Conotoxins and other conopeptides

Kaas, Quentin and Craik, David J. (2014). Conotoxins and other conopeptides. In Stéphane La Barre and Jean-Michel Kornprobst (Ed.), Outstanding Marine Molecules: Chemistry, Biology, Analysis (pp. 319-332) Weinheim, Germany: Wiley-VCH Verlag. doi:10.1002/9783527681501.ch14


Author Kaas, Quentin
Craik, David J.
Title of chapter Conotoxins and other conopeptides
Title of book Outstanding Marine Molecules: Chemistry, Biology, Analysis
Place of Publication Weinheim, Germany
Publisher Wiley-VCH Verlag
Publication Year 2014
Sub-type Research book chapter (original research)
DOI 10.1002/9783527681501.ch14
Open Access Status
ISBN 9783527334650
9783527681525
9783527681532
9783527681518
9783527681501
Editor Stéphane La Barre
Jean-Michel Kornprobst
Chapter number 14
Start page 319
End page 332
Total pages 14
Total chapters 23
Collection year 2015
Language eng
Formatted Abstract/Summary
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® 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.
Keyword Conotoxin
Conopeptide
Cone snails
Toxins
Ion channels
Neuroreceptors
Drug
Q-Index Code BX
Q-Index Status Confirmed Code
Institutional Status UQ

 
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Created: Tue, 03 Jun 2014, 14:40:26 EST by Susan Allen on behalf of Institute for Molecular Bioscience