Novel ligands for the affinity-chromatographic purification of antibodies

Affinity chromatography represents one of the most powerful fractionation t echniques for the large-scale purification of biotechnological products. De spite its potential, the use of this methodology is limited by the availabi lity of specific ligands for each target. Combinatorial chemistry and molec ular modeling, often combined, have become interesting and innovative metho ds for generating novel ligands, tailored to specific biotechnological need s. One of the greatest area of application has been the discovery of novel lig ands for the purification of antibodies, which represent an emerging but ve ry important class of innovative therapeutic agents for the treatment of a vast array of diseases. Naturally available affinity ligands, such as Prote in A or G for IgG purification or lectins for IgA and IgM purification, whi ch are obtained from microorganisms or genetically modified bacteria throug h complex and expensive procedures, are not well suited for large-scale pur ification and require moreover time-consuming analytical controls to check for the presence of contaminants which may affect the safety of the purifie d antibody for clinical purposes. Recent results suggest that the applicati on of combinatorial technologies and molecular modeling for the discovery o f synthetic ligands may open new avenues for the development of more effici ent, less expensive and-more importantly-safer procedures for antibody puri fication at the industrial level. (C) 2001 Elsevier Science B.V. All rights reserved.