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Contents

   



(Top)
 


1 Hypervariability  





2 Disulfide connectivities  





3 Types and biological activities  



3.1  Alpha  





3.2  Delta, kappa, and omega  





3.3  Mu







4 See also  





5 References  





6 External links  














Conotoxin






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From Wikipedia, the free encyclopedia
 


This article is missing information about genetic and architectural classification (ConoServer and PMC4278219). Please expand the article to include this information. Further details may exist on the talk page. (April 2019)

Alpha conotoxin precursor

α-Conotoxin PnIB from C. pennaceus, disulfide bonds shown in yellow. From the University of Michigan's Orientations of Proteins in Membranes database, PDB: 1AKG​.

Identifiers

Symbol

Toxin_8

Pfam

PF07365

InterPro

IPR009958

PROSITE

PDOC60004

SCOP2

1mii / SCOPe / SUPFAM

OPM superfamily

148

OPM protein

1akg

Available protein structures:

Pfam  

structures / ECOD  

PDB

RCSB PDB; PDBe; PDBj

PDBsum

structure summary

Omega conotoxin

Schematic diagram of the three-dimensional structure of ω-conotoxin MVIIA (ziconotide). Disulfide bonds are shown in gold. From PDB: 1DW5​.

Identifiers

Symbol

Conotoxin

Pfam

PF02950

InterPro

IPR004214

SCOP2

2cco / SCOPe / SUPFAM

OPM superfamily

112

OPM protein

1fyg

Available protein structures:

Pfam  

structures / ECOD  

PDB

RCSB PDB; PDBe; PDBj

PDBsum

structure summary

Aconotoxin is one of a group of neurotoxic peptides isolated from the venom of the marine cone snail, genus Conus.

Conotoxins, which are peptides consisting of 10 to 30 amino acid residues, typically have one or more disulfide bonds. Conotoxins have a variety of mechanisms of actions, most of which have not been determined. However, it appears that many of these peptides modulate the activity of ion channels.[1] Over the last few decades conotoxins have been the subject of pharmacological interest.[2]

The LD50 of conotoxin ranges from 5-25 μg/kg.[3][4][5]

Hypervariability[edit]

Conotoxins are hypervariable even within the same species. They do not act within a body where they are produced (endogenously) but act on other organisms.[6] Therefore, conotoxin genes experience less selection against mutations (like gene duplication and nonsynonymous substitution), and mutations remain in the genome longer, allowing more time for potentially beneficial novel functions to arise.[7] Variability in conotoxin components reduces the likelihood that prey organisms will develop resistance; thus cone snails are under constant selective pressure to maintain polymorphism in these genes because failing to evolve and adapt will lead to extinction (Red Queen hypothesis).[8]

Disulfide connectivities[edit]

Types of conotoxins also differ in the number and pattern of disulfide bonds.[9] The disulfide bonding network, as well as specific amino acids in inter-cysteine loops, provide the specificity of conotoxins.[10]

Types and biological activities[edit]

The number of conotoxins whose activities have been determined so far is five, and they are called the α(alpha)-, δ(delta)-, κ(kappa)-, μ(mu)-, and ω(omega)- types. Each of the five types of conotoxins attacks a different target:

Alpha[edit]

Alpha conotoxins have two types of cysteine arrangements,[18] and are competitive nicotinic acetylcholine receptor antagonists.

Delta, kappa, and omega[edit]

Omega, delta and kappa families of conotoxins have a knottin or inhibitor cystine knot scaffold. The knottin scaffold is a very special disulfide-through-disulfide knot, in which the III-VI disulfide bond crosses the macrocycle formed by two other disulfide bonds (I-IV and II-V) and the interconnecting backbone segments, where I-VI indicates the six cysteine residues starting from the N-terminus. The cysteine arrangements are the same for omega, delta and kappa families, even though omega conotoxins are calcium channel blockers, whereas delta conotoxins delay the inactivation of sodium channels, and kappa conotoxins are potassium channel blockers.[9]

Mu[edit]

