Abstract
Antibodies are widely used as therapeutic drugs in the treatment of various diseases. Currently, Protein A affinity chromatography is still the most popular technique in antibody purification. However, it has some limitations such as high cost, leakage of ligands and requirement of harsh elution conditions. Hydrophobic charge-induction chromatography (HCIC) provides an alternative to Protein A affinity chromatography. The binding between HCIC resins and target proteins can be achieved via hydrophobic interactions at neutral pH, and proteins can be eluted via electrostatic repulsion between proteins and charged ligands under acidic conditions. HCIC is applied to the purification of antibodies and some specific proteins successfully, which is a promising technique with economic benefits and high efficiency. In this review, theoretical analysis and factors affecting HCIC adsorption are presented that provides functional mechanism of HCIC. HCIC ligands with different structures available on the market and reported in the literature are discussed and their recent applications in antibody purification are reviewed. Moreover, affecting factors such as ligand density, preparation approaches and additives of HCIC resins on their adsorption performance are summarized and discussed. In addition, future development of HCIC such as polymer-grafted HCIC resins, membrane chromatography with HCIC and continuous chromatography are proposed.
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