Names | |
---|---|
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
| |
Other names
Dynorphin B-29; Dynorphin B (1–29)
| |
Identifiers | |
3D model (
JSmol)
|
|
ChemSpider | |
PubChem
CID
|
|
CompTox Dashboard (
EPA)
|
|
| |
| |
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).
|
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]
Names | |
---|---|
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
| |
Other names
Dynorphin B-29; Dynorphin B (1–29)
| |
Identifiers | |
3D model (
JSmol)
|
|
ChemSpider | |
PubChem
CID
|
|
CompTox Dashboard (
EPA)
|
|
| |
| |
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).
|
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]