RGD Cyclopeptide Equipped with a Lysine‐Engaging Salicylaldehyde Showing Enhanced Integrin Affinity and Cell Detachment Potency. Issue 19 (27th February 2023)

• Record Type: Journal Article
• Authors: Sacco, Giovanni; Arosio, Daniela; Paolillo, Mayra; Gloger, Andreas; Scheuermann, Jörg; Pignataro, Luca; Belvisi, Laura; Dal Corso, Alberto; Gennari, Cesare
• Is Part Of: Chemistry. Volume 29:Issue 19(2023)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2023-02-27
• Subjects: aldehydes -- cell adhesion -- covalent inhibitors -- integrins -- peptidomimetics; Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.202203768
• Languages: English
• ISSNs: 0947-6539

Abstract

Abstract: Salicylaldehyde (SA) derivatives are emerging as useful fragments to obtain reversible‐covalent inhibitors interacting with the lysine residues of the target protein. Here 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 is reported. Abstract : A RGD cyclopeptide with a C‐terminal salicylaldehyde tag shows a higher affinity for integrin αV β3 than control compounds. Covalent docking studies ascribe this increased affinity to a plausible formation of an intermolecular imine bond between salicylaldehyde and a Lys residue on the β3 integrin subunit.