A sleep-inducing peptide from Conus geographus venom

Olivera, Baldomero M.; McIntosh, J. Michael; Clark, Craig; Middlemas, David S.; Gray, William R.; Cruz, L J

doi:10.1016/0041-0101(85)90150-3

Cited by 48 publications

(19 citation statements)

References 9 publications

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“…The peptide put young mice into a sleeplike state (before its mechanism was elucidated, it was called the "sleeper peptide") but made older mice hyperactive (142,145). Conantokin-G is a small, 17-amino acid linear peptide without disulfide bonds.…”

Section: E Other Conopeptide Families Targeted To Ligand-gated Ion Cmentioning

confidence: 99%

ConusVenoms: A Rich Source of Novel Ion Channel-Targeted Peptides

Terlau

Olivera

2004

Physiological Reviews

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Terlau, Heinrich, and Baldomero M. Olivera. Conus Venoms: A Rich Source of Novel Ion Channel-Targeted Peptides. Physiol Rev 84: 41–68, 2004; 10.1152/physrev.00020.2003.—The cone snails (genus Conus) are venomous marine molluscs that use small, structured peptide toxins (conotoxins) for prey capture, defense, and competitor deterrence. Each of the 500 Conus can express ∼100 different conotoxins, with little overlap between species. An overwhelming majority of these peptides are probably targeted selectively to a specific ion channel. Because conotoxins discriminate between closely related subtypes of ion channels, they are widely used as pharmacological agents in ion channel research, and several have direct diagnostic and therapeutic potential. Large conotoxin families can comprise hundreds or thousands of different peptides; most families have a corresponding ion channel family target (i.e., ω-conotoxins and Ca channels, α-conotoxins and nicotinic receptors). Different conotoxin families may have different ligand binding sites on the same ion channel target (i.e., μ-conotoxins and δ-conotoxins to sites 1 and 6 of Na channels, respectively). The individual peptides in a conotoxin family are typically each selectively targeted to a diverse set of different molecular isoforms within the same ion channel family. This review focuses on the targeting specificity of conotoxins and their differential binding to different states of an ion channel.

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Section: E Other Conopeptide Families Targeted To Ligand-gated Ion Cmentioning

confidence: 99%

ConusVenoms: A Rich Source of Novel Ion Channel-Targeted Peptides

Terlau

Olivera

2004

Physiological Reviews

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863

828

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“…Conantokins are peptide toxins found in the venom of fish-hunting Conus. Unlike other toxins from Conus venoms, conantokins lack cysteine residues [3]; they incorporate, instead, numerous y-carboxyglutamic acid (Gla), a post-translationally modified residue. Conantokin-G (Con-G) is a 17-amino-acid peptide, containing five Gla residues, found in the venom of C. geographus.…”

Section: Introductionmentioning

confidence: 99%

Role of modified glutamic acid in the helical structure of conantokin‐T

et al. 1997

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Circular dichroism (CD) and 2-dimensional NMR were used to study the solution conformation of conantokin-T (Con-T), a small peptide toxin found in the venom of fish-hunting cone snails, and its Glu-substituted analog. Con-T lacks disulfide bonds but contains many y-carboxyglutamic acids (Gla), a posttranslationally modified residue. Our results show that Con-T adopts an a-helical conformation in aqueous solution even in the absence of calcium. Glu replacements diminish both helicity and function of Con-T. The helical content of Con-T is higher than most natural helical peptides of this length in aqueous solution. The sequence of this small toxin incorporates several known elements that stabilize a-helical structure in peptides. Gla residues form several salt bridges that stabilize helical conformation of Con-T.

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“…This peptide is one of the most widely used conopeptides in neuroscience (Terlau and Olivera, 2004). The "sleeper peptides" (e.g., the disulfide-poor conopeptide conantokin-G) plunge mice into a state of mental torpor (Olivera et al, 1985b) due to their activity on NMDA glutamate receptors (Donevan and McCabe, 2000). Some other peptides have been given colorful names, including the "moonwalker peptides" (conolysins) that cause mice to adopt a "popstar's signature dance maneuver" (Biggs et al, 2007), the "fin-popping peptide" (PVIIA), the "lock-jaw peptide" (PVIA) or the "King Kong peptides" (e.g., TxVIA), which causes injected lobsters to adopt an "exaggerated dominant stance," probably due to agonist activity on sodium channels (Hillyard et al, 1989).…”

Section: Conopeptide Pharmacological Activitiesmentioning

confidence: 99%

Conotoxins and Other Conopeptides

Kaas

Craik

2014

Outstanding Marine Molecules

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Conopeptides are a large family of peptide toxins produced by marine cone snails. They act with high potency and exquisite specificity on a range of ion channels and transporters of the nervous system, making them valuable drug leads and important molecular probes in neurophysiological studies. Most conopeptides are small, ranging from 10 to 30 amino acid residues, but some contain up to about 90 amino acids. They display a large chemical diversity because they have very diverse sequences and a large number of post-translational modifications. Disulfide-rich conopeptides are commonly referred to as conotoxins, and have particularly diverse structures and a broad range of molecular targets. One conotoxin, MVIIA (also named Prialt 1 or ziconotide), is an N-type calcium channel blocker that is used clinically as an analgesic to treat neuropathic pain. Other conopeptides have also attracted considerable interest for their potential pharmaceutical applications. In this chapter, the marine cone snails and their venoms are introduced and the chemical diversity of conopeptides is described, along with the techniques used to unravel this diversity. The three-dimensional structures of conopeptides are discussed and linked to their pharmacological activities.

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A sleep-inducing peptide from Conus geographus venom

Cited by 48 publications

References 9 publications

ConusVenoms: A Rich Source of Novel Ion Channel-Targeted Peptides

ConusVenoms: A Rich Source of Novel Ion Channel-Targeted Peptides

Role of modified glutamic acid in the helical structure of conantokin‐T

Conotoxins and Other Conopeptides

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