Institute for Advanced Study and Center for Integrated Protein Science, Department of Chemistry, Technische Universität München, Lichtenbergstr. 4, 85747 Garching, Germany.
Max-Planck-Institute for Medical Research, Department of Biointerface Science and Technology, Heidelberg, Postal address: Heisenbergstr. 3, 70 569 Stuttgart, Germany.
Sci Rep. 2017 Jan 11;7:39805. doi: 10.1038/srep39805.
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 IC-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.
整合素是一类异源二聚体细胞表面受体，是细胞结构和行为的关键调节剂，影响细胞形态、增殖、存活和分化。因此，特定整合素的突变或其表达失调与多种疾病有关。在过去的几十年中，已经开发出许多整合素特异性配体，并用于调节医学和生物物理研究中的整合素功能。这些配体的 IC 值报道差异很大，并且使用不同的基于细胞和无细胞的系统进行测量。对这些值进行系统比较对于为给定的应用选择最佳配体非常重要。在这项研究中，我们使用均相 ELISA 样固相结合测定法评估了广泛的配体与 RGD 结合整合素 αvβ3、αvβ5、αvβ6、αvβ8、α5β1、αIIbβ3 的结合亲和力。
