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Neoendorphin

Class of opioid peptides

Neoendorphins are a group of endogenous opioid peptides derived from the proteolytic cleavage of prodynorphin. They include α-neoendorphin and 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 A1-8, and dynorphin B. These opioid neurotransmitters are especially active in CNS receptors, whose primary function is pain sensation. These peptides all have the consensus amino acid sequence of Tyr-Gly-Gly-Phe-Met (met-enkephalin) or Tyr-Gly-Gly-Phe-Leu (leu-enkephalin). Binding of neoendorphins to opioid receptors, in the dorsal root ganglion (DRG) neurons results in the reduction of time of calcium-dependent action potential. The α-neoendorphins binds to μ-opioid, δ-opioid, κ-opioid receptor (KOR), cand β-neoendorphin binds to KOR.

01Types

Sequence Molecular Formula
α-neoendorphin H-Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro-Lys-OH C60H89N15O13
β-neoendorphin H-Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro-OH C54H77N13O12
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Sources and credits

This article is adapted from the Wikipedia article Neoendorphin, written by its contributors and licensed under CC BY-SA 4.0. Fathomly has changed the layout, removed citation markers, navigation and maintenance notices, and adjusted punctuation. This adapted version is shared under the same license. For references, see the original article.

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