article
author Khor, S.M.
Thordarson, P.
Gooding, J.J.
author_facet Khor, S.M.
Thordarson, P.
Gooding, J.J.
author_sort Khor, S.M.
title The impact of antibody/epitope affinity strength on the sensitivity of electrochemical immunosensors for detecting small molecules
title_short The impact of antibody/epitope affinity strength on the sensitivity of electrochemical immunosensors for detecting small molecules
title_full The impact of antibody/epitope affinity strength on the sensitivity of electrochemical immunosensors for detecting small molecules
title_fullStr The impact of antibody/epitope affinity strength on the sensitivity of electrochemical immunosensors for detecting small molecules
title_full_unstemmed The impact of antibody/epitope affinity strength on the sensitivity of electrochemical immunosensors for detecting small molecules
title_sort impact of antibody/epitope affinity strength on the sensitivity of electrochemical immunosensors for detecting small molecules
publisher Springer Verlag (Germany)
publishDate 2013
url http://eprints.um.edu.my/15519/1/Analytical_and_Bioanalytical_Chemistry_405%282013%293889-3898_%28post-print_version%29.pdf
http://eprints.um.edu.my/15519/
http://dx.doi.org/10.1007/s00216-013-6782-8 http://download.springer.com/static/pdf/674/art253A10.1007252Fs00216-013-6782-8.pdf?originUrl=http3A2F2Flink.springer.com2Farticle2F10.10072Fs00216-013-6782-8&token2=exp=1450677127~acl=2Fstatic2Fpdf2F6742Fart252
_version_ 1643690072576360448
score 13.211869

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