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        Purification, Characterization, and Biotinylation of Single-Chain Antibodies

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        The variable region (Fv) portion of an antibody is comprised of the antibody VH and VL domains and is the smallest antibody fragment containing a complete antigen-binding site. To stabilize the association of the recombinant VH and VL domains, they have been linked in single-chain Fv constructs with a short peptide that bridges the approx 3.5 nm between the carboxy terminus of one domain and the ammo terminus of the other (1 3 ). An NMR comparison of the unlinked Fv fragment of the antibody McPC603 with the corresponding scFv containing a VH -(Gly4 Ser)3 -VL linker has shown no perturbation of the folding of the variable domains by the linker (4 ,5 ). In comparison to the much larger Fab′, F(ab′)2 , and IgG forms of monoclonal antibody (MAb) from which they are derived, scFvs have lower retention times in nontarget tissues, more rapid blood clearance, and better tumor penetration (6 8 ). ScFvs, therefore, represent potentially very useful molecules for the targeted delivery of drugs, toxins, or radionuclides to a tumor site.
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