Mu-conotoxin

nmr solution structure of piiia toxin, nmr, 20 structures

Identifiers

Symbol

Mu-conotoxin

Pfam

PF05374

Pfam clan

CL0083

InterPro

IPR008036

SCOP2

1gib / SCOPe / SUPFAM

OPM superfamily

112

OPM protein

1ag7

Available protein structures:

Pfam  

structures / ECOD  

PDB

RCSB PDB; PDBe; PDBj

PDBsum

structure summary

Mu-conotoxins have two types of cysteine arrangements, but the knottin scaffold is not observed.[19] Mu-conotoxins target the muscle-specific voltage-gated sodium channels,[9] and are useful probes for investigating voltage-dependent sodium channels of excitable tissues.[19][20] Mu-conotoxins target the voltage-gated sodium channels, preferentially those of skeletal muscle,[21] and are useful probes for investigating voltage-dependent sodium channels of excitable tissues.[22]

Different subtypes of voltage-gated sodium channels are found in different tissues in mammals, e.g., in muscle and brain, and studies have been carried out to determine the sensitivity and specificity of the mu-conotoxins for the different isoforms.[23]

See also[edit]

References[edit]

This article incorporates text from the public domain Pfam and InterPro:
  • IPR008036
    1. ^ Terlau H, Olivera BM (2004). "Conus venoms: a rich source of novel ion channel-targeted peptides". Physiol. Rev. 84 (1): 41–68. doi:10.1152/physrev.00020.2003. PMID 14715910.
  • ^ Olivera BM, Teichert RW (2007). "Diversity of the neurotoxic Conus peptides: a model for concerted pharmacological discovery". Molecular Interventions. 7 (5): 251–60. doi:10.1124/mi.7.5.7. PMID 17932414.
  • ^ "Archived copy" (PDF). Archived (PDF) from the original on 2017-08-29. Retrieved 2017-03-31.{{cite web}}: CS1 maint: archived copy as title (link)
  • ^ "Biological Agent Reference Sheet - Conotoxin" (PDF). Emory University.
  • ^ Baker, A.L. "toxin ld50 list". PhycoKey.
  • ^ Olivera BM, Watkins M, Bandyopadhyay P, Imperial JS, de la Cotera EP, Aguilar MB, Vera EL, Concepcion GP, Lluisma A (September 2012). "Adaptive radiation of venomous marine snail lineages and the accelerated evolution of venom peptide genes". Ann. N. Y. Acad. Sci. 1267 (1): 61–70. Bibcode:2012NYASA1267...61O. doi:10.1111/j.1749-6632.2012.06603.x. PMC 3488454. PMID 22954218.
  • ^ Wong ES, Belov K (March 2012). "Venom evolution through gene duplications". Gene. 496 (1): 1–7. doi:10.1016/j.gene.2012.01.009. PMID 22285376.
  • ^ Liow LH, Van Valen L, Stenseth NC (July 2011). "Red Queen: from populations to taxa and communities". Trends Ecol. Evol. 26 (7): 349–58. doi:10.1016/j.tree.2011.03.016. PMID 21511358.
  • ^ a b c Jones RM, McIntosh JM (2001). "Cone venom--from accidental stings to deliberate injection". Toxicon. 39 (10): 1447–1451. doi:10.1016/S0041-0101(01)00145-3. PMID 11478951.
  • ^ Sato K, Kini RM, Gopalakrishnakone P, Balaji RA, Ohtake A, Seow KT, Bay BH (2000). "lambda-conotoxins, a new family of conotoxins with unique disulfide pattern and protein folding. Isolation and characterization from the venom of Conus marmoreus". J. Biol. Chem. 275 (50): 39516–39522. doi:10.1074/jbc.M006354200. PMID 10988292.
