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Kaveh-Baghbaderani, Y; Allgayer, R; Schwaminger, SP; Fraga-Garcia, P; Berensmeier, S.
Magnetic Separation of Antibodies with High Binding Capacity by Site-Directed Immobilization of Protein A-Domains to Bare Iron Oxide Nanoparticles
ACS APPL NANO MATER. 2021; 4(5): 4956-4963. Doi: 10.1021/acsanm.1c00487
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Co-authors Med Uni Graz: Schwaminger Sebastian
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Abstract:: The demand for purified antibodies is ever-rising. This study presents a nanoparticle-based material for efficient magnetic separation of immunoglobulin G (IgG) with high binding capacity. The characteristics include: (i) Cost-effective bare iron oxide nanoparticles are used as the solid phase on which optimized protein A-based ligands are directly immobilized. An additional chemical modification or activation is not needed. (ii) Oriented immobilization of the ligands is promoted using a C-terminal peptide tag, containing amino acids with an affinity for iron oxide. (iii) The immobilized ligand consists of eight polymerized B-domains of Protein A. This affinity adsorbent for antibody capture allows a recovery of up to 418 mg IgG per gram of particle, which exceeds the state of the art of magnetic nanoparticles as well as microparticles. Particles with a lower ligand density show a higher percentage recovery of IgG, which allows for a cost-effective design of the adsorbent. Furthermore, the selectivity of the immobilized ligand is shown by means of purification of rabbit polyclonal IgG using rabbit serum.
Find related publications in this database (Keywords): affinity tag; antibody purification; iron oxide nanoparticles; magnetic separation; protein A