News Column

Findings from S. Lorey and Colleagues Provides New Insights into Tissue Engineering

June 18, 2014



By a News Reporter-Staff News Editor at Biotech Week -- Current study results on Biomedicine and Biomedical Engineering have been published. According to news reporting from Halle, Germany, by NewsRx journalists, research stated, "Targeting molecules to tumor cells is a promising mode of action for cancer therapy. Ubiquitin-based high affinity, specific, and stable binding molecules for extradomain B are accumulated in the tumor."

The news correspondents obtained a quote from the research, "Ubiquitin may be engineered for high affinity target binding and modified with half-life extension technologies. Ubiquitin qualifies as a well suited scaffold protein adaptable to specific tasks. Targeting effector molecules to tumor cells is a promising mode of action for cancer therapy and diagnostics. Binding proteins with high affinity and specificity for a tumor target that carry effector molecules such as toxins, cytokines, or radiolabels to their intended site of action are required for these applications. In order to yield high tumor accumulation while maintaining low levels in healthy tissues and blood, the half-life of such conjugates needs to be in an optimal range. Scaffold-based binding molecules are small proteins with high affinity and short systemic circulation. Due to their low molecular complexity, they are well suited for combination with effector molecules as well as half-life extension technologies yielding therapeutics with half-lives adapted to the specific therapy. We have identified ubiquitin as an ideal scaffold protein due to its outstanding biophysical and biochemical properties. Based on a dimeric ubiquitin library, high affinity and specific binding molecules, so-called Affilin ® molecules, have been selected against the extradomain B of fibronectin, a target almost exclusively expressed in tumor tissues. Extradomain B-binding molecules feature high thermal and serum stability as well as strong in vitro target binding and in vivo tumor accumulation. Application of several half-life extension technologies results in molecules of largely unaffected affinity but significantly prolonged in vivo half-life and tumor retention."

According to the news reporters, the research concluded: "Our results demonstrate the utility of ubiquitin as a scaffold for the generation of high affinity binders in a modular fashion, which can be combined with effector molecules and half-life extension technologies."

For more information on this research see: Novel Ubiquitin-derived High Affinity Binding Proteins with Tumor Targeting Properties. Journal of Biological Chemistry, 2014;289(12):8493-8507. Journal of Biological Chemistry can be contacted at: Amer Soc Biochemistry Molecular Biology Inc, 9650 Rockville Pike, Bethesda, MD 20814-3996, USA. (American Society for Biochemistry and Molecular Biology - www.asbmb.org; Journal of Biological Chemistry - www.jbc.org/)

Our news journalists report that additional information may be obtained by contacting S. Lorey, Scil Prot GmbH, D-06120 Halle, Saale, Germany. Additional authors for this research include E. Fiedler, A. Kunert, J. Nerkamp, C. Lange, M. Fiedler, E. Bosse-Doenecke, M. Meysing, M. Gloser, C. Rundfeldt, U. Rauchhaus, I. Hanssgen, T. Gottler, A. Steuernagel, U. Fiedler and U. Haupts (see also Biomedicine and Biomedical Engineering).

Keywords for this news article include: Tissue Engineering, Biomedicine and Biomedical Engineering, Halle, Europe, Germany, Therapy, Peptides, Proteins, Technology, Ubiquitins, Amino Acids, Bioengineering

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


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Source: Biotech Week


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