Investigating the Interaction of Cyclic RGD Peptidomimetics with α_Vβ₆ Integrin by Biochemical and Molecular Docking Studies.

ABSTRACT: The interaction of a small library of cyclic RGD (Arg-Gly-Asp) peptidomimetics with α_Vβ₆ integrin has been investigated by means of competitive solid phase binding assays to the isolated receptor and docking calculations in the crystal structure of the α_Vβ₆ binding site. To this aim, a rigid receptor-flexible ligand docking protocol has been set up and then applied to predict the binding mode of the cyclic RGD peptidomimetics to α_Vβ₆ integrin. Although the RGD interaction with α_Vβ₆ recapitulates the RGD binding mode observed in α_Vβ₃, differences between the integrin binding pockets can strongly affect the ligand binding ability. In general, the peptidomimetics exhibited IC₅₀ values for integrin α_Vβ₆ (i.e., the con

SUBMITTER: Civera M 

PROVIDER: S-EPMC5664067 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature