期刊
ACS APPLIED NANO MATERIALS
卷 4, 期 5, 页码 4956-4963出版社
AMER CHEMICAL SOC
DOI: 10.1021/acsanm.1c00487
关键词
affinity tag; antibody purification; iron oxide nanoparticles; magnetic separation; protein A
资金
- Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) [388673920]
The study introduces a nanoparticle-based material for efficient magnetic separation of IgG antibodies with high binding capacity. Utilizing optimized protein A-based ligands directly immobilized on cost-effective bare iron oxide nanoparticles, the material allows for selective and high-recovery antibody capture, surpassing current technologies in both recovery rate and cost-effectiveness.
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.
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