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A dipeptide is an organic compound derived from two amino acids. The constituent amino acids can be the same or different. When different, two isomers of the dipeptide are possible, depending on the sequence. Several dipeptides are physiologically important, and some are both physiologically and commercially significant.
The reaction with a second amino acid allows for the ring to open, later forming an acylated unsaturated dipeptide. The reaction happens in a step-wise function which allows for the amino group to be protected and the azlactone to be produced. Catalytic hydrogenation and hydrolysis then take place in order to produce the dipeptide . [6]
These dipeptides are extremely easy to use: simply substitute a serine or threonine residue together with the preceding amino acid residue in the peptide sequence with the appropriate pseudoproline dipeptide (see the figure on your right). The native sequence is regenerated on cleavage and deprotection. [15] [16] [17]
Glycylglycine is the dipeptide of glycine, making it the simplest peptide. [1] The compound was first synthesized by Emil Fischer and Ernest Fourneau in 1901 by boiling 2,5-diketopiperazine (glycine anhydride) with hydrochloric acid. [2] Shaking with alkali [1] and other synthesis methods have been reported. [3]
Arginylglycylaspartic acid (RGD) is the most common peptide motif responsible for cell adhesion to the extracellular matrix (ECM), found in species ranging from Drosophila to humans.
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