Because dipeptides are prone to hydrolysis, the high solubility is exploited in infusions, i.e. to provide nutrition.
The two modified amino acids are then combined in the presence of a coupling agent, which facilitates formation of the amide bond: Subsequent to this coupling reaction, the amine protecting group P and the ester are converted to the free amine and carboxylic acid, respectively.
[1] Dipeptides are produced from polypeptides by the action of the hydrolase enzyme dipeptidyl peptidase.
[5] Dietary proteins are digested to dipeptides and amino acids, and the dipeptides are absorbed more rapidly than the amino acids, because their uptake involves a separate mechanism.
Dipeptides activate G-cells found in the stomach to secrete gastrin.