Targeting a Homogeneously Glycosylated Antibody Fc To Bind Cancer Cells Using a Synthetic Receptor Ligand

摘要

Site-selective chemical modification of proteins has wide application in biochemistry and biotechnology, including the incorporation of labels and defined post-translational modifications onto proteins to facilitate biochemical studies and incorporation of synthetic modifications onto proteins to alter bioactivity and physical properties. As part of our research into the role of N-linked glycosylation in antibody-dependent immune responses, we have needed to develop methods for targeting immunoglobulin G subclass 1 (IgGl)-type antibody fragment crystallizable (Fc) regions to bind to cancer cells in the absence of antibody fragment antigen binding (Fab) regions (Figure 1a).