A novel peptide ligand for IgG purification by affinity chromatography

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

Simposio; 25th American Peptide Symposium; 2017

Therapeutic monoclonal IgGs are nowadays produced in large quantities. However, their purification has an enormous impact in their production costs because protein A based affinity chromatography presents leaking and acidic conditions for elution as its main drawbacks1. On the contrary, peptides can provide mild elution conditions, mayor specificity and lower costs of production. A screening with a combinatorial peptide library has been done. It resulted in a new peptide that was then immobilized in a chromatographic matrix. Afterward, a sample of IgG mixed in culture supernatant has been passed through the column resulting in a single step purified protein.Protein A is the most used method for their purification, but the harsh elution conditions produce leeching, contaminating the product of interest and increasing the purification process costs by ruining the chromatographic resin.We performed a screening of a combinatorial peptide library and selected a novel peptide to synthesize and immobilize in a chromatographic resin. The generated resin was able to completely adsorb pure IgG. Afterwards, we confronted our resin with a spiked sample of culture supernatant with the antibody and observed it purified our protein of interest in a single step.1Wang RZ, Lin DQ, Tong HF, Lu HL, Yao SJ. J Chromatogr B Analyt Technol Biomed Life Sci 2013; 936:33-41.