Artificial RGD receptor molecules

Abstract

Integrins play a pivotal role in cell–cell adhesion, signalling 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 (α_Vβ₃-, a_IIbβ₃- and a₅β₁-integrin). Here, the RGD signal is transduced into the cytoplasm and triggers a variety of biological events such as 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 present state of research and future prospects.

Keywords:

• RGD peptide
• integrins
• molecular recognition
• artificial receptors
• amino acids

Acknowledgement

Funding of both the Schrader and Schmuck groups by the DFG (Deutsche Forschungsgemeinschaft) is gratefully acknowledged.