Arg-Gly-Asp

The hydantoin moiety has been utilized as a biostere for the peptide linkage, transforming a peptide lead into an orally available drug candidate. Therefore, an Arg-Gly-Asp-Ser tetrapeptide (18) lead structure was modified to a non-peptide RGD mimetic as an orally active fibrinogen receptor antagonist 19. ° ... 

Horton MA, Taylor ML, Arnett TR et al (1991) Arg-Gly-Asp (RGD) peptides and the anti-vitronectin receptor antibody 23C6 inhibit dentine resorption and cell spreading by osteoclasts. Exp Cell Res 195 368-375... 

S. L, Arnaout, M. A. Crystal struemre of the extracellular segment of integrin OvPs in complex with an Arg-Gly-Asp ligand. Science 2002, 296,151-155. 

Helfrich MH, Nesbitt SA, Dorey EL, Horton MA (1992) Rat osteoclasts adhere to a wide range of RGD (Arg-Gly-Asp) peptide-containing proteins, including the bone sialoproteins and fibronectin, via a beta 3 integrin. J Bone Miner Res 7 335-343... 

Technetium-labeled peptides and proteins have been investigated as potential thrombus-imaging agents. Complex 70, which combines 99mTc with the tripeptide motif Arg-Gly-Asp, binds GP Iib/IIIa recep-... 

The binding of integrins to certain ligands is mediated by a short amino acid sequence. Thus, the binding site for fibronectin is confined to a sequence of four amino acid residues, Arg-Gly-Asp-Ser (RGDS) (R7). Synthetic peptides containing the RGDS sequence prevented adhesion of cells to fibronectin (B4, R7) and also inhibited metastasis formation in animal models (B4, R7). 

Gyongyossy-Issa MI, Muller W, Devine DV. The covalent coupling of Arg-Gly-Asp-containing peptides to liposomes purification and biochemical function of the lipopeptide. Arch Biochem Biophys 1998 353(1) 101-108. 

Hart SL, Knight AM, Harbottle RP, et al. Cell binding and intemaUzation by filamentous phage displaying a cyclic Arg-Gly-Asp-containing peptide. J Biol Chem 1994 269(17) 12468-12474. 

Although the single amino acids cannot bind the adhesion receptors on cells, they provide other ehemieal functional groups which may improve the adsorption of eell adhesion-mediating molecules on the material surface. Similar efifeet was observed on ion-implanted polyethylene grafted with the Arg-Gly-Asp (RGD)... 

The domain structure in fibronectins is made up of a few types of peptide module that are repeated numerous times. Each of the more than 50 modules is coded for by one exon in the fibronectin gene. Alternative splicing (see p. 246) of the hnRNA transcript of the fibronectin gene leads to fibronectins with different compositions. The module that causes adhesion to cells contains the characteristic amino acid sequence -Arg-Gly-Asp-Ser-. It is these residues that enable fibronectin to bind to cell-surface receptors, known as integrins. 

M. Aumailley, M. Gurrath, G. Muller, J. Calvete, R. TimpI, H. Kessler, Arg-Gly-Asp constrained within cyclic pentapeptides, strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment PI, FEBS. Lett. 291(1) (1991) 50-54. 

When H-Cys(Acm)-Arg-Gly-Asp-Phe-Cys(Acm)-NH2, prepared from the same protected peptide resin by HF treatment, was subjected to I2 oxidation in soln, the peptide and other reagents could not be separated, and the desired product was not obtained. 

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