Karl D. Hardman

TL;DR: Three single-chain antigen-binding proteins are novel recombinant polypeptides, composed of an antibody variable light-chain amino acid sequence tethered to a variable heavy-chain sequence (VH) by a designed peptide that links the carboxyl terminus of the VL sequence to the amino terminusof the VH sequence.

TL;DR: The effects of linker length on binding affinity and degree of aggregation have been examined in the antifluorescein 4-4-20 and anticarcinoma CC49 single-chain Fvs and a new linker sequence was designed in which a proline was placed at the C-terminal side of the proteolytic clip site in the 212 linker.

TL;DR: In vivo targeting of tumors with a single-chain antigen-binding protein, derived from the DNA sequence of the variable regions of the antitumor monoclonal antibody B6.2, has the same in vitro antigen- binding properties as the B 6.2 Fab' fragment.

TL;DR: In this paper, a single polypeptide chain binding molecule has been proposed which has binding specificity and affinity substantially similar to the binding specificity of the light and heavy chain aggregate variable region of an antibody.

TL;DR: Reversible solvent denaturation studies demonstrated that the unfolding/refolding equilibria for the scFv proteins can be fit to a simple two-state model and that two of thescFv designs were found to be slightly more stable than single IgG domains (VL and CL) when assessed in terms of the free energy of unfolding.