In vitro and in vivo application of anti-cotinine antibody and cotinine-conjugated compounds
The combination of a high-affinity antibody to a hapten, and hapten-conjugated compounds, can provide an alternative to the direct chemical cross-linking of the antibody and compounds. An optimal hapten for in vitro use is one that is absent in biological systems. For in vivo applications, additiona...
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Korean Society for Biochemistry and Molecular Biology
2014
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4163880/ |
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pubmed-41638802014-09-16 In vitro and in vivo application of anti-cotinine antibody and cotinine-conjugated compounds Kim, Hyori Yoon, Soomin Chung, Junho Review Article The combination of a high-affinity antibody to a hapten, and hapten-conjugated compounds, can provide an alternative to the direct chemical cross-linking of the antibody and compounds. An optimal hapten for in vitro use is one that is absent in biological systems. For in vivo applications, additional characteristics such as pharmacological safety and physiological inertness would be beneficial. Additionally, methods for cross-linking the hapten to various chemical compounds should be available. Cotinine, a major metabolite of nicotine, is considered advantageous in these aspects. A high-affinity anti-cotinine recombinant antibody has recently become available, and can be converted into various formats, including a bispecific antibody. The bispecific anti-cotinine antibody was successfully applied to immunoblot, enzyme immunoassay, immunoaffinity purification, and pre-targeted in vivo radioimmunoimaging. The anti-cotinine IgG molecule could be complexed with aptamers to form a novel affinity unit, and extended the in vivo half-life of aptamers, opening up the possibility of applying the same strategy to therapeutic peptides and chemical compounds. [BMB Reports 2014; 47(3): 130-134] Korean Society for Biochemistry and Molecular Biology 2014-03 /pmc/articles/PMC4163880/ /pubmed/24499668 http://dx.doi.org/10.5483/BMBRep.2014.47.3.006 Text en Copyright © 2014, Korean Society for Biochemistry and Molecular Biology http://creativecommons.org/licenses/by-nc/3.0 This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Kim, Hyori Yoon, Soomin Chung, Junho |
| spellingShingle |
Kim, Hyori Yoon, Soomin Chung, Junho In vitro and in vivo application of anti-cotinine antibody and cotinine-conjugated compounds |
| author_facet |
Kim, Hyori Yoon, Soomin Chung, Junho |
| author_sort |
Kim, Hyori |
| title |
In vitro and in vivo application of anti-cotinine antibody and cotinine-conjugated compounds |
| title_short |
In vitro and in vivo application of anti-cotinine antibody and cotinine-conjugated compounds |
| title_full |
In vitro and in vivo application of anti-cotinine antibody and cotinine-conjugated compounds |
| title_fullStr |
In vitro and in vivo application of anti-cotinine antibody and cotinine-conjugated compounds |
| title_full_unstemmed |
In vitro and in vivo application of anti-cotinine antibody and cotinine-conjugated compounds |
| title_sort |
in vitro and in vivo application of anti-cotinine antibody and cotinine-conjugated compounds |
| description |
The combination of a high-affinity antibody to a hapten, and hapten-conjugated compounds, can provide an alternative to the direct chemical cross-linking of the antibody and compounds. An optimal hapten for in vitro use is one that is absent in biological systems. For in vivo applications, additional characteristics such as pharmacological safety and physiological inertness would be beneficial. Additionally, methods for cross-linking the hapten to various chemical compounds should be available. Cotinine, a major metabolite of nicotine, is considered advantageous in these aspects. A high-affinity anti-cotinine recombinant antibody has recently become available, and can be converted into various formats, including a bispecific antibody. The bispecific anti-cotinine antibody was successfully applied to immunoblot, enzyme immunoassay, immunoaffinity purification, and pre-targeted in vivo radioimmunoimaging. The anti-cotinine IgG molecule could be complexed with aptamers to form a novel affinity unit, and extended the in vivo half-life of aptamers, opening up the possibility of applying the same strategy to therapeutic peptides and chemical compounds. [BMB Reports 2014; 47(3): 130-134] |
| publisher |
Korean Society for Biochemistry and Molecular Biology |
| publishDate |
2014 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4163880/ |
| _version_ |
1613133812026310656 |