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Recent Progress on Toxins in Pharmacology and Drug Discovery
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Recent Progress on Toxins in Pharmacology and Drug Discovery

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Toxicology".

Deadline for manuscript submissions: closed (30 November 2024) | Viewed by 2861

Special Issue Editor

Dr. Steve Peigneur

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Guest Editor
Toxicology and Pharmacology, Katholieke Universiteit (KU) Leuven, Campus Gasthuisberg, Leuven, Belgium
Interests: antimicrobial; cytotoxic; worms; acetylcholine receptor; centipede; cone snail; scorpion; voltage-gated ion channel; conotoxin; cancer; wasp; snake; spider; electrophysiology; nmda; pain; plants; cannabinoid receptor
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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 IJMS 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 submissions that pass pre-check are 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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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
 

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Published Papers (2 papers)

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Research

16 pages, 4369 KiB  
Article
Structure–Function Relationship of a Novel MTX-like Peptide (MTX1) Isolated and Characterized from the Venom of the Scorpion Maurus palmatus
by Rym ElFessi, Oussema Khamessi, Michel De Waard, Najet Srairi-Abid, Kais Ghedira, Riadh Marrouchi and Riadh Kharrat
Int. J. Mol. Sci. 2024, 25(19), 10472; https://doi.org/10.3390/ijms251910472 - 28 Sep 2024
Viewed by 1242
Abstract
Maurotoxin (MTX) is a 34-residue peptide from Scorpio maurus venom. It is reticulated by four disulfide bridges with a unique arrangement compared to other scorpion toxins that target potassium (K+) channels. Structure–activity relationship studies have not been well performed for this [...] Read more.
Maurotoxin (MTX) is a 34-residue peptide from Scorpio maurus venom. It is reticulated by four disulfide bridges with a unique arrangement compared to other scorpion toxins that target potassium (K+) channels. Structure–activity relationship studies have not been well performed for this toxin family. The screening of Scorpio maurus venom was performed by different steps of fractionation, followed by the ELISA test, using MTX antibodies, to isolate an MTX-like peptide. In vitro, in vivo and computational studies were performed to study the structure–activity relationship of the new isolated peptide. We isolated a new peptide designated MTX1, structurally related to MTX. It demonstrated toxicity on mice eight times more effectively than MTX. MTX1 blocks the Kv1.2 and Kv1.3 channels, expressed in Xenopus oocytes, with IC50 values of 0.26 and 180 nM, respectively. Moreover, MTX1 competitively interacts with both 125I-apamin (IC50 = 1.7 nM) and 125I-charybdotoxin (IC50 = 5 nM) for binding to rat brain synaptosomes. Despite its high sequence similarity (85%) to MTX, MTX1 exhibits a higher binding affinity towards the Kv1.2 and SKCa channels. Computational analysis highlights the significance of specific residues in the β-sheet region, particularly the R27, in enhancing the binding affinity of MTX1 towards the Kv1.2 and SKCa channels. Full article
(This article belongs to the Special Issue Recent Progress on Toxins in Pharmacology and Drug Discovery)
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14 pages, 2839 KiB  
Article
Tick-Derived Peptide Blocks Potassium Channel TREK-1
by Canwei Du, Linyan Chen, Guohao Liu, Fuchu Yuan, Zheyang Zhang, Mingqiang Rong, Guoxiang Mo and Changjun Liu
Int. J. Mol. Sci. 2024, 25(15), 8377; https://doi.org/10.3390/ijms25158377 - 31 Jul 2024
Viewed by 1310
Abstract
Ticks transmit a variety of pathogens, including rickettsia and viruses, when they feed on blood, afflicting humans and other animals. Bioactive components acting on inflammation, coagulation, and the immune system were reported to facilitate ticks’ ability to suck blood and transmit tick-borne diseases. [...] Read more.
Ticks transmit a variety of pathogens, including rickettsia and viruses, when they feed on blood, afflicting humans and other animals. Bioactive components acting on inflammation, coagulation, and the immune system were reported to facilitate ticks’ ability to suck blood and transmit tick-borne diseases. In this study, a novel peptide, IstTx, from an Ixodes scapularis cDNA library was analyzed. The peptide IstTx, obtained by recombinant expression and purification, selectively inhibited a potassium channel, TREK-1, in a dose-dependent manner, with an IC50 of 23.46 ± 0.22 μM. The peptide IstTx exhibited different characteristics from fluoxetine, and the possible interaction of the peptide IstTx binding to the channel was explored by molecular docking. Notably, extracellular acidification raised its inhibitory efficacy on the TREK-1 channel. Our results found that the tick-derived peptide IstTx blocked the TREK-1 channel and provided a novel tool acting on the potassium channel. Full article
(This article belongs to the Special Issue Recent Progress on Toxins in Pharmacology and Drug Discovery)
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