A comprehensive evaluation of the activity and selectivity profile of ligands for RGD-binding integrins

Cita com:
hdl:2117/102476
CovenanteeTechnische Universität München
Document typeArticle
Defense date2017-01-11
PublisherMacmillan Publishers
Rights accessOpen Access
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Except where otherwise noted, its contents are licensed under a Creative Commons license
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Attribution-NonCommercial-NoDerivs 3.0 Spain
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 avß3, avß5, avß6, avß8, a5ß1, aIIbß3, using homogenous ELISA-like solid phase binding assay.
CitationKapp, T., Rechenmacher, F., Neubauer, S., Maltsev, O., Cavalcanti-Adam, E., Zarka, R., Reuning, U., Notni, J., Wester, H.J., Mas-Moruno, C., Spatz, J., Geiger, B., Kessler, H. A comprehensive evaluation of the activity and selectivity profile of ligands for RGD-binding integrins. "Scientific reports", 11 Gener 2017, vol. 7.
ISSN2045-2322
Publisher versionhttp://www.nature.com/articles/srep39805
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