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USE OF A CU(II)-CHELATING RESIN FOR THE PARTIAL ENRICHMENT OF HUMAN SERUM ALBUMIN AND IMMUNOGLOBULIN G FROM HUMAN PLASMA BY IMMOBILIZED METAL AFFINITY CHROMATOGRAPHY

SORAYA MADOUI ¹*, HANANE KHITHER ¹, KAMEL MOKHNACHE ², SOUMIA BENBRINIS ¹, NOURDINE CHAREF ¹

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In this proof-of-concept study, we investigated the use of Immobilized Metal Affinity Chromatography (IMAC) for the partial enrichment of Human Serum Albumin (HSA) and Immunoglobulin G (IgG) from human plasma. A functionalized chromatographic adsorbent, N, N-bis(salicylidenepropylenetriamine)-aminomethyl polystyrene, was synthesized and loaded with Cu(II) ions. The optimal conditions for adsorption and desorption of target proteins were evaluated using different buffer systems. Protein-containing fractions were analyzed by SDS-PAGE and quantified using an automated biochemical analyzer. HSAenriched fractions were obtained using a buffer containing 5 mM Tris-HCl, 10 mM imidazole, 10 mM MOPS, and 35 mM NaCl, or a phosphate buffer (10 mM) supplemented with 35 mM NaCl and 5 mM imidazole. The recovery of HSA in eluted fractions was 19.5 - 28.6% of the theoretical HSA input; when including the non-adsorbed flow-through fraction, the total protein accounted for reached 38.6 - 67.8% of the theoretical input, excluding NaOH wash fractions. IgG-enriched fractions were recovered using low imidazole concentrations (5 - 10 mM) in a phosphate/MOPS buffer system, with a recovery of 24% of the theoretical IgG input in selectively eluted fractions. These results demonstrate for the first time the potential of this novel Schiff base-functionalized Cu(II)-chelating resin as a cost-effective and promising IMAC support for the partial enrichment of major plasma proteins under mild buffer conditions.