Leumorphin
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| IUPAC name
L-Tyrosylglycylglycyl-L-phenylalanyl-L-leucyl-L-arginyl-L-arginyl-L-glutaminyl-L-phenylalanyl-L-lysyl-L-valyl-L-valyl-L-threonyl-L-arginyl-L-seryl-L-glutaminyl-L-α-glutamyl-L-α-aspartyl-L-prolyl-L-asparaginyl-L-alanyl-L-tyrosyl-L-serylglycyl-L-α-glutamyl-L-leucyl-L-phenylalanyl-L-α-aspartyl-L-alanine
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| Other names
Dynorphin B-29; Dynorphin B (1–29)
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| Identifiers | |
3D model (JSmol)
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PubChem CID
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CompTox Dashboard (EPA)
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| Properties | |
| C161H236N42O48 | |
| Molar mass | 3527.85 g/mol |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Leumorphin, also known as dynorphin B1–29, is a naturally occurring endogenous opioid peptide.[1][2][3] Derived as a proteolytic cleavage product of residues 226-254 of prodynorphin (preproenkephalin B),[4][5] leumorphin is a nonacosapeptide (29 amino acids in length) and has the sequence Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Gln-Phe-Lys-Val-Val-Thr-Arg-Ser-Gln-Glu-Asp-Pro-Asn-Ala-Tyr-Ser-Gly-Glu-Leu-Phe-Asp-Ala. It can be further reduced to dynorphin B (dynorphin B-13) and dynorphin B-14 by pitrilysin metallopeptidase 1 (formerly referred to as "dynorphin-converting enzyme"), an enzyme of the endopeptidase family.[6][7][8] Leumorphin behaves as a potent and selective κ-opioid receptor agonist, similarly to other endogenous opioid peptide derivatives of prodynorphin.[9][10]
See also
References
- ^ Schwarzer C (September 2009). "30 years of dynorphins—new insights on their functions in neuropsychiatric diseases". Pharmacology & Therapeutics. 123 (3): 353–370. doi:10.1016/j.pharmthera.2009.05.006. PMC 2872771. PMID 19481570.
- ^ Nakao K, Suda M, Sakamoto M, et al. (December 1983). "Leumorphin is a novel endogenous opioid peptide derived from preproenkephalin B". Biochemical and Biophysical Research Communications. 117 (3): 695–701. doi:10.1016/0006-291X(83)91653-4. PMID 6689399.
- ^ Suda M, Nakao K, Sakamoto M, et al. (August 1984). "Leumorphin is a novel endogenous opioid peptide in man". Biochemical and Biophysical Research Communications. 123 (1): 148–155. doi:10.1016/0006-291X(84)90392-9. PMID 6548137.
- ^ Leon F. Tseng (1 September 1995). Pharmacology of Opioid Peptides. CRC Press. p. 171. ISBN 978-3-7186-5632-5. Retrieved 22 April 2012.
- ^ Nock B, Giordano AL, Cicero TJ, O'Connor LH (August 1990). "Affinity of drugs and peptides for U-69,593-sensitive and -insensitive kappa opiate binding sites: the U-69,593-insensitive site appears to be the beta endorphin-specific epsilon receptor". The Journal of Pharmacology and Experimental Therapeutics. 254 (2): 412–9. PMID 2166790.
- ^ Devi L, Gupta P, Fricker LD (January 1991). "Subcellular localization, partial purification, and characterization of a dynorphin processing endopeptidase from bovine pituitary". Journal of Neurochemistry. 56 (1): 320–9. doi:10.1111/j.1471-4159.1991.tb02598.x. PMID 1670956.
- ^ Berman YL, Juliano L, Devi LA (October 1995). "Purification and characterization of a dynorphin-processing endopeptidase". The Journal of Biological Chemistry. 270 (40): 23845–50. doi:10.1074/jbc.270.40.23845. PMID 7559562.
- ^ Mzhavia N, Berman YL, Qian Y, Yan L, Devi LA (May 1999). "Cloning, expression, and characterization of human metalloprotease 1: a novel member of the pitrilysin family of metalloendoproteases". DNA and Cell Biology. 18 (5): 369–80. doi:10.1089/104454999315268. PMID 10360838.
- ^ Suda M, Nakao K, Yoshimasa T, et al. (September 1984). "Human leumorphin is a potent, kappa opioid receptor agonist". Neuroscience Letters. 50 (1–3): 49–52. doi:10.1016/0304-3940(84)90460-9. PMID 6149506. S2CID 42419724.
- ^ Inenaga K, Nagatomo T, Nakao K, Yanaihara N, Yamashita H (January 1994). "Kappa-selective agonists decrease postsynaptic potentials and calcium components of action potentials in the supraoptic nucleus of rat hypothalamus in vitro". Neuroscience. 58 (2): 331–40. doi:10.1016/0306-4522(94)90039-6. PMID 7908725. S2CID 24631286.