Neoendorphin
Neoendorphins are a group of endogenous opioid peptides derived from the proteolytic bond cleavage, cleavage of prodynorphin. They include alpha-Neoendorphin, α-neoendorphin and beta-Neoendorphin, β-neoendorphin. The α-neoendorphin is present in greater amounts in the brain than β-neoendorphin. Both are products of the dynorphin gene, which also expresses dynorphin A, dynorphin A-(1-8), and dynorphin B. These opioid neurotransmitters are especially active in Central Nervous System receptors, whose primary function is pain sensation. These peptides all have the consensus amino acid sequence of Try-Gly-Gly-Phe-Met (met-enkephalin) or Tyr-Gly-Gly-Phe-Leu ( leu-enkephalin). Binding of neoendorphins to opioid receptors (OPR), in the dorsal root ganglion (DRG) neurons results in the reduction of time of calcium-dependent action potential. The α-neoendorphins bind OPRD1(delta), OPRK1(kappa), and OPRM1 (mu) and β-neoendorphin bind OPRK1. Types See also * Endorphin References< ...
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Beta-Neoendorphin
β-Neoendorphin is an endogenous opioid peptide with a nonapeptide structure and the amino acid sequence tyrosine, Tyr-glycine, Gly-Gly-phenylalanine, Phe-leucine, Leu-arginine, Arg-lysine, Lys-Tyr-proline, Pro (YGGFLRKYP). β-Neoendorphins (β-NEP) have the capability to stimulate wound healing by accelerating keratinocyte migration. This is achieved by β-NEP's activation of MAPK, mitogen-activated protein kinase (MAPK) and extracellular signal-regulated kinases 1 and 2 (ERK 1 and ERK 2); along with the upregulation of matrix metalloproteinase 2 and 9 (MMP2, MMP-2 and MMP9, MMP-9). Wound healing by β-NEP results in migration without consequences on proliferation in human keratinocytes. See also * Neoendorphin References

Opioid peptides {{biochemistry-stub ...
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