Peptide Affinity Chromatography Applied to Therapeutic Antibodies Purification

Area of Science:

• Biotechnology
• Chemical Engineering
• Biochemistry

Background:

• Therapeutic monoclonal antibody (mAb) production is crucial in the pharmaceutical industry, with over 100 FDA-approved mAbs.
• Current downstream processing relies heavily on immobilized protein A affinity chromatography, which is expensive and has limitations.
• The need for more efficient and cost-effective purification methods is evident.

Purpose of the Study:

• To review the design, synthesis, and application of short-peptide ligands as alternatives to protein A for mAb purification.
• To highlight the advantages of peptide ligands, including lower cost, higher capacity, and improved stability.
• To discuss the immobilization of these ligands onto chromatographic supports.

Main Methods:

• Screening of combinatorial peptide libraries to identify potential mAb-binding peptides.
• Solid-phase peptide synthesis for the production of selected peptide ligands.
• Immobilization of synthesized peptides onto chromatographic supports.
• Evaluation of the performance of peptide-based affinity matrices for mAb purification.

Main Results:

• Peptide ligands derived from combinatorial libraries offer a low-cost alternative to protein A.
• Immobilized peptide ligands provide high capacity and selectivity for mAb purification.
• Peptide-based matrices exhibit enhanced stability and longer half-lives compared to protein A matrices.

Conclusions:

• Short-peptide ligands represent a promising and economically viable strategy for industrial mAb purification.
• The development of peptide-based affinity chromatography significantly advances downstream processing in biopharmaceutical manufacturing.
• Further research into peptide ligand design and immobilization can optimize mAb purification processes.