Venoms and Drugs

A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Animal Venoms".

Deadline for manuscript submissions: 30 September 2025 | Viewed by 3849

Special Issue Editor


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Guest Editor
Department of Pharmacology and Toxicology, College of Veterinary Medicine, Gyeongsang National University, 501 Jinju Daero, Jinju 52828, Republic of Korea
Interests: venoms; toxins; molecular function; mechanism of action; drug discovery; therapeutics; signal transduction
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Special Issue Information

Dear Colleagues,

Venoms (or zootoxins) are complex mixtures of biologically active substances (proteins, peptides, enzymes, and small molecules) produced by animals, such as snakes, spiders, scorpions, and some marine organisms. These substances are typically delivered through specialized anatomical structures like fangs, stingers, or spines.

This Special Issue, “Venoms and Drugs”, aims to explore the fascinating interface between venom-derived compounds and their potential therapeutic applications. Venoms, often viewed primarily as harmful substances, harbor a myriad of bioactive molecules with unique pharmacological properties. These molecules have shown promise in the development of novel drugs for a variety of diseases, from chronic pain and cancer to cardiovascular and infectious diseases.

We encourage the submission of original research articles, reviews, and case studies that delve into the biological, chemical, and pharmacological aspects of venoms. Contributions that provide insights into the molecular mechanisms of venom action, innovative drug design, and clinical applications are particularly welcome.

Potential topics for this Special Issue include, but are not limited to, the following:

  1. Isolation and characterization of venom components;
  2. Molecular mechanisms of venom action;
  3. Venom-derived peptides and proteins as therapeutic agents;
  4. Drug development from venom components;
  5. Preclinical and clinical studies on venom-based drugs;
  6. Venom toxins and their receptors;
  7. Synthetic and bioengineered toxin analogs;
  8. Venoms in pain management and neuroprotection.

We look forward to receiving valuable contributions that will help advance our understanding of the therapeutic potential of venoms and foster the development of innovative treatments.

Prof. Dr. Euikyung Kim
Guest Editor

Manuscript Submission Information

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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 double-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 2700 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

  • venom components
  • molecular mechanism
  • preclinical
  • clinical
  • toxin receptors
  • toxin analogs

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Published Papers (3 papers)

