A novel multivalent (99m)Tc-labeled EG2-C4bpα antibody for targeting the epidermal growth factor receptor in tumor xenografts

Nuclear Medicine and Biology
Chongjiao LiXiaoli Lan

Abstract

The C4b binding protein (C4bp) α/β-chain C-terminal effectively induces polymerization during protein synthesis. Using this fragment and the single-domain antibody EG2, which targets the epidermal growth factor receptor (EGFR), we generated the novel multimeric antibody EG2-C4bpα. We radiolabeled EG2-C4bpα with (99m)Tc and evaluated its targeting efficiency and pharmacokinetics in tumor xenografts. EGFR expression and EGFR-EG2-C4bpα binding was evaluated in A431 and OCM-1 cells by Western blotting and flow cytometry, respectively. EG2-C4bpα was radiolabeled with [(99m)Tc(CO)3(OH2)3](+) using a tricarbonyl vial followed by purification on a PD-10 column. In vitro studies with (99m)Tc-EG2-C4bpα were performed in A431 and/or OCM-1 cells. Single photon emission computed tomography (SPECT) imaging and biodistribution studies were carried out in (99m)Tc-EG2-C4bpα-injected mice bearing A431- and OCM-1-derived tumors. EGFR immunofluorescent staining in A431 and OCM-1 tumors was performed. A431 cells showed higher EGFR expression levels than OCM-1 cells, and flow cytometry confirmed EG2-C4bpα bound more A431 cells than OCM-1 cells. (99m)Tc-EG2-C4bpα was successfully prepared with radiochemical yields of 30.3-50.4%. The binding affinity ...Continue Reading

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