title: Biomimetic affinity ligands for immunoglobulins based on the multicomponent Ugi reaction.
abstract: Affinity chromatography is the method of choice for biomolecule separation and isolation with highly specific target recognition; it is ideally suited to the purification of immunotherapeutic proteins (i.e., mAbs). Conventional affinity purification protocols are based on natural immunoglobulin (Ig)-binding proteins, which are expensive to produce, labile, unstable, and exhibit lot-to-lot variability. Biological ligands are now being replaced by cost-effective, synthetic ligands, derived from the concepts of rational design and combinatorial chemistry, aided by in silico approaches. In this chapter, we describe a new synthetic procedure for the development of affinity ligands for immunoglobulins based on the multicomponent Ugi reaction. The lead ligand developed herein is specific for the IgG-Fab fragment and mimics Protein L (PpL), an IgG-binding protein isolated from Peptostreptococcus magnus strains and usually used for the purification of antibodies and their fragments.
authors.affiliation: Department of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK.
authors.forename: Graziella
authors.initials: G
authors.lastname: El Khoury
authors.forename: Laura A
authors.initials: LA
authors.lastname: Rowe
authors.forename: Christopher R
authors.initials: CR
authors.lastname: Lowe
mesh_terms: D040761:Biomimetic Materials / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism*; D060326:Chemistry Techniques, Synthetic / Q000379:methods*; D002846:Chromatography, Affinity; D020650:Combinatorial Chemistry Techniques; D015195:Drug Design; D007074:Immunoglobulin G / Q000378:metabolism*; D008024:Ligands; D054852:Small Molecule Libraries / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism; D014227:Triazines / Q000737:chemistry
chemical_list: D007074:Immunoglobulin G; D008024:Ligands; D054852:Small Molecule Libraries; D014227:Triazines