conotoxins

conotoxins

(kō″nō-tŏks′ĭn) [Gr. konos, cone + ″]
Any of a group of poisonous peptides made by mollusks known as cone snails. Conotoxins are potent nerve toxins and are considered to be potential biological or chemical warfare agents. Some conotoxins may also be used to treat neuropathic pain.
References in periodicals archive ?
Cone shells contain therapeutically useful peptides including the conotoxins, and one such peptide, ziconotide, has been approved.
A recent ABC article noted a team of Australian researchers working with conotoxins from sea snail venom to create a new non-narcotic pain relief drug.
Different concentrations of chemokines CCL3, CCL4, CCL5, or CXCL16 (R&D Systems; 0.1-50 ng/ml) were applied together with BzATP, in the presence or absence of antagonists mecamylamine hydrochloride (100 [micro]M; Sigma-Aldrich), [alpha]-bungarotoxin (1 [micro]M; Tocris Bioscience, Bristol, UK), and strychnine hydrochloride (10 [micro]M; Sigma-Aldrich) or of the conotoxins ArIB [V11L, V16D] (500 nM) or RgIA4 (200nM) [16-19].
Mirza, "Conotoxins: structure, therapeutic potential and pharmacological applications," Current Pharmaceutical Design, vol.
Conotoxins proteins have many merits, such as low relative molecular mass, stable structure, remarkable activity, high selectivity, and ease of synthesis [1].
Other chapters describe the characteristics of conotoxins; cone snail injuries, their treatment, and prevention measures; and the therapeutic and medicinal value of conotoxins, such as for epilepsy, pain, stroke, and cardioprotection.
The venom from marine cone snails, used to immobilize prey, contains numerous peptides called conotoxins, some of which can act as painkillers in mammals.
Craik and colleagues have based their findings on conotoxins, the small proteins contained in cone snail venom that have long been known for its pain relieving properties.
Identification of Conus peptidylprolyl cis-trans isomerases (PPIases) and assessment of their role in the oxidative folding of conotoxins. J.
Cysteine-rich peptides such as conotoxins and insulin-like peptides are an increasingly important class of biomolecules.
considered the replacement of the disulphide bridge by a side-chain-to-side-chain lactam bridge in accordance with observations on several biologically relevant peptides, such as conotoxins, endothelin-1, and somatostatin analogue that gave interesting results by the same modification [29].