Dynorphin B-13; Rimorphin
3D model (JSmol)
CompTox Dashboard (EPA)
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Dynorphin B, also known as rimorphin, is a form of dynorphin and an endogenous opioid peptide with the amino acid sequence Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Gln-Phe-Lys-Val-Val-Thr. Dynorphin B is generated as a proteolytic cleavage product of leumorphin, which in turn is a cleavage product of preproenkephalin B (prodynorphin).
Dynorphin B has an identical N-terminal sequence, but different C-terminal sequence to Dynorphin A. In an alanine scan of the non-glycine residues of dynorphin B, it was discovered that Tyr1 and Phe4 residues are critical for both opioid receptor affinity and κ-opioid receptor agonist potency, Arg6 and Arg7 promote κ-opioid affinity and Lys10 contributes to the opioid receptor affinity.
Inducers of Dynorphin B
Cannabinoid CP55,940 and △9-tetrahydrocannabinol (△9-THC) can induce the release of dynorphin B, which in return acts as an agonist of κ-opioid receptors, resulting in the production of antinociception. Similarly, Tyr-D-Arg-Phe-Sar (TAPS) is capable of promoting a release of dynorphin B through the simulation of μ1-opioid receptors, causing a production of antinociception. The antinociceptive effect produced by dynorphin B allows for spinal analgesia.
- Dynorphin B - Compound Summary, PubChem.
- Paul V. Malven (12 January 1993). Mammalian Neuroendocrinology. CRC Press. p. 70. ISBN 978-0-8493-8757-9. Retrieved 22 April 2012.
- Joshi, Anand A.; Murray, Thomas F.; Aldrich, Jane V. (September 2017). "Alanine scan of the opioid peptide dynorphin B amide". Biopolymers. 108 (5): e23026. doi:10.1002/bip.23026. PMC 6003702. PMID 28464209.
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