Insights into the Binding of Cyclic RGD Peptidomimetics to α₅β₁ Integrin by using Live-Cell NMR And Computational Studies.

ABSTRACT: The interaction of a small library of cyclic DKP-RGD peptidomimetics with α₅β₁ integrin has been investigated by means of an integrated experimental and computational approach. Bioaffinity NMR techniques, including saturation transfer difference (STD) and transferred NOESY, were applied to the ligands in a suspension of intact MDA-MB-231 breast cancer cells, in which integrin α₅β₁ is highly expressed. The NMR data were compared with the docking calculations of the RGD ligands in the crystal structure of the α₅β₁ binding site, and were integrated with competitive binding assays to the purified α₅β₁ integrin. Ligand binding epitopes involve protons of both the RGD moiety and the DKP scaffold, although the

SUBMITTER: Guzzetti I 

PROVIDER: S-EPMC5288746 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature