| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1374999 | Bioorganic & Medicinal Chemistry Letters | 2008 | 4 Pages |
Abstract
A flexible, trifunctional poly(ethylene glycol)-succinamide-Lysine-Lysine-maleimide (PEG-SU-Lys-Lys-mal) linker was employed to simultaneously allow biotin tagging and cell-surface targeting through an integrin α4β1-binding peptidomimetic that was regiospecifically conjugated to an IgG1-derived Fc fragment with an engineered C-terminal selenocysteine residue. The resulting antibody derivative mediates Fc receptor binding by virtue of the Fc protein and selectively targets cancer cells expressing human integrin α4β1. The PEG-SU-Lys-Lys-mal linker may have general utility as an organic tether for the construction of antibody–drug conjugates.
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Related Topics
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Authors
Joshua D. Thomas, Thomas Hofer, Christoph Rader, Terrence R. Burke Jr.,