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9.6
4.9
Journals
Marine Drugs
Special Issues
Conotoxins
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Conotoxins

A special issue of Marine Drugs (ISSN 1660-3397).

Deadline for manuscript submissions: closed (30 April 2011) | Viewed by 15596

Special Issue Editors

Prof. Dr. David Craik

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Guest Editor
Institute for Molecular Bioscience, University of Queensland, Brisbane QLD 4072, Australia
Prof. Dr. David Adams

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Guest Editor
Illawarra Health and Medical Research Institute (IHMRI), University of Wollongong, Wollongong, NSW 2522, Australia
Interests: acetylcholine nicotinic receptors; voltage-gated ion channels; venom peptides; conotoxins; structure-function relationship; electrophysiology; nociception
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This special issue will focus on structural-activity and pharmacological studies of conotoxins. Conotoxins have created much interest in the last two decades because of their exquisite potency and selectivity for a variety of membrane receptors, transporters, and voltage-gated ion channels that has made them exciting targets as drug leads. One conotoxin is currently on the market for neuropathic pain and several others are in preclinical or clinical development. This issue brings together a collection of articles that describes recent developments in the field from leading experts.

Prof. Dr. David Craik
Prof. Dr. David Adams
Guest Editor

Keywords

  • nicotinic acetylcholine receptors
  • G protein-coupled receptors
  • calcium channels
  • sodium channels
  • potassium channels
  • transporters
  • structure-activity relationships
  • NMR
  • electrophysiology

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Published Papers (2 papers)

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1080 KiB  
Article
Optimal Cleavage and Oxidative Folding of α-Conotoxin TxIB as a Therapeutic Candidate Peptide
by Xiaosa Wu, Yong Wu, Furong Zhu, Qiuyuan Yang, Qianqian Wu, Dongting Zhangsun and Sulan Luo
Mar. Drugs 2013, 11(9), 3537-3553; https://doi.org/10.3390/md11093537 - 17 Sep 2013
Cited by 18 | Viewed by 7560
Abstract
Alpha6beta2 nicotinic acetylcholine receptors (nAChRs) are potential therapeutic targets for the treatment of several neuropsychiatric diseases, including addiction and Parkinson’s disease. Alpha-conotoxin (α-CTx) TxIB is a uniquely selective ligand, which blocks α6/α3β2β3 nAChRs only, but does not block the other subtypes. Therefore, α-CTx [...] Read more.
Alpha6beta2 nicotinic acetylcholine receptors (nAChRs) are potential therapeutic targets for the treatment of several neuropsychiatric diseases, including addiction and Parkinson’s disease. Alpha-conotoxin (α-CTx) TxIB is a uniquely selective ligand, which blocks α6/α3β2β3 nAChRs only, but does not block the other subtypes. Therefore, α-CTx TxIB is a valuable therapeutic candidate peptide. Synthesizing enough α-CTx TxIB with high yield production is required for conducting wide-range testing of its potential medicinal applications. The current study optimized the cleavage of synthesized α-CTx TxIB resin-bounded peptide and folding of the cleaved linear peptide. Key parameters influencing cleavage and oxidative folding of α-CTx TxIB were examined, such as buffer, redox agents, pH, salt, co-solvent and temperature. Twelve conditions were used for cleavage optimization. Fifty-four kinds of one-step oxidative solution were used to assess their effects on each α-CTx TxIB isomers’ yield. The result indicated that co-solvent choices were particularly important. Completely oxidative folding of globular isomer was achieved when the NH4HCO3 or Tris-HCl folding buffer at 4 °C contained 40% of co-solvent DMSO, and GSH:GSSG (2:1) or GSH only with pH 8~8.7. Full article
(This article belongs to the Special Issue Conotoxins)
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3439 KiB  
Article
Design of New α-Conotoxins: From Computer Modeling to Synthesis of Potent Cholinergic Compounds
by Igor E. Kasheverov, Maxim N. Zhmak, Alexey Y. Khruschov and Victor I. Tsetlin
Mar. Drugs 2011, 9(10), 1698-1714; https://doi.org/10.3390/md9101698 - 28 Sep 2011
Cited by 26 | Viewed by 7027
Abstract
A series of 14 new analogs of α-conotoxin PnIA Conus pennaceus was synthesized and tested for binding to the human α7 nicotinic acetylcholine receptor (nAChR) and acetylcholine-binding proteins (AChBP) Lymnaea stagnalis and Aplysia californica. Based on computer modeling and the X-ray structure [...] Read more.
A series of 14 new analogs of α-conotoxin PnIA Conus pennaceus was synthesized and tested for binding to the human α7 nicotinic acetylcholine receptor (nAChR) and acetylcholine-binding proteins (AChBP) Lymnaea stagnalis and Aplysia californica. Based on computer modeling and the X-ray structure of the A. californica AChBP complex with the PnIA[A10L, D14K] analog [1], single and multiple amino acid substitutions were introduced in α-conotoxin PnIA aimed at compounds of higher affinity and selectivity. Three analogs, PnIA[L5H], PnIA[A10L, D14K] and PnIA[L5R, A10L, D14R], have high affinities for AChBPs or α7 nAChR, as found in competition with radioiodinated α-bungarotoxin. That is why we prepared radioiodinated derivatives of these α-conotoxins, demonstrated their specific binding and found that among the tested synthetic analogs, most had almost 10-fold higher affinity in competition with radioactive α-conotoxins as compared to competition with radioactive α-bungarotoxin. Thus, radioiodinated α-conotoxins are a more sensitive tool for checking the activity of novel α-conotoxins and other compounds quickly dissociating from the receptor complexes. Full article
(This article belongs to the Special Issue Conotoxins)
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