Tripeptide arginine-glycine-aspartic acid

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. 

Polymer additives can improve manufacturing processes and product quality, as they aid the formation of a continuous coating phase without any detrimental effect to the polymer. Biomedical applications of acrylic terpolymer with arginylglycylaspartic acid, i.e., a tripeptide composed of L-arginine, glycine and L-aspartic acid peptides, have been studied by Fussell and Cooper [39]. Chauhan and co-workers have investigated the biological activities of synthesised terpolymers based on p-hydroxybenzaldehyde... 

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