RGD cyclopeptide equipped with a lysine-engaging salicylaldehyde shows enhanced integrin affinity and cell detachment potency

Salicylaldehyde (SA) derivatives are emerging as useful fragments to obtain reversible-covalent inhibitors interacting with lysine residues of the target protein. Here we report on the SA installation at the C terminus of an integrin-binding cyclopeptide, leading to enhanced ligand affinity for the receptor as well as stronger biological activity in cultured glioblastoma cells.