Dipeptide

A dipeptide is an organic compound derived from two amino acids. The amino acids can be the same or different. When different, two isomers of the dipeptide are possible, depending on the sequence. Similar descriptions apply to tripeptide (three amino acid residues, two peptide bonds), tetrapeptide, and so on; longer chains are called oligopeptide, polypeptide, protein.

Glycylglycine is the simplest dipeptide.

Production

Synthetic dipeptides

Dipeptides are produced by coupling amino acids. The amino group on one amino acid is rendered non-nucleophilic (P in eq) and the carboxylic acid group in the second amino acid is deactivated as its methyl ester. The two modified amino acids are then combined in the presence of a coupling agent, which facilitates formation of the amide bond:

RCH(NHP)CO2H + R'CH(NH2)CO2CH3RCH(NHP)C(O)NH(CHR')CO2CH3 + H2O

Subsequent to this coupling reaction, the amine protecting group P and the ester are converted to the free amine and carboxylic acid, respectively.[1]

For many amino acids, the ancillary functional groups are protected. The condensation of the amine and the carboxylic acid to form the peptide bond generally employs coupling agents to activate the carboxylic acid.[2]

The Bergmann azlactone peptide synthesis is a classic organic synthesis for the preparation of dipeptides.[3]

Biosynthesis

Dipeptides are produced from polypeptides by the action of the hydrolase enzyme dipeptidyl peptidase.[4] 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.

Examples

One amino acid, two peptide bonds

In this usage, X dipeptide is taken literally: One amino acid X is equipped with two minimal peptide bonds: The C terminus COOH becomes COCH3, the N terminus NH2 becomes NHCH3. For instance, alanine dipeptide is CH3CONHCH(CH3)CONHCH3.[5]

References

  1. Subirós-Funosas, Ayman El-Faham, Fernando Albericio (2013). "Low-epimerization Peptide Bond Formation with Oxyma Pure: Preparation of Z-L-Phg-Val-OMe". Org. Synth. 90: 306. doi:10.15227/orgsyn.090.0306.
  2. Jean-Simon Suppo, Renata Marcia de Figueiredo, Jean-Marc Campagne (2015). "Dipeptide Syntheses via Activated α-Aminoesters". Org. Synth. 92: 296. doi:10.15227/orgsyn.092.0296.
  3. Bergmann, M. et al., Ann. 449, 277 (1926); "Bergmann Azlactone Peptide Synthesis"
  4. Steane, Richard. "Hydrolysis of a dipeptide". BioTopics. Retrieved 28 July 2014.
  5. Head-Gordon, Teresa; Head-Gordon, Martin; Frisch, Michael J.; Brooks, Charles; Pople, John (2009). "A theoretical study of alanine dipeptide and analogs". International Journal of Quantum Chemistry. 36: 311. doi:10.1002/qua.560360725.


This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.