Abstract
The rapidly increasing application of antibodies has inspired the development of several novel methods to isolate and target antibodies using smart biomaterials that mimic the binding of Fc-receptors to antibodies. The Fc-binding domain of antibodies is the primary binding site for e.g., effector proteins and secondary antibodies, whereas antigens bind to the Fab region. Protein A, G, and L, surface proteins expressed by pathogenic bacteria, are well known to bind immunoglobulin and have been widely exploited in antibody purification strategies. Several difficulties are encountered when bacterial proteins are used in antibody research and application. One of the major obstacles hampering the use of bacterial proteins is sample contamination with trace amounts of these proteins, which can invoke an immune response in the host. Many research groups actively develop synthetic ligands that are able to selectively and strongly bind to antibodies. Among the reported ligands, peptides that bind to the Fc-domain of antibodies are attractive tools in antibody research. Besides their use as high affinity ligands in antibody purification chromatography, Fc-binding peptides are applied e.g., to localize antibodies on nanomaterials and to increase the half-life of proteins in serum. In this review, recent developments of Fc-binding peptides are presented and their binding characteristics and diverse applications are discussed.
Highlights
Recent decades have seen the development of a myriad of applications of antibodies (Abs) and related proteins, and have become one of rapid growing classes of protein pharmaceuticals [1,2,3,4,5,6].Abs are members of the immunoglobulin (Ig) super family and amount up to 20% of the plasma proteins
Besides the high production cost, one of the major problems encountered when using bacterial proteins in affinity purification of Abs is the contamination of the purified Ab samples with traces of these proteins
Our group actively develops applications of Fc-binding peptides and in this review we aim to give a brief overview of the traditional
Summary
Recent decades have seen the development of a myriad of applications of antibodies (Abs) and related proteins, and have become one of rapid growing classes of protein pharmaceuticals [1,2,3,4,5,6]. All Abs share a common structure where two identical heavy chains glycoproteins and two identical poly peptide light chains are joined by disulfide bonds to form a large Y-shaped protein These macromolecular proteins of ≥150 kDa have two fragment antigen binding (Fab) domains where their cognate antigens bind with high selectivity and specificity. Besides the high production cost, one of the major problems encountered when using bacterial proteins in affinity purification of Abs is the contamination of the purified Ab samples with traces of these proteins (better known as ligand leakage). Our group actively develops applications of Fc-binding peptides and in this review we aim to give a brief overview of the traditional (bacterial protein). Modern applications of small IgG binding ligands that target the Fc-domain of Igs will be described
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