Dipeptide

A dipeptide is a kind of organic compound (and therefore a kind of molecule).[1] A dipeptide is made up of only two amino acids: one amino acid on each side of a peptide bond. A dipeptide can be made from two different amino acids or by two amino acids of the same kind. A peptide bond will be in between the two amino acids.

Skeletal formula of Gly-Gly. The peptide bond is between the carbon that is double bonded to the oxygen, and the nitrogen.

Gly-Gly, or Glycylglycine is a dipeptide and also the simplest peptide. It is the dipeptide of Glycine.[2]

List of dipeptides

Some of the dipeptides are

  • Acetylcarnosine, cataract prevention[3]
  • Advantame
  • Ala-Gln, infusion[4]
  • Alafosfalin
  • Alanyl-glutamine
  • Aloxistatin
  • Andrimid
  • Anserine are highly concentrated in muscle and brain tissues. They are used in sports medicines.[3]
      • Homoanserine, found in the brain and muscles of mammals
  • Argininosuccinic acid
  • BNC-210
  • Carnosine are highly concentrated in muscle and brain tissues. They are used in sports medicines.[3]
  • DAPT (chemical)
  • Diphenylalanine is a well-known building block in peptide nanotechnology
  • E-64
  • Gly-Tyr, infusion[4]
  • Glycylglycine
  • Hypoglycin B
  • imidazole-dipeptide[5] (related page Imidazole)
  • Kyotorphin is a neuroactive dipeptide which plays a role in pain regulation in the brain.
  • Melphalan flufenamide
  • Neotame
  • Val-Tyr, antihypertensive[3]
  • Balenine (or ophidine) has been identified in the muscles of several species of mammal (including man), and the chicken.
  • Glorin is a chemotactic dipeptide for the slime mold Polysphondylium violaceum.
  • Barettin is a cyclic dipeptide from the marine sponge Geodia barretti.
  • Pseudoproline
  • Dialanine is commonly used as a model in molecular dynamics.
  • Xenortides, isolated from the bacterium Xenorhabdus nematophila

Related page

References
  1. https://www.bionity.com/en/encyclopedia/Dipeptide.html#:~:text=A%20dipeptide%20is%20a%20molecule,by%20a%20single%20peptide%20bond. Bionity.com. Retrieved 2023-02-25
  2. https://onlinelibrary.wiley.com/doi/abs/10.1002/anie.201702425. Wiley Online Library. Retrieved 2023-02-26
  3. Yagasaki M, Hashimoto S (November 2008). "Synthesis and application of dipeptides; current status and perspectives". Applied Microbiology and Biotechnology. 81 (1): 13–22. doi:10.1007/s00253-008-1590-3. PMID 18795289.
  4. Fürst P, Pogan K, Stehle P (1997). "Glutamine dipeptides in clinical nutrition". Nutrition. 13 (7–8): 731–7. doi:10.1016/S0899-9007(97)83035-3. PMID 9263278.
  5. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7912684/. National Institutes of Health. Retrieved 2023-02-25




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