database / hormone
Dynorphin A (1-13)
Skeletal structure drawn from the computed atomic coordinates in PubChem CID 25075996. Carbons are implicit vertices; hydrogens on carbon are suppressed, as in any structural formula. Nothing here is estimated — every atom sits where PubChem placed it.
Research reference only. The observations below are recorded in the cited literature. Nothing here is advice or a recommendation, and no dosing information is published on this site.
Sequence
YGGFLRRIRPKLK
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys
- hydrophobic
- positive
- negative
- polar
- aromatic
- glycine
- proline
- cysteine
Computed backbone mass 1603.98 Da agrees with PubChem's reported 1604 Da (Δ 0.02 Da). Two independent sources agree on the primary structure.
Molecular data
| molecular formula | C75H126N24O15 |
|---|---|
| molecular weight | 1604 Da (PubChem) |
| computed backbone mass | 1603.98 Da |
| length | 13 residues |
| net charge (pH 7.4) | +5 |
| mean hydropathy | -0.78 |
| half-life | not characterised |
| delivery route | not characterised |
| PubChem CID | 25075996 |
| PDB | not characterised |
| UniProt parent | P01213 |
Mechanism
Kappa-opioid receptor agonist.
Reported targets: KOR
Experimental structure
No experimental structure of this peptide is deposited in the PDB. Nothing is rendered here — a predicted fold would not be a structure, and this site does not draw one.
Position in the parent protein
…PKRSSEVAGEGDGDSMGHEDLYKRYGGFLRRIRPKLKWDNQKRYGGFLRRQFKVVTRSQED…
Parent sequence from UniProt P01213. Cleaved from prodynorphin.
Reported effects
Each row is an outcome described in the literature indexed for this peptide. Reported in the cited work — not a claim, not a recommendation.
| reported outcome | where it appears |
|---|---|
| analgesic signalling | Metabolic syndrome reduces but does not eliminate the cardioprotective effec… Pflugers Archiv : European journal of physiology 2025 |
| stress-response modulation in models | Discovery of a pyridine-piperazine-based small molecule that enhances the ac… The Journal of pharmacology and experimental therapeutics 2026 |
Literature (5)
Metabolic syndrome reduces but does not eliminate the cardioprotective effect of adaptation to hypoxia: the link with changes in the opioid system — Pflugers Archiv : European journal of physiology 2025
abstract not reproduced — this record is not open-access, so it is linked rather than copied.
publisher record ↗ · PMID 41354854 · DOI 10.1007/s00424-025-03144-x
Discovery of a pyridine-piperazine-based small molecule that enhances the activity of peptidase neurolysin — The Journal of pharmacology and experimental therapeutics 2026
abstract not reproduced — this record is not open-access, so it is linked rather than copied.
publisher record ↗ · PMID 41759240 · DOI 10.1016/j.jpet.2026.103827
Structural basis of divergent substrate recognition and inhibition of human neurolysin — Scientific reports 2024
A zinc metallopeptidase neurolysin (Nln) processes diverse bioactive peptides to regulate signaling in the mammalian nervous system. To understand how Nln interacts with various peptides with dissimilar sequences, we determined crystal structures of Nln in complex with diverse peptides including dynorphins, angiotensin, neurotensin, and bradykinin. The structures show that Nln binds these peptides in a large dumbbell-shaped interior cavity constricted at the active site, making minimal structural changes to accommodate different peptide sequences. The structures also show that Nln readily binds similar peptides with distinct registers, which can determine whether the peptide serves as a substrate or a competitive inhibitor. We analyzed the activities and binding of Nln toward various forms of dynorphin A peptides, which highlights the promiscuous nature of peptide binding and shows how d…
open access ↗ · PMID 39117724 · DOI 10.1038/s41598-024-67639-w
Effects of Opioid Peptides on Changes in Lipid Metabolism in Rats Subjected to Swimming Stress — Bulletin of experimental biology and medicine 2017
abstract not reproduced — this record is not open-access, so it is linked rather than copied.
publisher record ↗ · PMID 28091903 · DOI 10.1007/s10517-017-3603-7
Purification and Biochemical Characterization of TsMS 3 and TsMS 4: Neuropeptide-Degrading Metallopeptidases in the <i>Tityus serrulatus</i> Venom — Toxins 2019
Although omics studies have indicated presence of proteases on the Tityus serrulatus venom (TsV), little is known about the function of these molecules. The TsV contains metalloproteases that cleave a series of human neuropeptides, including the dynorphin A (1-13) and the members of neuropeptide Y family. Aiming to isolate the proteases responsible for this activity, the metalloserrulase 3 and 4 (TsMS 3 and TsMS 4) were purified after two chromatographic steps and identified by mass spectrometry analysis. The biochemical parameters (pH, temperature and cation effects) were determined for both proteases, and the catalytic parameters (Km, kcat, cleavage sites) of TsMS 4 over fluorescent substrate were obtained. The metalloserrulases have a high preference for cleaving neuropeptides but presented different primary specificities. For example, the Leu-enkephalin released from dynorphin A (1-1…
open access ↗ · PMID 30935107 · DOI 10.3390/toxins11040194
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