White to off-white powder
Arg-Gly-Asp has been used:
- to saturate the cell surface Arg-Gly-Asp (RGD) receptors and inhibit marrow stromal cell (MSC) attachment to peptide modified hydrogel
- in adhesion assay
- in inhibition assay to confirm the β1-integrin-dependency of cell adhesion
- in textile fabrication and RGD textile functionalization
- to engineer a population of human dermal fibroblasts with impaired migration
- to modify glass substrate and evaluate the behavior of human bone marrow mesenchymal stem cells (hBM-MSCs)
- in the cell culture of human mammary epithelial cells
ChEBI: Arg-Gly-Asp is an oligopeptide.
Arg-Gly-Asp (RGD) is an integrin binding site, which belongs to the class of adhesive proteins. It functions as a brain tumor targeting ligand.
synthetic peptides containing the arginine-glycine-aspartate (rgd) were extensively used as inhibitors of integrin-ligand interactions in studies of cell adhesion, migration, growth and differentiation, since the rgd motif is an integrin-recognition motif found in many ligands.
Primary sequence involved with the binding of proteins to cell surfaces
rgd peptide can induce apoptosis in the absence of signals and integrin-mediated cell clustering. previous study demonstrates that rgd peptides promote apoptosis through activation of conformation changes enhancing pro-caspase-3 activation and autoprocessing [1].
anima study suggested that the rgd-4c-fitc-peptide bound to both endothelial and tumor cells in vivo and that peptide targeting should allow the delivery of therapeutic drugs to both endothelial and tumor cells [2].
integrin-ligand interaction
[1] nature. 1999 feb 11;397(6719):534-9.rgd peptides induce apoptosis by direct caspase-3 activation. buckley cd1, pilling d, henriquez nv, parsonage g, threlfall k, scheel-toellner d, simmons dl, akbar an, lord jm, salmon m.
[2] cancer res. 2002 sep 15;62(18):5139-43. arginine-glycine-aspartic acid (rgd)-peptide binds to both tumor and tumor-endothelial cells in vivo. zitzmann s1, ehemann v, schwab m.
