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Arginine-glycine-aspartic acid sequence

Thus, the arginine-glycine-aspartic acid sequence is also indicated by RGD. [Pg.507]

Xemilofiban 50 (Figure 11.13) and related compounds are peptido-mimetics based on the RGD (arginine-glycine-aspartic acid) sequence of fibrinogen... [Pg.356]

As a sidebar, it should be noted that there is a domain on the fibronectin molecule which binds to the simple peptide RGD (arginine-glycine-aspartic acid) and this has been explored as a means of interfering with the tumor adhesion process using longer, more stable, polypeptide sequences and other analogues or derivatives (Humphries et al. 1987). [Pg.234]

On such modified surfaces, some of the attached proteins are recognized by cytoskeletally associated receptors in the cell membrane. So, in the end, the extracellular substrate is mechanically connected with the intracellular cytoskele-ton, which may secrete its own adhesion proteins. Integrins, as an important class of cell receptors [63], bind to small domains on their adhesion proteins, e.g., the oligopeptide sequence arginine-glycine-aspartic acid (RGD) that is common in fibronectin [64],... [Pg.170]

RGD arginine-glycine-aspartic acid peptide sequence... [Pg.815]

Fig. 2. Schematic representation (not to scale) of the amino acid sequence of a Type I collagen. A Type I collagen consists of two identical of cd(I) and one unique a2(I) chains whose combination produces a triple helical structure 300 nm long and 0.5 nm thick, with a periodicity of 67 nm. Arginine-glycine-aspartic acid adhesive peptides ( ) start at peptide sequence 1083 in the cd(I) chain as well as at 772, 822, and 1005 in the a2(l) chain. (The schematic was redrawn using information obtained from the following references Ayad et al, 1994 Mathews and van Holde, 1990 and Darnell et al, 1990.)... Fig. 2. Schematic representation (not to scale) of the amino acid sequence of a Type I collagen. A Type I collagen consists of two identical of cd(I) and one unique a2(I) chains whose combination produces a triple helical structure 300 nm long and 0.5 nm thick, with a periodicity of 67 nm. Arginine-glycine-aspartic acid adhesive peptides ( ) start at peptide sequence 1083 in the cd(I) chain as well as at 772, 822, and 1005 in the a2(l) chain. (The schematic was redrawn using information obtained from the following references Ayad et al, 1994 Mathews and van Holde, 1990 and Darnell et al, 1990.)...
Bone sialoprotein, osteopontin, and osteocalcin are synthesized and deposited as the mineralization process begins and mineral nodules form (Stein and Lian, 1993). Bone sialoprotein contains the cell-adhesive arginine-glycine-aspartic acid peptide sequence and may thus mediate osteoblast adhesion on the extracellular matrix (Gehron-Robey, 1989). Osteocalcin, a calcium-binding protein, interacts with hydroxyapatite and is thought to mediate coupling of bone resorption (by osteoclasts) and bone formation (by osteoblasts and/or osteocytes) (Stein and Lian, 1993). [Pg.138]

Fig. 8. Schematic representation of protein-mediated cell adhesion on biomaterial surfaces. Biomaterial surface properties (such as hydrophilicity/hydrophobicity, topography, energy, and charge) affect subsequent interactions of adsorbed proteins these interactions include but are not limited to adsorbed protein type, concentration, and conformation. Changes in protein-surface interactions may alter accessibility of adhesive domains (such as the peptide sequence arginine-glycine-aspartic acid) to cells (such as osteoblasts, fibroblasts, or endothelial cells) and thus modulate cellular adhesion. (Adapted and redrawn from Schakenraad, 1996.)... Fig. 8. Schematic representation of protein-mediated cell adhesion on biomaterial surfaces. Biomaterial surface properties (such as hydrophilicity/hydrophobicity, topography, energy, and charge) affect subsequent interactions of adsorbed proteins these interactions include but are not limited to adsorbed protein type, concentration, and conformation. Changes in protein-surface interactions may alter accessibility of adhesive domains (such as the peptide sequence arginine-glycine-aspartic acid) to cells (such as osteoblasts, fibroblasts, or endothelial cells) and thus modulate cellular adhesion. (Adapted and redrawn from Schakenraad, 1996.)...
Fig. 8 Endothelialization on PEU surfaces modified by MPEO-derived SMAs. A Un-treated PEU surface (control) imaged by optical microscopy [OM] B MPEO-OH (without functional endgroups at the end of PEG spacers) as SMA imaged by scanning electronic microscopy [SEM] basic amino acid (typically lysine)-functionalized MPEO derivatives as SMA by C OM and D SEM arginine-glycin-aspartic acid tri-peptide sequence [RGD]-functionalized MPEO derivatives as SMA by E OM and F SEM [82,83]. Reproduced from [180,181]... Fig. 8 Endothelialization on PEU surfaces modified by MPEO-derived SMAs. A Un-treated PEU surface (control) imaged by optical microscopy [OM] B MPEO-OH (without functional endgroups at the end of PEG spacers) as SMA imaged by scanning electronic microscopy [SEM] basic amino acid (typically lysine)-functionalized MPEO derivatives as SMA by C OM and D SEM arginine-glycin-aspartic acid tri-peptide sequence [RGD]-functionalized MPEO derivatives as SMA by E OM and F SEM [82,83]. Reproduced from [180,181]...
RGD A signature peptide sequence arginine-glycine-aspartic acid foi... [Pg.20]

On the nanoscale, the surface chemistry of the scaffold must recreate the important cell-ECM properties of adhesion and control. Biocompatibility of the scaffold surface with cells is key for allowing adhesion and migration of cells. The amino acid sequence of arginine-glycine-aspartic acid (RGD) has been identified on fibronectin and other ECM glycoproteins as a key adhesion domain, and the design of synthetic scaffolds incorporating the peptide has been successful... [Pg.3120]

RGD is the one-letter amino acid code abbreviation for arginine-glycine-aspartic acid. Peptide sequences containing a RGD motif are used as specific ligands to mediate cell adhesion. [Pg.256]


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See also in sourсe #XX -- [ Pg.379 ]




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Arginine acidity

Arginine aspartate

Arginine-glycine-aspartate

Arginine-glycine-aspartic acid

Argininic acid

Aspartic acid

Aspartic acid/aspartate

Glycine, acidity

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