Abstract
A major goal of antibody (Ab)-based tumor targeting has been to specifically deliver a variety of agents, such as radioisotopes, drugs, toxins, lymphokines, and enzymes for imaging and therapy. Intact immunoglobulin G molecules are large (150 kDa) glycoproteins that exhibit a slow systemic clearance, often leading to poor tumor-targeting specificity Fig1 ). Smaller Ab-derived molecules include enzymatically produced 50-kDa Fabs and engineered 25-kDa single-chain Fvs (scFvs) consisting of heavy- and light-chain variable regions (VH and VL) connected by a flexible peptide linker of 14–24 residues (1) ,2; Fig. 2; Fig. 1)). Compared to immunoglobulin G molecules, Fabs and scFvs exhibit significantly improved tumor specificity and intratumoral penetration (3)-5. However, the rapid blood clearance and monovalent nature of these small molecules result in considerably lower quantitative tumor retention (36).
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Kipriyanov, S.M. (2002). Generation of Bispecific and Tandem Diabodies. In: O’Brien, P.M., Aitken, R. (eds) Antibody Phage Display. Methods in Molecular Biology™, vol 178. Humana Press. https://doi.org/10.1385/1-59259-240-6:317
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DOI: https://doi.org/10.1385/1-59259-240-6:317
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