INTRO

A dipeptide is an organic molecule formed by the combination of two amino acids.

The amino acids that make up the protein can be the same or different.
Depending on the sequence, two isomers of the dipeptide are possible.
Several dipeptides have physiological significance, and several have both physiological and
commercial significance.
Aspartame, an artificial sweetener, is a well-known dipeptide .[1]

Glycylglycine is the most basic dipeptide.

Dipeptides are crystalline white solids.

Many are significantly more water-soluble than the parent amino acids. For example, the
dipeptide Ala-Gln has a solubility of 586 g/L, which is more than 10 times that of Gln (35 g/L).
Dipeptides can also have varied stabilities, such as hydrolysis.
Gln does not survive sterilizing treatments, whereas this dipeptide does.
Because dipeptides are easily hydrolyzed, their high solubility is advantageous.

The amine protecting group P and the ester are changed to free amine and carboxylic acid as a
result of this coupling reaction .[3]

The accessory functional groups of many amino acids are protected.

In most cases, coupling agents are used to activate the carboxylic acid during the condensation
of the amine and the carboxylic acid to form the peptide link .[4]