Probing the bimolecular interface between RGD-containing ligands and the α_vβ₃ integrin receptor - An important therapeutic target. Part 2

Identification of the binding site for RGD-containing ligands in the osteoclastic α_vβ₃ integrin receptor will provide important insight to understand mechanism of action and help in rational design of selective inhibitors of bone resorption as novel therapeutics. To this end, photoaffinity scanning (PAS) approach employing small bioactive RGD-containing peptides and echistatin analogs carrying both a benzophenone photophore and a radioiodine tag were designed and synthesized. Part 2 reports on the utilization of PAS to probe the receptor-ligand bimolecular interface and characterized the principal RGD-binding site in the integrin receptor.