2. Academic Validation
  3. A Comprehensive Evaluation of the Activity and Selectivity Profile of Ligands for RGD-binding Integrins

A Comprehensive Evaluation of the Activity and Selectivity Profile of Ligands for RGD-binding Integrins

  • Sci Rep. 2017 Jan 11;7:39805. doi: 10.1038/srep39805.
Tobias G Kapp 1,  Florian Rechenmacher 1,  Stefanie Neubauer 1,  Oleg V Maltsev 1,  Elisabetta A Cavalcanti-Adam 2,  Revital Zarka 3,  Ute Reuning 4,  Johannes Notni 5,  Hans-Jürgen Wester 5,  Carlos Mas-Moruno 6,  Joachim Spatz 2,  Benjamin Geiger 3,  Horst Kessler 1
Affiliations

Affiliations

  • 1 Institute for Advanced Study and Center for Integrated Protein Science, Department of Chemistry, Technische Universität München, Lichtenbergstr. 4, 85747 Garching, Germany.
  • 2 Max-Planck-Institute for Medical Research, Department of Biointerface Science and Technology, Heidelberg, Postal address: Heisenbergstr. 3, 70 569 Stuttgart, Germany.
  • 3 Department of Molecular Cell Biology, Weizmann Institute of Science, Rehovot, 7610001, Israel.
  • 4 Clinical Research Unit, Department of Obstetrics &Gynecology, Technische Universität München, Ismaninger Strasse 22, 81675 Munich, Germany.
  • 5 Pharmaceutical Radiochemistry, Technische Universität München, Munich, Germany.
  • 6 Biomaterials, Biomechanics and Tissue Engineering Group, Department of Materials Science and Metallurgical Engineering, and Centre for Research in NanoEngineering (CRNE), Technical University of Catalonia, 08028-Barcelona, Spain.
PMID: 28074920 DOI: 10.1038/srep39805
Abstract

Integrins, a diverse class of heterodimeric cell surface receptors, are key regulators of cell structure and behaviour, affecting cell morphology, proliferation, survival and differentiation. Consequently, mutations in specific integrins, or their deregulated expression, are associated with a variety of diseases. In the last decades, many integrin-specific ligands have been developed and used for modulation of Integrin function in medical as well as biophysical studies. The IC50-values reported for these ligands strongly vary and are measured using different cell-based and cell-free systems. A systematic comparison of these values is of high importance for selecting the optimal ligands for given applications. In this study, we evaluate a wide range of ligands for their binding affinity towards the RGD-binding integrins αvβ3, αvβ5, αvβ6, αvβ8, α5β1, αIIbβ3, using homogenous ELISA-like solid phase binding assay.

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