Peptide affinity chromatography applied to therapeutic antibodies purification

GR BARREDO VACCHELLI ; SL GIUDICESSI; MC MARTÍNEZ CERON; O CASCONE; SA CAMPERI

International Journal of Peptide Research and Therapeutic

Springer Science

Año: 2021 vol. 47 p. 2905 - 2921

1573-3904

The interest in therapeutic monoclonal antibodies (mAbs) has significantly grown in the pharmaceutical industry, exceeding 100 FDA mAbs approved. Although the upstream processing of their industrial production has been significantly improved in the last years, the downstream processing still depends on immobilized protein A affinity chromatography. The high cost, low capacity and short half-life of immobilized protein A chromatography matrices, encouraged the design of alternative short-peptide ligands for mAb purification. Most of these peptides have been obtained by screening combinatorial peptide libraries. These low-cost ligands can be produced easily with high purity by solid-phase peptide synthesis (SPPS) and can be immobilized on chromatographic supports, thus obtaining matrices with high capacity. Furthermore, matrices with immobilized peptide ligands have longer half-life than those with protein A due to the higher stability of the peptides. In this review the design and synthesis of peptide ligands, their immobilization on chromatographic supports and the evaluation of the affinity supports for their application in mAb purification is described.