Artificial RGD Receptor Molecules

Thomas Schrader (1) , Thomas Gersthagen (2) , Carsten Schmuck (2)

1 Universitätsstr. 5
2 The department of Chemistry

Integrins play a pivotal role in cell-cell adhesion, signaling and apoptosis. Many extracellular proteins use the RGD sequence (arginine-glycine-aspartate) as a key to dock onto and unlock their respective binding partners at the cell membrane (αVβ3-, aIIbß3- and the a5ß1-integrin). Here, the RGD signal is transduced into the cytoplasm and triggers a variety of biological events like blood coagulation, cell matrix binding, cell differentiation and angiogenesis. A misfunction of this recognition system causes severe diseases, rendering the RGD recognition system an attractive drug target. Inhibition of RGD-integrin interactions can be reached in two different ways, by blocking integrins with RGD-mimetics or by capping RGD-containing proteins by artificial RGD receptors. This review provides an overview over the very young history of artificial RGD receptor development, beginning with early research in arginine recognition, over the discovery of the first primitive RGD-receptor until the current state of research and future prospects.

Mots clés: Physical Sciences

Thomas Schrader, Thomas Gersthagen, Carsten Schmuck. Artificial RGD Receptor Molecules. Supramolecular Chemistry, 2010, 22 (11-12), pp.853-861. ⟨10.1080/10610278.2010.514613⟩. ⟨hal-00640229⟩