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Studies in the Area of Chromatography Reported from Technical University (Improving the binding capacities of protein A chromatographic materials by...

July 11, 2014



Studies in the Area of Chromatography Reported from Technical University (Improving the binding capacities of protein A chromatographic materials by means of ligand polymerization)

By a News Reporter-Staff News Editor at Science Letter -- Researchers detail new data in Science. According to news reporting originating from Garching, Germany, by NewsRx correspondents, research stated, "Protein A chromatography is one of the most important techniques used in the purification of monoclonal antibodies. Due to the low dynamic binding capacity of protein A chromatographic materials compared to other stationary phases, protein A chromatography is often discussed to be the bottleneck among current purification processes."

Our news editors obtained a quote from the research from Technical University, "Several approaches were tested within this study in order to maximize IgG binding capacities of current acrylamido-based based resins. Genetic engineering techniques were used in order to polymerize one of the IgG binding domains (B-domain) of protein A from Staphylococcus aureus (SpA) to achieve ligands with an increased length. The solution-binding ratio and the total size of ligand-antibody complexes were used to characterize the interaction potential of novel ligands, revealing a relatively linear dependency between the number of binding domains upon the amount of bound antibody molecules. This relationship was also valid up to a ligand which was comprised of 8 B-domains after attaching them onto acrylamido-based based stationary phases using epoxy coupling techniques. Equilibrium binding capacities of more than 80 mg(hlgG) mL(-1) were achieved using the B8 ligand. Furthermore, static binding capacities, especially for smaller ligands comprised of fewer B-domains, were improved up to 87 mg(hlgG) mL(-1) using site-specific coupling chemistry, which is an improvement of more than 20% compared to commercially available materials."

According to the news editors, the research concluded: "In order to evaluate pore exclusion effects due to the use of prolonged affinity ligands, prepared materials were characterized regarding their effective intraparticle porosity and breakthrough capacity."

For more information on this research see: Improving the binding capacities of protein A chromatographic materials by means of ligand polymerization. Journal of Chromatography A, 2014;1347():80-86. Journal of Chromatography A can be contacted at: Elsevier Science Bv, PO Box 211, 1000 Ae Amsterdam, Netherlands. (Elsevier - www.elsevier.com; Journal of Chromatography A - www.elsevier.com/wps/product/cws_home/502688)

The news editors report that additional information may be obtained by contacting M.F. von Roman, Technical University of Munich, Fac Mech Engn, Bioseparat Engn Grp, D-85748 Garching, Germany (see also Science).

Keywords for this news article include: Europe, Germany, Science, Garching

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


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Source: Science Letter


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