  • ^ Nicke A, Wonnacott S, Lewis RJ (2004). "Alpha-conotoxins as tools for the elucidation of structure and function of neuronal nicotinic acetylcholine receptor subtypes". Eur. J. Biochem. 271 (12): 2305–2319. doi:10.1111/j.1432-1033.2004.04145.x. PMID 15182346.
  • ^ Leipold E, Hansel A, Olivera BM, Terlau H, Heinemann SH (2005). "Molecular interaction of delta-conotoxins with voltage-gated sodium channels". FEBS Lett. 579 (18): 3881–3884. doi:10.1016/j.febslet.2005.05.077. PMID 15990094.
  • ^ Shon KJ, Stocker M, Terlau H, Stühmer W, Jacobsen R, Walker C, Grilley M, Watkins M, Hillyard DR, Gray WR, Olivera BM (1998). "kappa-Conotoxin PVIIA is a peptide inhibiting the shaker K+ channel". J. Biol. Chem. 273 (1): 33–38. doi:10.1074/jbc.273.1.33. PMID 9417043.
  • ^ Li RA, Tomaselli GF (2004). "Using the deadly mu-conotoxins as probes of voltage-gated sodium channels". Toxicon. 44 (2): 117–122. doi:10.1016/j.toxicon.2004.03.028. PMC 2698010. PMID 15246758.
  • ^ Nielsen KJ, Schroeder T, Lewis R (2000). "Structure-activity relationships of omega-conotoxins at N-type voltage-sensitive calcium channels". J. Mol. Recognit. 13 (2): 55–70. doi:10.1002/(SICI)1099-1352(200003/04)13:2<55::AID-JMR488>3.0.CO;2-O. PMID 10822250. Archived from the original (abstract) on 2011-08-13.
  • ^ Bowersox SS, Luther R (1998). "Pharmacotherapeutic potential of omega-conotoxin MVIIA (SNX-111), an N-type neuronal calcium channel blocker found in the venom of Conus magus". Toxicon. 36 (11): 1651–1658. doi:10.1016/S0041-0101(98)00158-5. PMID 9792182.
  • ^ Prommer E (2006). "Ziconotide: a new option for refractory pain". Drugs Today. 42 (6): 369–78. doi:10.1358/dot.2006.42.6.973534. PMID 16845440.
  • ^ Gray WR, Olivera BM, Zafaralla GC, Ramilo CA, Yoshikami D, Nadasdi L, Hammerland LG, Kristipati R, Ramachandran J, Miljanich G (1992). "Novel alpha- and omega-conotoxins from Conus striatus venom". Biochemistry. 31 (41): 11864–11873. doi:10.1021/bi00156a009. PMID 1390774.
  • ^ a b Nielsen KJ, Watson M, Adams DJ, Hammarström AK, Gage PW, Hill JM, Craik DJ, Thomas L, Adams D, Alewood PF, Lewis RJ (July 2002). "Solution structure of mu-conotoxin PIIIA, a preferential inhibitor of persistent tetrodotoxin-sensitive sodium channels" (PDF). J. Biol. Chem. 277 (30): 27247–55. doi:10.1074/jbc.M201611200. PMID 12006587.
  • ^ Zeikus RD, Gray WR, Cruz LJ, Olivera BM, Kerr L, Moczydlowski E, Yoshikami D (1985). "Conus geographus toxins that discriminate between neuronal and muscle sodium channels". J. Biol. Chem. 260 (16): 9280–8. doi:10.1016/S0021-9258(17)39364-X. PMID 2410412.
  • ^ McIntosh JM, Jones RM (October 2001). "Cone venom--from accidental stings to deliberate injection". Toxicon. 39 (10): 1447–51. doi:10.1016/S0041-0101(01)00145-3. PMID 11478951.
  • ^ Cruz LJ, Gray WR, Olivera BM, Zeikus RD, Kerr L, Yoshikami D, Moczydlowski E (August 1985). "Conus geographus toxins that discriminate between neuronal and muscle sodium channels". J. Biol. Chem. 260 (16): 9280–8. doi:10.1016/S0021-9258(17)39364-X. PMID 2410412.
  • ^ Floresca CZ (2003). "A comparison of the mu-conotoxins by [3H]saxitoxin binding assays in neuronal and skeletal muscle sodium channel". Toxicol Appl Pharmacol. 190 (2): 95–101. doi:10.1016/s0041-008x(03)00153-4. PMID 12878039.
  • External links[edit]