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Research

17 pages, 1736 KiB  
Article
Electrical Cell Impedance Sensing (ECIS): Feasibility of a Novel In Vitro Approach to Studying Venom Toxicity and Potential Therapeutics
by Abhinandan Choudhury, Kaitlin Linne, Tommaso C. Bulfone, Tanvir Hossain, Abu Ali Ibn Sina, Philip L. Bickler, Bryan G. Fry and Matthew R. Lewin
Toxins 2025, 17(4), 193; https://doi.org/10.3390/toxins17040193 - 11 Apr 2025
Viewed by 954
Abstract
Snakebite envenoming is often discussed in terms of lethality and limb loss, but local tissue injury and coagulotoxic effects of venom are significantly more common acute manifestations of snakebite envenoming (SBE). Local tissue injury and the hemorrhagic and coagulotoxic effects of venom are [...] Read more.
Snakebite envenoming is often discussed in terms of lethality and limb loss, but local tissue injury and coagulotoxic effects of venom are significantly more common acute manifestations of snakebite envenoming (SBE). Local tissue injury and the hemorrhagic and coagulotoxic effects of venom are challenging to study in live animals and can be ethically fraught due to animal welfare concerns such that attention to the 3Rs of animal welfare motivates the development of in vitro techniques in this arena. Herein, we tested the use of a wound-healing study technique known as Electric Cell-Substrate Impedance Sensing (ECIS) to assess populations of cultured cells exposed to venom with or without sPLA2 and/or metalloprotease inhibitors (varespladib and marimastat, respectively). For comparison, the StarMax coagulation analyzer for coagulotoxicity was further used to evaluate the venoms and the neutralizing capabilities of the abovementioned direct toxin inhibitors (DTIs) against the same venoms examined using ECIS. Three viper and three elapid venoms that were examined for their effects on H1975 cells were Agkistrodon contortrix (Eastern Copperhead), Crotalus helleri (Southern Pacific Rattlesnake), and Vipera ammodytes (Horned Viper) and Naja atra (Chinese Cobra), Naja mossambica (Mozambique Spitting Cobra), and Naja nigricollis (Black-necked Spitting Cobra), respectively. The combination of cellular and coagulation techniques appears to usefully discriminate the in vitro capabilities and limitations of specific inhibitors to inhibit specific venom effects. This study suggests that ECIS with or without concomitant coagulation testing is a feasible method to generate reproducible, meaningful preclinical data and could be used with any type of cell line. Importantly, this approach is both quantitative and has the potential of reducing animal use and suffering during the evaluation of potential therapeutics. To further evaluate the potential of this method, rescue studies should be performed. Full article
(This article belongs to the Special Issue Venoms and Drugs)
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20 pages, 3095 KiB  
Article
The Anthelmintic Activity of Stonefish (Synanceia spp.) Ichthyocrinotoxins and Their Potential as Novel Therapeutics
by Danica Lennox-Bulow, Jamie Seymour, Alex Loukas and Michael Smout
Toxins 2025, 17(2), 66; https://doi.org/10.3390/toxins17020066 - 2 Feb 2025
Viewed by 1044
Abstract
Parasitic gastrointestinal worms (i.e., helminths) remain a significant global health and economic burden. The increasing inefficacy of current anthelmintic drugs against parasitic diseases necessitates the discovery of novel therapeutic options. This study investigated the anthelmintic properties and therapeutic potential of stonefish ichthyocrinotoxins (i.e., [...] Read more.
Parasitic gastrointestinal worms (i.e., helminths) remain a significant global health and economic burden. The increasing inefficacy of current anthelmintic drugs against parasitic diseases necessitates the discovery of novel therapeutic options. This study investigated the anthelmintic properties and therapeutic potential of stonefish ichthyocrinotoxins (i.e., secreted skin toxins). xWORM (xCELLigence Worm Real-Time Motility Assay) was used to evaluate the anthelmintic activity of ichthyocrinotoxins from two stonefish species, Synanceia horrida (Estuarine Stonefish) and Synanceia verrucosa (Reef Stonefish), against the infective third-stage larvae of Nippostrongylus brasiliensis (Rodent Hookworm). Both toxins demonstrated potent anthelmintic effects, with S. horrida ichthyocrinotoxin exhibiting greater potency (IC50 = 196.0 µg/mL) compared to ichthyocrinotoxin from S. verrucosa (IC50 = 329.7 µg/mL). Fractionation revealed that the anthelmintic activity of S. verrucosa is likely driven by synergistic interactions between the large (>3 kDa) and small (<3 kDa) components. In contrast, the small components isolated from S. horrida ichthyocrinotoxin were responsible for the majority of the observed activity, making them a more attractive therapeutic candidate. Furthermore, despite the cytotoxicity of crude S. horrida ichthyocrinotoxin against human skin and bile duct cell lines, the isolated small components exhibited potent anthelmintic effects (IC50 = 70.5 µg/mL) with negligible cytotoxicity (<10% decrease in survival at 100 µg/mL). While further research is necessary to fully characterise these compounds and assess their clinical suitability, this study highlights the potential of stonefish ichthyocrinotoxins as a novel source of anthelmintic therapeutics. Full article
(This article belongs to the Special Issue Venoms and Drugs)
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14 pages, 2748 KiB  
Article
Identification of New Angiotensin-Converting Enzyme Inhibitory Peptides Isolated from the Hydrolysate of the Venom of Nemopilema nomurai Jellyfish
by Ramachandran Loganathan Mohan Prakash, Deva Asirvatham Ravi, Du Hyeon Hwang, Changkeun Kang and Euikyung Kim
Toxins 2024, 16(9), 410; https://doi.org/10.3390/toxins16090410 - 20 Sep 2024
Viewed by 1282
Abstract
Recently, jellyfish venom has gained attention as a promising reservoir of pharmacologically active compounds, with potential applications in new drug development. In this investigation, novel peptides, isolated from the hydrolysates of Nemopilema nomurai jellyfish venom (NnV), demonstrate potent inhibitory activities against angiotensin-converting enzyme [...] Read more.
Recently, jellyfish venom has gained attention as a promising reservoir of pharmacologically active compounds, with potential applications in new drug development. In this investigation, novel peptides, isolated from the hydrolysates of Nemopilema nomurai jellyfish venom (NnV), demonstrate potent inhibitory activities against angiotensin-converting enzyme (ACE). Proteolytic enzymes—specifically, papain and protamex—were utilized for the hydrolysis under optimized enzymatic conditions, determined by assessing the degree of hydrolysis through the ninhydrin test. Comparative analyses revealed that papain treatment exhibited a notably higher degree of NnV hydrolysis compared to protamex treatment. ACE inhibitory activity was quantified using ACE kit-WST, indicating a substantial inhibitory effect of 76.31% for the papain-digested NnV crude hydrolysate, which was validated by captopril as a positive control. The separation of the NnV-hydrolysate using DEAE sepharose weak-anion-exchange chromatography revealed nine peaks under a 0–1 M NaCl stepwise gradient, with peak no. 3 displaying the highest ACE inhibition of 96%. The further purification of peak no. 3 through ODS-C18 column reverse-phase high-performance liquid chromatography resulted in five sub-peaks (3.1, 3.2, 3.3, 3.4, and 3.5), among which 3.2 exhibited the most significant inhibitory activity of 95.74%. The subsequent analysis of the active peak (3.2) using MALDI–TOF/MS identified two peptides with distinct molecular weights of 896.48 and 1227.651. The peptide sequence determined by MS/MS analysis revealed them as IVGRPLANG and IGDEPRHQYL. The docking studies of the two ACE-inhibitory peptides for ACE molecule demonstrated a binding affinity of −51.4 ± 2.5 and −62.3 ± 3.3 using the HADDOCK scoring function. Full article
(This article belongs to the Special Issue Venoms and Drugs)
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