Fibronectin tripeptide sequence

Probably the smallest sequence known to be responsible for receptor recognition is the RGD-tripeptide, initially discovered in fibronectin [143]. However, the specificity of the interaction with different integrins, the counter receptors of RGD sequences on the cell surface, is established by the flanking sequences of the RGD motif and the conformation of the tripeptide. In other words, the presentation of the RGD sequence is important for specific recognition by individual integrins. 

Recently, TTR1 fibrils have been decorated with the classic RGD tripeptide motif isolated from fibronectin, which encourages cell adhesion via integrin cell surface receptors (Gras et al., 2008). This bioactive tag was added to the TTR1 sequence which drives fibril assembly and the tag shown to be exposed on the fibril surface and accessible to cells following assembly. The RGD-modified fibrils were bioactive in a cell dissociation assay which measures the ability of fibrils to competitively bind to cells and induce cell detachment from a surface, as illustrated in Figure 19. In... 

The trIpeptIde RGD sequence (Arg-Gly-Asp), found In fibronectins and some other matrix proteins. Is recognized by several Integrlns. 

Historically, these peptides were identified by isolating domains ofinterest from naturally evolved proteins. The tripeptide RGD sequence (arginine-glycine—aspartic acid), a commonly used cell-adhesion domain, is a prime example of this. RGD was isolated in 1983 from the extracellular and plasma protein fibronectin and was identified as the minimal sequence necessary to promote cell-attachment properties (Pierschbacher and Ruoslahti 1984). Other commonly used domains include elastin-hke sequences, which are derived from the protein elastin found in connective tissue (Meyer and Chilkoti 2002), and recombinant-silks (Prince et al. 1995). Both of these peptide domains are used to confer their unique mechanical properties (i.e., resilience, elasticity, and strength) to the resulting biomaterial. 

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