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An engineered antibody fragment (minibody; scFv-C H 3γ 1  dimer,  M  r  80 000) specific for carcinoembryonic antigen (CEA) has previously demonstrated excellent tumor targeting coupled with rapid clearance  in vivo . In this study, variable (V) genes from the anti- p185 HER-2  10H8 antibody were similarly assembled and expressed. Four constructs were made: first, the V genes were assembled in both orientations (V L -linker-V H  and V H -linker-V L ) as single chain Fvs (scFvs). Then each scFv was fused to the human IgG1 C H 3 domain, either by a two amino acid linker (ValGlu) that resulted in a non-covalent, hingeless minibody, or by IgG1 hinge and a GlySer linker peptide to produce a covalent, hinge-minibody. The constructs, expressed in NS0 mouse myeloma cells at levels of 20–60 mg/l, demonstrated binding to the human p185 HER-2  overexpressing breast cancer cell line, MCF7/HER2. Binding affinities ( K  D  ∼ 2–4 nM) were equivalent to that for the parental 10H8 mAb ( K  D  ∼ 1.6 nM). Radioiodinated 10H8 hinge-minibody was evaluated in athymic mice, bearing MCF7/HER2 xenografts. Maximum tumor uptake was 5.6 (±1.65)% injected dose/g (ID/g) at 12 h, which was lower than that of the anti-CEA minibody, whereas the blood clearance (β-phase, 5.62 h) was similar. Thus, minibodies with different specificities display similar pharmacokinetics, while tumor uptake may vary depending on the antigen–antibody system.

Characterization of engineered anti-p185 HER-2 (scFv-C H 3) 2 antibody fragments (minibodies) for tumor targeting