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...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
Springer Verlag (Germany)
2013
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| Subjects: | |
| Online Access: | http://eprints.um.edu.my/15519/1/Analytical_and_Bioanalytical_Chemistry_405%282013%293889-3898_%28post-print_version%29.pdf |
| _version_ | 1825720693286764544 |
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| author | Khor, S.M. Thordarson, P. Gooding, J.J. |
| author_facet | Khor, S.M. Thordarson, P. Gooding, J.J. |
| author_sort | Khor, S.M. |
| collection | UM |
| 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. |
| first_indexed | 2024-03-06T05:39:00Z |
| format | Article |
| id | um.eprints-15519 |
| institution | Universiti Malaya |
| language | English |
| last_indexed | 2024-03-06T05:39:00Z |
| publishDate | 2013 |
| publisher | Springer Verlag (Germany) |
| record_format | dspace |
| spelling | 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 |
| 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 |
| title | 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_short | 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 |
| topic | QD Chemistry |
| url | http://eprints.um.edu.my/15519/1/Analytical_and_Bioanalytical_Chemistry_405%282013%293889-3898_%28post-print_version%29.pdf |
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