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Overview
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Background
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.
In vitro: 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].
In vivo: 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].
Clinical trials: Currenlty no clinical data are available.[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.
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- Properties
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Overview