Pushing Antibody-Based Labeling Systems to Higher Sensitivity by Linker-Assisted Affinity Enhancement

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00027162%3A_____%2F11%3A%230000823" target="_blank" >RIV/00027162:_____/11:#0000823 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1021/bc2001787" target="_blank" >http://dx.doi.org/10.1021/bc2001787</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/bc2001787" target="_blank" >10.1021/bc2001787</a>

Result language
angličtina
Original language name
Pushing Antibody-Based Labeling Systems to Higher Sensitivity by Linker-Assisted Affinity Enhancement
Original language description
The sensitivity of antibody/hapten-based labeling systems is limited by the natural affinity ceiling of immunoglobulins. Breaking this limit by antibody engineering is difficult. We thus attempted a different approach and investigated if the so-called bridge effect, a corecognition of the linker present between hapten and carrier protein during antibody generation, can be utilized to improve the affinity of such labeling systems. The well-known haptens 2,4-dinitrophenol (2,4-DNP) and 2,4-dichlorophenoxyacetic acid (2,4-D) were equipped with various linkers, and the resulting affinity change of their cognate antibodies was analyzed by ELISA. Anti-2,4-DNP antibodies exhibited the best affinity to their hapten when it was combined with aminobutanoic acidor aminohexanoic acid. The affinity of anti-2,4-D antibodies could be enhanced even further with longer aliphatic spacers connected to the hapten. The affinity toward aminoundecanoic acid-2,4-D derivatives, for instance, was improved abou
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Publication year
2011
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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