Synthesis and radioiodination of tyramine cellobiose for labeling monoclonal antibodies.

A tyramine cellobiose (TCB) adduct was synthesized by the reductive amination of cellobiose by tyramine with a product yield of 78%. The TCB adduct was purified by chromatography and then iodinated using the chloramine-T method. After iodination, the adduct was activated with cyanuric chloride and linked to protein by incubation at room temperature for 2 h. Immunoreactivity and avidity were well maintained compared to electrophilically radioiodinated 1A14 whole antibody. The tumor uptake and retention were strikingly greater with iodinated TCB-antibody compared to that of the conventionally iodinated antibody; whereas, the plasma clearance curve and uptake in other organs were not changed. This method of labeling increases the retention time of radioiodine in tumors and thus extends to iodinated antibodies one of the advantages of indium labels, namely that the isotope is not readily washed out of the tumor after it becomes localized.