database / hormone
Ziconotide
also known as Prialt, ω-conotoxin MVIIA
Skeletal structure drawn from the computed atomic coordinates in PubChem CID 16135415. 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
Primary structure not characterised in the public records this index draws on. Nothing is shown rather than something invented.
A cone-snail conotoxin with three disulfide bonds and a C-terminal amide; the fold, not the linear sequence, is the active entity.
Molecular data
| molecular formula | C102H172N36O32S7 |
|---|---|
| molecular weight | 2639.2 Da (PubChem) |
| computed backbone mass | not characterised |
| length | not characterised |
| net charge (pH 7.4) | not characterised |
| mean hydropathy | not characterised |
| half-life | not characterised |
| delivery route | intrathecal |
| PubChem CID | 16135415 |
| PDB | not characterised |
| UniProt parent | not characterised |
Mechanism
Selective N-type (Cav2.2) calcium channel blocker.
Reported targets: Cav2.2
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.
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 |
|---|---|
| analgesia in trials | Pharmaceutical Peptides: From Synthesis and Mechanistic Pharmacology to Futu… Pharmaceuticals (Basel, Switzerland) 2026 |
Registered trials
| NCT | title | status | phase |
|---|---|---|---|
| NCT01992562 | Single Shot Intrathecal Ziconotide for Painful Neuropathy or Myelopathy | WITHDRAWN | PHASE4 |
| NCT00076544 | Ziconotide Effectiveness and Safety Trial in Patients With Chronic Severe Pain | COMPLETED | PHASE3 |
| NCT03942848 | Intrathecal Ziconotide Antalgic Efficacy for Severe Refractory Neuropathic | UNKNOWN | PHASE3 |
| NCT01373983 | Intrathecal Bolus Doses of Ziconotide | COMPLETED | PHASE4 |
| NCT00996983 | Safety and Activity Study of Intrathecally Administered Ziconotide for Neuropathic Pain in P | UNKNOWN | PHASE2 |
Literature (7)
Pharmaceutical Peptides: From Synthesis and Mechanistic Pharmacology to Future Biologic Therapeutics — Pharmaceuticals (Basel, Switzerland) 2026
abstract not reproduced — this record is not open-access, so it is linked rather than copied.
publisher record ↗ · PMID 42356430 · DOI 10.3390/ph19060811
Pharmacological Inhibition of Cav2.2 Channels by Recombinant Phα1β Toxin (CTK01512-2) — Basic & clinical pharmacology & toxicology 2026
Phα1β is a peptide toxin originally isolated from the venom of the Brazilian spider Phoneutria nigriventer, known for its potent analgesic effects in preclinical models of acute and chronic pain. However, clinical translation has been limited by production constraints. A recombinant analogue, CTK01512-2, was developed and has demonstrated antinociceptive efficacy comparable to the native toxin in diverse experimental models. In this study, we examined the effects of CTK01512-2 on N-type voltage-gated calcium channels (Cav2.2) expressed in transiently transfected HEK-293 cells and confirmed its antinociceptive action in a mouse model of neuropathic pain. CTK01512-2 induced a partial (~50%) and reversible inhibition of Cav2.2-mediated calcium currents, with a calculated half-maximal inhibitory concentration (IC50) of 3.94 nM. In contrast to ω-conotoxin MVIIA, a clinically approved irrevers…
open access ↗ · PMID 42383434 · DOI 10.1111/bcpt.70268
Intrathecal Ziconotide Long-Term Management in Chronic Postamputation Pain — Case reports in anesthesiology 2026
abstract not reproduced — this record is not open-access, so it is linked rather than copied.
publisher record ↗ · PMID 42548796 · DOI 10.1155/cria/9977830
Functional crosstalk between neuropeptide FF system and N-type voltage-gated calcium channels in ziconotide-mediated antinociception in mice — Psychopharmacology 2026
abstract not reproduced — this record is not open-access, so it is linked rather than copied.
publisher record ↗ · PMID 41910723 · DOI 10.1007/s00213-026-07053-4
Antioxidant, Anti-Inflammatory and Anticancer Peptides from Extreme Marine Environments — Antioxidants (Basel, Switzerland) 2026
Marine organisms have proven to be excellent sources of bioactive natural products with potential therapeutic applications. To date, seventeen marine-derived molecules are on the market for the treatment of human diseases, mainly cancer. While multiple bioactivities of marine compounds have been consecutively reported, peptides represent promising candidates for these applications. This review focuses on peptides from marine organisms living in extreme marine environments, such as the deep ocean, polar regions, and tropical ecosystems. These are particularly promising for further bioprospecting, since their distinctive conditions have driven the evolution of unique biomolecules, as well as unique stability profile that can improve efficacy, shelf life, and performance under a wide range of industrial conditions. Ziconotide (Prialt), a neurotoxic peptide derived from the venom of a marine…
open access ↗ · PMID 42193237 · DOI 10.3390/antiox15050615
Dissecting oxidative folding of conotoxins using 3D structures of cysteine mutants predicted by AlphaFold 3: A case study of α-conotoxin RgIA, χ-conotoxin CMrVIA and ω-conotoxin MVIIA-Gly — Toxicon : official journal of the International Society on Toxinology 2025
abstract not reproduced — this record is not open-access, so it is linked rather than copied.
publisher record ↗ · PMID 40345559 · DOI 10.1016/j.toxicon.2025.108402
A Chemoenzymatic Approach To Produce a Cyclic Analogue of the Analgesic Drug MVIIA (Ziconotide) — Angewandte Chemie (International ed. in English) 2023
Ziconotide (ω-conotoxin MVIIA) is an approved analgesic for the treatment of chronic pain. However, the need for intrathecal administration and adverse effects have limited its widespread application. Backbone cyclization is one way to improve the pharmaceutical properties of conopeptides, but so far chemical synthesis alone has been unable to produce correctly folded and backbone cyclic analogues of MVIIA. In this study, an asparaginyl endopeptidase (AEP)-mediated cyclization was used to generate backbone cyclic analogues of MVIIA for the first time. Cyclization using six- to nine-residue linkers did not perturb the overall structure of MVIIA, and the cyclic analogues of MVIIA showed inhibition of voltage-gated calcium channels (CaV 2.2) and substantially improved stability in human serum and stimulated intestinal fluid. Our study reveals that AEP transpeptidases are capable of cyclizin…
open access ↗ · PMID 37148162 · DOI 10.1002/anie.202302812
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