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 ?
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.
Cone shells contain therapeutically useful peptides including the conotoxins, and one such peptide, ziconotide, has been approved.
The venom from marine cone snails, used to immobilize prey, contains numerous peptides called conotoxins, some of which can act as painkillers in mammals.
Though ziconotide, the only drug created from conotoxins is available to treat pain, it is less used as it involves an invasive method of infusing the drug directly into the spinal cord.
Identification of Conus peptidylprolyl cis-trans isomerases (PPIases) and assessment of their role in the oxidative folding of conotoxins.
Due to their enormous diversity and target specificity, conotoxins have become invaluable tools in molecular pharmacology and as therapeutic agents.
Drugs from the sea: Conotoxins as drug leads for neuropathic pain and other neurological conditions.
Neurologists, pharmacologists, toxicologists, and other medical specialists and scientists from around the world also discuss the use of other neurotoxins like tetanus toxin, bungarotoxins, conotoxins, and spider and wasp neurotoxins.
Also, in a study of the evolution of conotoxins, the small peptides expressed in Conus venoms and utilized in prey capture, Duda and Remigio (2008) obtained mRNA sequences from C.
Analgesic conotoxins act through numerous nonopioid targets," he adds, so these natural painkillers may ultimately help patients who become tolerant to narcotics.
Identification of tyrosine sulfation in Conus pennaceus conotoxins a-PnIA and a-PnIB: further investigation of labile sulfo-and phosphopeptides by electrospray, matrix-assisted laser desorption/ionization (MALDI) and atmospheric pressure MALDI mass spectrometry.
Conotoxins are only 10 to 40 amino acids in length and are extremely selective about their receptor binding sites.