|Locus||Chr. 2 p23|
|Jmol-3D images||Image 1|
|Except where noted otherwise, data are given for materials in their standard state (at 25 °C (77 °F), 100 kPa)|
|(what is: / ?)|
β-endorphin is a peptide, 31 amino acids long, resulting from processing of the precursor proopiomelanocortin (POMC). (Note, POMC also gives rise to other peptide hormones, including ACTH ( Adrenocorticotropic hormone ), as well α- and γ-MSH ( Melanocyte-Stimulating Hormone ), resulting from intracellular processing by internal enzymes known as prohormone convertases.)
It is an agonist of the opioid receptors, with evidence suggesting it serves as the endogenous ligand of the μ-opioid receptor, the same receptor to which the chemicals extracted from opium, such as morphine, have their analgesic and addictive effects (indeed, the μ-opioid receptor was named based on its most renowned ligand, morphine).
β-endorphin was discovered in camel pituitary extracts by C.H. Li and David Chung.
It is used as an analgesic in the body to numb or dull pains. That is the reason why humans start to feel better immediately after an acute physical trauma even though the symptoms are still present. The reason the pain dulls is because it binds to and activates opioid receptors. β-endorphin has approximately 80 times the analgesic potency of morphine.
- PubChem 16132316 - β-endorphin
- PubChem 3081525 - β-endorphin (1-9)
- PubChem 133304 - β-endorphin (2-9)
- β-endorphin at the US National Library of Medicine Medical Subject Headings (MeSH)