A Novel Peptide for IgG Purification by Affinity Chromatography

GABRIELA R. BARREDO; SOLEDAD L. SAAVEDRA; SILVANA L. GIUDICESSI; M. C. MARTÍNEZ CERON; FERNANDO ALBERICIO; OSVALDO CASCONE; SILVIA A. CAMPERI

Whistler

Simposio; 25th American Peptide Symposium; 2017

American Peptide Society

Therapeutic monoclonal IgGs are nowadays produced in largequantities. Protein A affinity chromatography is the standardmethodology for their purification, but the harsh elutionconditions produce leaching, thus contaminating the product ofinterest and reducing the operating life of the chromatographicmatrix.The therapeutic mAb Rituximab, provided by CMC Biologist(USA), was labeled with Texas-Red. A peptide combinatoriallibrary was synthesized on HMBA-ChemMatrix resin by theDivide-Couple-Recombine method. After library screening,colored fluorescent beads were isolated and analyzed by MALDITOF MS/MS. One of the peptide selected was re-synthesized ina larger quantity and immobilized on agarose. The generatedresin was able to completely adsorb IgG from CHO cellsupernatants while all the contaminants passed through withoutinteracting with the chromatographic matrix. In conclusion, anefficient Affinity Chromatogaphic method based in a simplepeptide allows the purification of the mAb Rituximab in a singlestep at low cost.