In vitro and in vivo application of anti-cotinine antibody and cotinine-conjugated compounds
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The combination of a high-affinity antibody to a hapten, andhapten-conjugated compounds, can provide an alternative tothe direct chemical cross-linking of the antibody andcompounds. An optimal hapten for in vitro use is one that isabsent in biological systems. For in vivo applications, additionalcharacteristics such as pharmacological safety and physiologicalinertness would be beneficial. Additionally, methods forcross-linking the hapten to various chemical compounds shouldbe available. Cotinine, a major metabolite of nicotine, isconsidered advantageous in these aspects. A high-affinityanti-cotinine recombinant antibody has recently becomeavailable, and can be converted into various formats, includinga bispecific antibody. The bispecific anti-cotinine antibody wassuccessfully applied to immunoblot, enzyme immunoassay,immunoaffinity purification, and pre-targeted in vivo radioimmunoimaging. The anti-cotinine IgG molecule could becomplexed with aptamers to form a novel affinity unit, andextended the in vivo half-life of aptamers, opening up thepossibility of applying the same strategy to therapeutic peptidesand chemical compounds.
Abstract
The combination of a high-affinity antibody to a hapten, andhapten-conjugated compounds, can provide an alternative tothe direct chemical cross-linking of the antibody andcompounds. An optimal hapten for in vitro use is one that isabsent in biological systems. For in vivo applications, additionalcharacteristics such as pharmacological safety and physiologicalinertness would be beneficial. Additionally, methods forcross-linking the hapten to various chemical compounds shouldbe available. Cotinine, a major metabolite of nicotine, isconsidered advantageous in these aspects. A high-affinityanti-cotinine recombinant antibody has recently becomeavailable, and can be converted into various formats, includinga bispecific antibody. The bispecific anti-cotinine antibody wassuccessfully applied to immunoblot, enzyme immunoassay,immunoaffinity purification, and pre-targeted in vivo radioimmunoimaging. The anti-cotinine IgG molecule could becomplexed with aptamers to form a novel affinity unit, andextended the in vivo half-life of aptamers, opening up thepossibility of applying the same strategy to therapeutic peptidesand chemical compounds.
참고문헌 (37)
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