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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.
Peptide bond formation via dehydration reaction. When two amino acids form a dipeptide through a peptide bond, [1] it is a type of condensation reaction. [2] In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other.
A dipeptide has two amino acids. A tripeptide has three amino acids. A tetrapeptide has four amino acids. A pentapeptide has five amino acids. (e.g., enkephalin). A hexapeptide has six amino acids. (e.g., angiotensin IV). A heptapeptide has seven amino acids. (e.g., spinorphin). An octapeptide has eight amino acids (e.g., angiotensin II).
This would compete with the intended peptide coupling reaction, resulting in low yield or even complete failure to synthesize the desired peptide. [ citation needed ] Two principle protecting group schemes are typically used in solid phase peptide synthesis: so-called Boc/benzyl and Fmoc/ tert- butyl approaches. [ 2 ]
This dipeptide is then condensed with glycine by glutathione synthetase to form glutathione. [129] In chemistry, peptides are synthesized by a variety of reactions. One of the most-used in solid-phase peptide synthesis uses the aromatic oxime derivatives of amino acids as activated units.
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