A novel peptide for IgG purification by affinity chromatography

G. R. BARREDO; S. L. SAAVEDRA; S. L. GIUDICESSI; M. C. MARTÍNEZ-CERON; F. ALBERICIO; O. CASCONE; S. A. CAMPERI

Whistler

Simposio; American Peptide Symposium 2017; 2017

American Peptide Society

Therapeutic monoclonal IgGs are nowadays produced in large quantities. Protein A affinity chromatography is the standard methodology for their purification, but the harsh elution conditions produce leaching, thus contaminating the product of interest and reducing the operating life of the chromatographic matrix.The therapeutic mAB Rituximab, provided by CMC Biologist (USA), was labeled with Texas-Red. A peptide combinatorial library was synthesized on HMBA-ChemMatrix resin by the Divide-Couple-Recombine method. After library screening, colored fluorescent beads were isolated and analyzed by MALDI TOF MS/MS. One of the peptide selected was re-synthesized in a larger quantity and immobilized on agarose. The generated resin was able to completely adsorb IgG from CHO cell supernatants while all the contaminants passed through without interacting with the chromatographic matrix. In conclusion, an efficient Affinity Chromatogaphy method based in a simple peptide allows the purification of the mAB Rituximab in a single step at low cost.