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Special Issue "Toxins in Drug Discovery and Pharmacology"

A special issue of Toxins (ISSN 2072-6651).

Deadline for manuscript submissions: 30 September 2017

Special Issue Editor

Guest Editor
Dr. Steve Peigneur

Catholic University Leuven (KU Leuven), Toxicology and Pharmacology, Herestraat 49-Box 922, 3000 Leuven, Belgium
Website | E-Mail

Special Issue Information

Dear Colleagues,

Venoms from marine and terrestrial animals (cone snails, scorpions, spiders, snakes, centipedes, cnidarian, etc.) can be seen as an untapped cocktail of biologically-active compounds, being increasingly recognized as new emerging source of peptide-based therapeutics. Venomous animals are considered to be specialized predators that have evolved the most sophisticated peptide chemistry and neuropharmacology for their own biological purposes by producing venoms that contains a structural and functional diversity of neurotoxins. These neurotoxins have shown to be highly selective ligands for a wide range of ion channels and receptors. Therefore, they represent interesting lead compounds for the development of, for example, analgesics, anti-cancer drugs, drugs for neurological disorders such as multiple sclerosis, Parkinson’s disease, Alzheimer’s disease, etc.

This Special Issue of Toxins aims to provide a comprehensive look at toxins and toxin inspired leads and will focus on the mechanism of action, structure-function and evolution of pharmacological interesting venom components, including but not limited to, recent developments relating to the emergence of venoms as an underutilized source of highly evolved bioactive peptides with clinical potential.

Dr. Steve Peigneur
Guest Editor

Manuscript Submission Information

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. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short 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 thoroughly refereed through a single-blind 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.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1500 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • sodium channels

  • potassium channels

  • calcium channels

  • chloride ion channels

  • TRP channels

  • ASIC channels

  • opiate receptors

  • acetylcholine receptors

  • NMDA receptor

  • Antibiotics

  • antimicrobial peptides

  • botulinum toxins

  • cone snail venom peptides

  • spider venom peptides

  • amphibian peptides

  • sea anemone toxins

  • scorpion toxins

  • snake toxins

  • centipede toxins

Published Papers (1 paper)

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Research

Open AccessFeature PaperArticle Lengths of the C-Terminus and Interconnecting Loops Impact Stability of Spider-Derived Gating Modifier Toxins
Toxins 2017, 9(8), 248; doi:10.3390/toxins9080248
Received: 17 July 2017 / Revised: 8 August 2017 / Accepted: 8 August 2017 / Published: 12 August 2017
PDF Full-text (6638 KB) | HTML Full-text | XML Full-text
Abstract
Spider gating modifier toxins (GMTs) are potent modulators of voltage-gated ion channels and have thus attracted attention as drug leads for several pathophysiological conditions. GMTs contain three disulfide bonds organized in an inhibitory cystine knot, which putatively confers them with high stability; however,
[...] Read more.
Spider gating modifier toxins (GMTs) are potent modulators of voltage-gated ion channels and have thus attracted attention as drug leads for several pathophysiological conditions. GMTs contain three disulfide bonds organized in an inhibitory cystine knot, which putatively confers them with high stability; however, thus far, there has not been a focused study to establish the stability of GMTs in physiological conditions. We examined the resistance of five GMTs including GpTx-1, HnTx-IV, HwTx-IV, PaurTx-3 and SgTx-1, to pH, thermal and proteolytic degradation. The peptides were stable under physiological conditions, except SgTx-1, which was susceptible to proteolysis, probably due to a longer C-terminus compared to the other peptides. In non-physiological conditions, the five peptides withstood chaotropic degradation, and all but SgTx-1 remained intact after prolonged exposure to high temperature; however, the peptides were degraded in strongly alkaline solutions. GpTx-1 and PaurTx-3 were more resistant to basic hydrolysis than HnTx-IV, HwTx-IV and SgTx-1, probably because a shorter interconnecting loop 3 on GpTx-1 and PaurTx-3 may stabilize interactions between the C-terminus and the hydrophobic patch. Here, we establish that most GMTs are exceptionally stable, and propose that, in the design of GMT-based therapeutics, stability can be enhanced by optimizing the C-terminus in terms of length, and increased interactions with the hydrophobic patch. Full article
(This article belongs to the Special Issue Toxins in Drug Discovery and Pharmacology)
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