Special Issue "Ion Channel Neurotoxins"
A special issue of Toxins (ISSN 2072-6651).
Deadline for manuscript submissions: 31 August 2014
Dr. Jean-Marc Sabatier
Laboratory INSERM U1097-ERT 62 'Ingenierie des Peptides a Visee Therapeutique', Universite de la Mediterranee, Faculte de Medecine Nord, Boulevard Pierre Dramard, 13916 Marseille, Cedex 20, France
Phone: +33 640 15 24 19
Fax: +33 442 29 16 12
Interests: toxinology; animal toxins; ion channel blockers; toxin-derived drug; drug design; peptide and protein engineering; therapy
Animal venoms (scorpions, snakes, cone snails, worms, sea anemones, frogs, wasps, etc.) are invaluable sources of pharmacologically-active compounds with various molecular targets. Among venom compounds, peptide toxins target the diverse ion channels (potassium, calcium, sodium and chloride channels). These molecules are often highly potent, more or less selective and, sometimes, have a potential therapeutic value depending on their cellular targets. Some peptide toxins are structurally optimized to be developed as candidate drugs to treat pain and specific human pathologies, such as autoimmune and neurological disorders. This special issue of ‘Toxins’ deals with all aspects of the venomous molecules, including structural properties, pharmacology, structure-activity relationships, toxin-based drug design, toxin engineering and development as chemotherapeutic drugs.
Dr. Jean-Marc Sabatier
Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.
Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Toxins is an international peer-reviewed Open Access monthly journal published by MDPI.
- animal toxin
- venomous animal
- ion channel
- ion channel modulator
- drug design
- toxin engineering
- chemotherapeutic drug
Article: Binding Modes of Two Scorpion Toxins to the Voltage-Gated Potassium Channel Kv1.3 Revealed from Molecular Dynamics
Toxins 2014, 6(7), 2149-2161; doi:10.3390/toxins6072149
Received: 30 May 2014; in revised form: 8 July 2014 / Accepted: 10 July 2014 / Published: 22 July 2014| PDF Full-text (1369 KB) | HTML Full-text | XML Full-text
Article: Recombinant Expression and Functional Characterization of Martentoxin: A Selective Inhibitor for BK Channel (α + β4)
Toxins 2014, 6(4), 1419-1433; doi:10.3390/toxins6041419
Received: 18 February 2014; in revised form: 27 March 2014 / Accepted: 1 April 2014 / Published: 22 April 2014| PDF Full-text (1505 KB) | HTML Full-text | XML Full-text
The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.
Author: Rong Chen; Research School of Biology, Australian National University, Canberra, ACT 0200, Australia
Abstract: Molecular dynamics (MD) simulations are used to examine the binding modes of two scorpion toxins, margatoxin (MgTx) and hongotoxin (HgTx), to the voltage gated K+ channel Kv1.3. Two alternative binding modes of MgTx-Kv1.3 in which Lys28 and Lys35 from the toxin protrudes into the filter of the channel, respectively, are examined using MD simulations with distance restraints. It is found that the MgTx-Kv1.3 complex is stable only when the side chain of MgTx-Lys35 occludes the channel filter, suggesting that MgTx-Lys35 is the filter residue for Kv1.3. On the other hand, HgTx forms a stable complex with Kv1.3 when the side chain of HgTx-Lys28 protrudes into the filter of the channel. The HgTx-Kv1.3 complex is further stabilized by the salt bridge between HgTx-Arg24 and Kv1.3-Asp433. A systematic survey of all the possible binding modes of HgTx-Kv1.3 is carried out by rotating the toxin at 3° intervals around the channel axis while the position of HgTx-Lys28 relative to the filter is maintained. This identifies a yet second possible binding mode in which HgTx-Arg24 interacts with Kv1.3-Ser426 rather than Kv1.3-Asp433. Potential of mean force calculations show that the dissociation constant of HgTx-Kv1.3 is 8 pM for the Arg24-Asp433 mode and 180 pM for the Arg24-Ser426 mode, suggesting that the Arg24-Asp433 mode is slightly
Last update: 1 April 2014