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Conopeptide characterization and classifications: An analysis using ConoServer

Toxicon, 2010
Cone snails are carnivorous marine gastropods that have evolved potent venoms to capture their prey. These venoms comprise a rich and diverse cocktail of peptide toxins, or conopeptides, whose high diversity has arisen from an efficient hypermutation mechanism, combined with a high frequency of post-translational modifications.
Quentin K Kaas, David Craik
exaly   +4 more sources

Therapeutic Potential of Conopeptides

Future Medicinal Chemistry, 2012
Conopeptides from the venoms of marine snails have attracted much interest as leads in drug design. Currently, one drug, Prialt(®), is on the market as a treatment for chronic neuropathic pain. Conopeptides target a range of ion channels, receptors and transporters, and are typically small, relatively stable peptides that are generally amenable to ...
Schroeder, Christina I., Craik, David J.
openaire   +3 more sources

Conopeptides: From deadly venoms to novel therapeutics

Drug Discovery Today, 2000
Marine cone snails have developed many distinct venoms that contain biologically active peptides as part of an envenomation survival strategy for feeding and defense. These peptides, known as conopeptides, have been optimized through evolution to target specific ion channels and receptors with very high affinities and selectivities.
, Shen, , Layer, , McCabe
openaire   +2 more sources

Drugs from Slugs. Part II – Conopeptide bioengineering

Chemico-Biological Interactions, 2012
The biological transformation of toxins as research probes, or as pharmaceutical drug leads, is an onerous and drawn out process. Issues regarding changes to pharmacological specificity, desired potency, and bioavailability are compounded naturally by their inherent toxicity.
Jon-Paul, Bingham   +3 more
openaire   +2 more sources

Drugs from the Sea: Conopeptides as Potential Therapeutics

Current Medicinal Chemistry, 2004
Marine cone snails from the genus Conus are estimated to consist of up to 700 species. These predatory molluscs have devised an efficient venom apparatus that allows them to successfully capture polychaete worms, other molluscs or in some cases fish as their primary food sources.
Bruce G, Livett   +2 more
openaire   +2 more sources

Determination of disulfide bridge pattern in ω‐conopeptides

International Journal of Peptide and Protein Research, 1995
Synthetic versions of seven naturally occurring ω‐conopeptides were subjected to structural analyses in order to determine their disulfide bridge pattern. The method applied in this study uses a combination of amino‐acid composition and peptide sequence analysis of various peptide fragments generated by different enzymatic digestions.
D, Chung   +4 more
openaire   +2 more sources

Therapeutic Potential of Cone Snail Venom Peptides (Conopeptides)

Current Topics in Medicinal Chemistry, 2012
Cone snails have evolved many 1000s of small, structurally stable venom peptides (conopeptides) for prey capture and defense. Whilst < 0.1% have been pharmacologically characterised, those with known function typically target membrane proteins of therapeutic importance, including ion channels, transporters and GPCRs. Several conopeptides reduce pain in
Vetter, Irina, Lewis, Richard J.
openaire   +3 more sources

Post-translationally modified conopeptides: Biological activities and pharmacological applications

Peptides, 2021
Conus venoms comprise a large variety of biologically active peptides (conopeptides or conotoxins) that are employed for prey capture and other biological functions. Throughout the course of evolution of the cone snails, they have developed an envenomation scheme that necessitates a potent mixture of peptides, most of which are highly post ...
openaire   +2 more sources

Synthesis and insecticidal activity of cysteine-free conopeptides from Conus betulinus

Toxicon, 2023
The cone snail Conus betulinus is a vermivorous species that is widely distributed in the South China Sea. Its crude venom contains various peptides used to prey on marine worms. In previous studies, a systematic analysis of the peptide toxin sequences from C. betulinus was carried out using a multiomics technique.
Jiao, Chen   +3 more
openaire   +2 more sources

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