arginineglycineaspartic

Arginineglycineaspartic, commonly abbreviated Arg-Gly-Asp or RGD, is a short tripeptide comprising arginine (R), glycine (G), and aspartic acid (D). This motif occurs in a variety of extracellular matrix proteins, including fibronectin, vitronectin, and laminin, where it contributes to cell–matrix interactions.

RGD serves as a recognition sequence for several integrin receptors on the surface of cells. Binding of the RGD motif to integrins such as αvβ3 and α5β1 mediates cell adhesion, spreading, and signaling; thus it influences cell migration, proliferation, and survival. The affinity of RGD interactions depends on the peptide's context and conformation; cyclic variants (cRGD) often exhibit higher affinity and stability.

In biomaterials and tissue engineering, RGD motifs are widely used to promote cell attachment by grafting peptides onto surfaces, scaffolds, or hydrogels. Cyclic RGD peptides and multivalent formats are used to enhance targeting and potency. RGD-based approaches also appear in drug delivery and research into integrin-mediated processes; inhibitors derived from the motif have been explored for anti-angiogenic therapies, though results vary.

The RGD motif was identified in early extracellular matrix studies as a key determinant of cell adhesion, representing one of the best-characterized peptide recognition sequences in cell biology.