    General

  • Protein folding
  • Structure determination methods
  • All-α folds:

  • Globin fold
  • Homeodomain fold
  • Alpha solenoid
  • Death fold
  • All-β folds:

  • Beta barrel
  • Beta-propeller
  • Beta helix
  • α/β folds:

  • Leucine-rich repeat
  • Flavodoxin fold
  • Rossmann fold
  • Thioredoxin fold
  • Trefoil knot fold
  • α+β folds:

  • Ferredoxin fold
  • Ribonuclease A
  • SH2-like fold
  • Irregular folds:

  • cytotoxin
  • enterotoxin
  • hemotoxin
  • hepatotoxin
  • neurotoxin
  • phototoxin
  • Bacterial
    toxins

    Exotoxin

  • difficile
  • B
  • botulinum
  • other:

  • Listeriolysin O
  • Cocci

  • Leukocidin
  • Staphylococcus

  • Exfoliatin
  • Toxic shock syndrome toxin
  • Staphylococcal Enterotoxin B (SEB)
  • Actinomycetota

  • Diphtheria toxin
  • Gram
    negative

  • E. coli heat-stable enterotoxin
  • Cholera toxin/Heat-labile enterotoxin
  • Pertussis toxin
  • Pseudomonas exotoxin
  • Extracellular adenylate cyclase
  • Mechanisms

  • type II
  • type III
  • Endotoxin

  • Bacillus thuringiensis delta endotoxin
  • Other B. thuringiensis toxins
  • Virulence
    factor

  • Fibronectin binding protein A
  • Mycotoxins

  • Amatoxin (alpha-amanitin, beta-amanitin, gamma-amanitin, epsilon-amanitin)
  • beta-Nitropropionic acid
  • Citrinin
  • Cytochalasin
  • Ergotamine
  • Fumonisin (Fumonisin B1, Fumonisin B2, Fumonisin B3, Fumonisin B4)
  • Gliotoxin
  • Ibotenic acid
  • Lolitrem B
  • Muscimol
  • Orellanine
  • Ochratoxin
  • Patulin
  • Phalloidin
  • Sterigmatocystin
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  • Plant toxins

  • Anisatin
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  • Invertebrate
    toxins

    Scorpion:

  • Charybdotoxin
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  • Lq2
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  • BmKAEP
  • Phaiodotoxin
  • Imperatoxin
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  • spider:

  • CSTX
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  • Vanillotoxin
  • Huwentoxin
  • Mollusca:

  • Eledoisin
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  • Vertebrate
    toxins

    Fish:

  • Tetrodotoxin
  • Amphibian:

  • Batrachotoxin
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  • Epibatidine
  • Histrionicotoxin
  • Pumiliotoxin 251D
  • Samandarin
  • Samandaridine
  • Tarichatoxin
  • Zetekitoxin AB
  • Reptile/
    Snake venom:

  • Beta-Bungarotoxin
  • Calciseptine
  • Taicatoxin
  • Calcicludine
  • Cardiotoxin III
    • note: some toxins are produced by lower species and pass through intermediate species

    Calcium

    VDCCsTooltip Voltage-dependent calcium channels

  • Azelnidipine
  • Barnidipine
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  • Cronidipine
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  • Ryodipine (riodipine)
  • Sagandipine
  • Sornidipine
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  • Tiamdipine
  • Trombodipine
  • Vatanidipine; Diltiazem derivatives: Clentiazem
  • Diltiazem
  • Iprotiazem
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  • Siratiazem; Phenylalkylamines: Anipamil
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  • Dexverapamil
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  • Cyproheptadine
  • Dronedarone
  • Fantofarone
  • SR-33805
  • Tetrahydropalmatine
  • Activators

    Potassium

    VGKCsTooltip Voltage-gated potassium channels

  • Adekalant
  • Almokalant
  • Amiodarone
  • Azimilide
  • Bretylium
  • Bunaftine
  • Charybdotoxin
  • Clamikalant
  • Conotoxins
  • Dalazatide
  • Dendrotoxin
  • Dofetilide
  • Dronedarone
  • E-4031
  • Hanatoxin
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  • Ibutilide
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  • Linopirdine
  • Lolitrem B
  • Maurotoxin
  • Nifekalant
  • Notoxin
  • Paxilline
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  • Quinidine
  • ShK-186
  • Sotalol
  • Tedisamil
  • Terikalant
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  • Vernakalant
  • Activators

