Special Issue "Sea Anemone Venom"

A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Marine and Freshwater Toxins".

Deadline for manuscript submissions: 15 September 2020.

Special Issue Editor

Dr. Margarita Monastyrnaya
Guest Editor
G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, 159, Pr. 100 let Vladivostoku, Vladivostok 690022, Russia
Interests: the study of structure–functional relationships of sea anemone toxins, peptides, and polypeptides, neurotoxins of structural type II, APETx-like peptides, alpha-pore-forming toxins, and Kunitz type peptides, in order to establish mechanisms of their interactions with targets, various subtypes of Kv, Nav, ASICs channels, TRP receptors, serine proteases, and cytoplasmic membranes, and to identify pharmacological potential of these peptide substances

Special Issue Information

Dear Colleagues,

The wide spread of severe pathologies and poorly treatable infections associated with an increase in communicative connections of the people and the number of natural and industrial emergencies in many regions of the planet has prompted a large-scale search for new effective pharmacological, so-called molecular-targeting compounds possessing high specificity of action on certain biological targets. The most promising natural source of pharmacologically active compounds is a sea anemone (phylum Cnidaria) venom representing a complex mix of different toxins, peptides, polypeptides used for prey capture, defense, digestion, and intraspecific competition. Acting in small concentrations but with a high specificity on biological targets, endogenous proteases, cytoplasmic membranes, and various types and subtypes of ion channels/receptors playing a functionally significant role in physiological and pathophysiological processes of a body, sea anemone peptides can modulate (block, activate or potentiate) the channel functional activity and, thus, exert a pharmacological effect.

This Special Issue invites authors to publish works on sea anemone toxins, peptides, and polypeptides. The search and isolation of new functionally active peptides, the determination of structures and molecular mechanisms of interaction with biological targets, the assessment of peptides pharmacological potential by in vivo, in vitro, and in silico methods, as well as the achievements of omics technology in studying the structural, functional, and genetic diversity of the sea anemone compounds are priority themes for this release. Editors welcome articles on electrophysiological properties of channels, the mechanisms of channel interactions with various modulators, the role of certain subtypes in organisms, and the consideration of some channelopathies effects on nervous, cardiovascular or musculoskeletal systems. Reviews summarizing important results achieved in the above research areas as well as short communications on the latest data of experimental and theoretical studies expanding the understanding of toxins and their target structure–functional relationships will also be interesting for readers.

Dr. Margarita Monastyrnaya
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 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 2000 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.


  • Sea anemone
  • Molecular evolution
  • Peptides
  • Toxins
  • Structure
  • Function
  • Activity
  • Biological templates
  • Pharmacological potential

Published Papers (1 paper)

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Open AccessArticle
APETx-Like Peptides from the Sea Anemone Heteractis crispa, Diverse in Their Effect on ASIC1a and ASIC3 Ion Channels
Toxins 2020, 12(4), 266; https://doi.org/10.3390/toxins12040266 - 20 Apr 2020
Currently, five peptide modulators of acid-sensing ion channels (ASICs) attributed to structural class 1b of sea anemone toxins have been described. The APETx2 toxin is the first and most potent ASIC3 inhibitor, so its homologs from sea anemones are known as the APETx-like [...] Read more.
Currently, five peptide modulators of acid-sensing ion channels (ASICs) attributed to structural class 1b of sea anemone toxins have been described. The APETx2 toxin is the first and most potent ASIC3 inhibitor, so its homologs from sea anemones are known as the APETx-like peptides. We have discovered that two APETx-like peptides from the sea anemone Heteractis crispa, Hcr 1b-3 and Hcr 1b-4, demonstrate different effects on rASIC1a and rASIC3 currents. While Hcr 1b-3 inhibits both investigated ASIC subtypes with IC50 4.95 ± 0.19 μM for rASIC1a and 17 ± 5.8 μM for rASIC3, Hcr 1b-4 has been found to be the first potentiator of ASIC3, simultaneously inhibiting rASIC1a at similar concentrations: EC50 1.53 ± 0.07 μM and IC50 1.25 ± 0.04 μM. The closest homologs, APETx2, Hcr 1b-1, and Hcr 1b-2, previously demonstrated the ability to inhibit hASIC3 with IC50 63 nM, 5.5, and 15.9 μM, respectively, while Hcr 1b-2 also inhibited rASIC1a with IC50 4.8 ± 0.3 μM. Computer modeling allowed us to describe the peculiarities of Hcr 1b-2 and Hcr 1b-4 interfaces with the rASIC1a channel and the stabilization of the expanded acidic pocket resulting from peptides binding which traps the rASIC1a channel in the closed state. Full article
(This article belongs to the Special Issue Sea Anemone Venom)
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