Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
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SHR Neuro Krebs Kardio Lipid Stoffw Microb
Padwal, P; Finger, C; Fraga-García, P; Kaveh-Baghbaderani, Y; Schwaminger, SP; Berensmeier, S.
Seeking Innovative Affinity Approaches: A Performance Comparison between Magnetic Nanoparticle Agglomerates and Chromatography Resins for Antibody Recovery.
ACS Appl Mater Interfaces. 2020; 12(36): 39967-39978.
Doi: 10.1021/acsami.0c05007
Web of Science
PubMed
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- Co-Autor*innen der Med Uni Graz
- Schwaminger Sebastian
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- Abstract:
- Monoclonal antibodies are key molecules in medicine and pharmaceuticals. A potentially crucial drawback for faster advances in research here is their high price due to the extremely expensive antibody purification process, particularly the affinity capture step. Affinity chromatography materials have to demonstrate the high binding capacity and recovery efficiency as well as superior chemical and mechanical stability. Low-cost materials and robust, faster processes would reduce costs and enhance industrial immunoglobulin purification. Therefore, exploring the use of alternative materials is necessary. In this context, we conduct the first comparison of the performance of magnetic nanoparticles with commercially available chromatography resins and magnetic microparticles with regard to immobilizing Protein G ligands and recovering immunoglobulin G (IgG). Simultaneously, we demonstrate the suitability of bare as well as silica-coated and epoxy-functionalized magnetite nanoparticles for this purpose. All materials applied have a similar specific surface area but differ in the nature of their matrix and surface accessibility. The nanoparticles are present as micrometer agglomerates in solution. The highest Protein G density can be observed on the nanoparticles. IgG adsorbs as a multilayer on all materials investigated. However, the recovery of IgG after washing indicates a remaining monolayer, which points to the specificity of the IgG binding to the immobilized Protein G. One important finding is the impact of the ligand-binding stoichiometry (Protein G surface coverage) on IgG recovery, reusability, and the ability to withstand long-term sanitization. Differences in the materials' performances are attributed to mass transfer limitations and steric hindrance. These results demonstrate that nanoparticles represent a promising material for the economical and efficient immobilization of proteins and the affinity purification of antibodies, promoting innovation in downstream processing.
- Find related publications in this database (using NLM MeSH Indexing)
- Epoxy Resins - chemistry
- Immunoglobulin G - chemistry
- Magnetite Nanoparticles - chemistry
- Particle Size - administration & dosage
- Porosity - administration & dosage
- Surface Properties - administration & dosage
- Find related publications in this database (Keywords)
- immunoglobulin purification
- affinity chromatography
- protein A
- protein G
- protein immobilization
- ligand density
- magnetic separation
- iron oxide nanoparticles
- nanoparticle agglomeration