  • Retigabine
  • IRKsTooltip Inwardly rectifying potassium channel

    Blockers

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  • Activators

  • Bimakalim
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  • Naminidil
  • Nicorandil
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  • Sarakalim
  • KCaTooltip Calcium-activated potassium channel

    Blockers

  • GAL-021
  • Activators

  • Meclofenamic acid
  • Niflumic acid
  • Nimesulide
  • Rottlerin (mallotoxin)
  • Tolfenamic acid
  • K2PsTooltip Tandem pore domain potassium channel

    Blockers

  • Arachidonic acid
  • Fluoxetine
  • Norfluoxetine
  • Activators

    Sodium

    VGSCsTooltip Voltage-gated sodium channels

  • Aprindine
  • Disopyramide
  • Dronedarone
  • Encainide
  • Flecainide
  • Lidocaine
  • Lorajmine
  • Lorcainide
  • Mexiletine
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  • Pilsicainide
  • Prajmaline
  • Procainamide
  • Propafenone
  • Quinidine
  • Sparteine
  • Tocainide
  • Activators

  • Atracotoxins (ω-Atracotoxin, Robustoxin, Versutoxin)
  • Batrachotoxin
  • Ciguatoxins
  • Grayanotoxins
  • Poneratoxin
  • ENaCTooltip Epithelial sodium channel

    Blockers

  • Benzamil
  • Triamterene
  • Activators

    ASICsTooltip Acid-sensing ion channel

    Blockers

  • Amiloride
  • Aspirin
  • Ibuprofen
  • PcTX1
  • Chloride

    CaCCsTooltip Calcium-activated chloride channel

  • Ethacrynic acid
  • Flufenamic acid
  • Fluoxetine
  • Furosemide
  • Glibenclamide
  • Mefloquine
  • Mibefradil
  • Niflumic acid
  • Activators

    CFTRTooltip Cystic fibrosis transmembrane conductance regulator

    Blockers

  • Lonidamine
  • Piretanide
  • Activators

  • 1,10-Phenanthroline
  • 4,7-Phenanthroline
  • 7,8-Benzoquinoline
  • Ivacaftor
  • Phenanthridine
  • Unsorted

    Blockers

  • Flufenamic acid
  • Meclofenamic acid
  • Mefenamic acid
  • Mepacrine
  • Niflumic acid
  • Talniflumate
  • Tolfenamic acid
  • Trifluoperazine
  • Others

    TRPsTooltip Transient receptor potential channels

    LGICsTooltip Ligand gated ion channels

    See also: Receptor/signaling modulatorsTransient receptor potential channel modulators

    nAChRsTooltip Nicotinic acetylcholine receptors

    Agonists
    (and PAMsTooltip positive allosteric modulators)

  • 6-Chloronicotine
  • A-84,543
  • A-366,833
  • A-582,941
  • A-867,744
  • ABT-202
  • ABT-418
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  • Acetylcholine
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  • Bephenium hydroxynaphthoate
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  • Cytisine
  • Decamethonium
  • Desformylflustrabromine
  • Dianicline
  • Dimethylphenylpiperazinium
  • Epibatidine
  • Epiboxidine
  • Ethanol (alcohol)
  • Ethoxysebacylcholine
  • EVP-4473
  • EVP-6124
  • Galantamine
  • GTS-21
  • Ispronicline
  • Ivermectin
  • JNJ-39393406
  • Levamisole
  • Lobeline
  • MEM-63,908 (RG-3487)
  • Morantel
  • Nicotine (tobacco)
  • NS-1738
  • PHA-543,613
  • PHA-709,829
  • PNU-120,596
  • PNU-282,987
  • Pozanicline
  • Pyrantel
  • Rivanicline
  • RJR-2429
  • Sazetidine A
  • SB-206553
  • Sebacylcholine
  • SIB-1508Y
  • SIB-1553A
  • SSR-180,711
  • Suberyldicholine
  • Suxamethonium (succinylcholine)
  • Suxethonium (succinyldicholine)
  • TC-1698
  • TC-1734
  • TC-1827
  • TC-2216
  • TC-5214
  • TC-5619
  • TC-6683
  • Tebanicline
  • Tribendimidine
  • Tropisetron
  • UB-165
  • Varenicline
  • WAY-317,538
  • XY-4083
  • Antagonists
    (and NAMsTooltip negative allosteric modulators)

