Citation:

Roque, ACA, Lowe CR.  2007.  Rationally designed ligands for use in Affinity Chromatography: An artificial Protein L. Affinity Chromatography: Methods and Protocols. (M. Zachariou, Ed.).:93-110., U.S.A.: Humana Press Inc.

Abstract:

Synthetic affinity ligands can circumvent the drawbacks of natural immunoglobulin (Ig)-binding proteins by imparting resistance to chemical and biochemical degradation and to in situ sterilization, as well as ease and low cost of production. Protein L (PpL), isolated from Peptostreptococcus magnus strains, interacts with the Fab (antigen-binding fragment) portion of Igs, specifically with kappa light chains, and represents an almost universal ligand for the purification of antibodies. The concepts of rational design and solid-phase combinatorial chemistry were used for the discovery of a synthetic PpL mimic affinity ligand. The procedure presented in this chapter represents a general approach with the potential to be applied to different systems and target proteins.

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