Leu-Enkephalin

Leu-Enkephalin is a naturally occurring opioid peptide that is found in the brain and spinal cord. It is one of the two forms of enkephalin, the other being Met-Enkephalin. Leu-Enkephalin is a pentapeptide, meaning it is composed of five amino acids. Its sequence is Tyr-Gly-Gly-Phe-Leu.

Structure and Function[edit | edit source]

Leu-Enkephalin is derived from the proenkephalin gene and is released by the body in response to pain or stress. It functions by binding to opioid receptors in the brain and spinal cord, which inhibits the release of GABA. This results in an analgesic, or pain-relieving, effect.

The structure of Leu-Enkephalin is characterized by its five amino acids. The first, tyrosine, is an aromatic amino acid that is often involved in protein-protein interactions. The next two, glycine, are the smallest amino acids and provide flexibility to the peptide chain. The fourth, phenylalanine, is another aromatic amino acid that contributes to the overall structure of the peptide. The final amino acid, leucine, is a hydrophobic amino acid that helps to stabilize the peptide.

Clinical Significance[edit | edit source]

Due to its analgesic properties, Leu-Enkephalin has been studied for its potential use in pain management. However, its short half-life in the body has limited its therapeutic use. Researchers are currently exploring ways to increase its stability and bioavailability.

In addition to its role in pain management, Leu-Enkephalin has also been implicated in various neurological disorders, including Parkinson's disease, Alzheimer's disease, and schizophrenia. Further research is needed to fully understand the role of this peptide in these conditions.