  • 18-MC
  • α-Neurotoxins (e.g., α-bungarotoxin, α-cobratoxin, α-conotoxin, many others)
  • ABT-126
  • Alcuronium
  • Allopregnanolone
  • Amantadine
  • Anatruxonium
  • AQW051
  • Atracurium
  • Barbiturates (e.g., pentobarbital, sodium thiopental)
  • BNC-210
  • Bungarotoxins (e.g., α-bungarotoxin, κ-bungarotoxin)
  • Bupropion
  • BW284C51
  • BW-A444
  • Candocuronium iodide (chandonium iodide)
  • Chlorisondamine
  • Cisatracurium
  • Coclaurine
  • Coronaridine
  • Curare
  • Cyclopropane
  • Dacuronium bromide
  • Decamethonium
  • Dehydronorketamine
  • Desflurane
  • Dextromethorphan
  • Dextropropoxyphene
  • Dextrorphan
  • Diadonium
  • DHβE
  • Dihydrochandonium
  • Dimethyltubocurarine (metocurine)
  • Dioscorine
  • Dipyrandium
  • Dizocilpine (MK-801)
  • Doxacurium
  • Encenicline
  • Enflurane
  • Erythravine
  • Esketamine
  • Fazadinium
  • Gallamine
  • Gantacurium chloride
  • Halothane
  • Hexafluronium
  • Hexamethonium (benzohexonium)
  • Hydroxybupropion
  • Hydroxynorketamine
  • Ibogaine
  • Isoflurane
  • Ketamine
  • Kynurenic acid
  • Laudanosine
  • Laudexium (laudolissin)
  • Levacetylmethadol
  • Levomethadone
  • Malouetine
  • ME-18-MC
  • Mecamylamine
  • Memantine
  • Methadone
  • Methorphan (racemethorphan)
  • Methyllycaconitine
  • Metocurine
  • Mivacurium
  • Morphanol (racemorphan)
  • Neramexane
  • Nitrous oxide
  • Norketamine
  • Pancuronium bromide
  • Pempidine
  • Pentamine
  • Pentolinium
  • Phencyclidine
  • Pipecuronium bromide
  • Progesterone
  • Promegestone
  • Radafaxine
  • Rapacuronium bromide
  • Reboxetine
  • Rocuronium bromide
  • Sevoflurane
  • Stercuronium iodide
  • Surugatoxin
  • Thiocolchicoside
  • Threohydrobupropion
  • Toxiferine
  • Tramadol
  • Trimetaphan camsilate (trimethaphan camsylate)
  • Tropeinium
  • Tubocurarine
  • Vanoxerine
  • Vecuronium bromide
  • Xenon
  • Precursors
    (and prodrugs)

  • Adafenoxate
  • Choline (lecithin)
  • Citicoline
  • Cyprodenate
  • Dimethylethanolamine
  • Glycerophosphocholine
  • Meclofenoxate (centrophenoxine)
  • Phosphatidylcholine
  • Phosphatidylethanolamine
  • Phosphorylcholine
  • Pirisudanol
  • See also
    Receptor/signaling modulators
    Muscarinic acetylcholine receptor modulators
    Acetylcholine metabolism/transport modulators


    Retrieved from "https://en.wikipedia.org/w/index.php?title=Conotoxin&oldid=1183872786"

    Categories: 
    Snail toxins
    Ion channel toxins
    Neurotoxins
    Nicotinic antagonists
    Peripheral membrane proteins
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