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Special Issue "Marine Invertebrate Toxins"

A special issue of Marine Drugs (ISSN 1660-3397).

Deadline for manuscript submissions: 28 April 2018

Special Issue Editors

Guest Editor
Dr. Ana G Cabado

Food Safety Department-Idi, ANFACO-CECOPESCA
Website | E-Mail
Interests: marine toxins; food safety; chemical; biological contaminants
Guest Editor
Dr. Lucía Blanco

Website | E-Mail
Interests: chemical contaminants; marine biotoxins; food safety

Special Issue Information

Dear Colleagues,

Marine invertebrates are conspicuous residents in oceans, anywhere from the sea surface to the deep. These creatures are so fascinating because of the many differences between them. As a part of defensive and/or predation strategies, toxins have evolved in invertebrate animals and are particularly abundant. They produce toxins that vary from small to high molecular weight molecules and display unique chemical and biological features of scientific concern.

Protein and peptide toxins, as well as non-proteinaceous compounds, and their derivatives, are a class of specific chemical substances capable of causing diseases on contact with or absorption by body tissues. They bind to a variety of cognate receptors to exert poisonous effects. Over the past few decades, our understanding of the mechanisms of action, molecular definitions and interactions of toxins with their targets has increased enormously. These findings rapidly expanded the biomedical applications of toxins, such as for targeted drug delivery, and in the design of new drugs.

This Special Issue provides an initial survey of marine invertebrate toxins and their salient properties. It gathers original peer-reviewed articles and reviews reflecting updated research in domains concerning marine invertebrate toxins, i.e., chemical, immunological, environmental, pharmacological and physiological aspect, as well as mechanism of action and applicability.

Dr. Ana G Cabado
Dr. Lucía Blanco
Guest Editors

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. Marine Drugs 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 1800 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.


  • invertebrate marine toxins
  • conotoxins
  • shellfish toxins
  • nemertine toxins
  • alkaloids from marine sponges
  • makaluvamine
  • annelida
  • echinoderms
  • sea anemone
  • ascidian toxins.

Published Papers (1 paper)

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Open AccessArticle APETx4, a Novel Sea Anemone Toxin and a Modulator of the Cancer-Relevant Potassium Channel KV10.1
Mar. Drugs 2017, 15(9), 287; doi:10.3390/md15090287
Received: 1 August 2017 / Revised: 5 September 2017 / Accepted: 7 September 2017 / Published: 13 September 2017
Cited by 1 | PDF Full-text (2821 KB) | HTML Full-text | XML Full-text | Supplementary Files
The human ether-à-go-go channel (hEag1 or KV10.1) is a cancer-relevant voltage-gated potassium channel that is overexpressed in a majority of human tumors. Peptides that are able to selectively inhibit this channel can be lead compounds in the search for new anticancer
[...] Read more.
The human ether-à-go-go channel (hEag1 or KV10.1) is a cancer-relevant voltage-gated potassium channel that is overexpressed in a majority of human tumors. Peptides that are able to selectively inhibit this channel can be lead compounds in the search for new anticancer drugs. Here, we report the activity-guided purification and electrophysiological characterization of a novel KV10.1 inhibitor from the sea anemone Anthopleura elegantissima. Purified sea anemone fractions were screened for inhibitory activity on KV10.1 by measuring whole-cell currents as expressed in Xenopus laevis oocytes using the two-microelectrode voltage clamp technique. Fractions that showed activity on Kv10.1 were further purified by RP-HPLC. The amino acid sequence of the peptide was determined by a combination of MALDI- LIFT-TOF/TOF MS/MS and CID-ESI-FT-ICR MS/MS and showed a high similarity with APETx1 and APETx3 and was therefore named APETx4. Subsequently, the peptide was electrophysiologically characterized on KV10.1. The selectivity of the toxin was investigated on an array of voltage-gated ion channels, including the cardiac human ether-à-go-go-related gene potassium channel (hERG or Kv11.1). The toxin inhibits KV10.1 with an IC50 value of 1.1 μM. In the presence of a similar toxin concentration, a shift of the activation curve towards more positive potentials was observed. Similar to the effect of the gating modifier toxin APETx1 on hERG, the inhibition of Kv10.1 by the isolated toxin is reduced at more positive voltages and the peptide seems to keep the channel in a closed state. Although the peptide also induces inhibitory effects on other KV and NaV channels, it exhibits no significant effect on hERG. Moreover, APETx4 induces a concentration-dependent cytotoxic and proapoptotic effect in various cancerous and noncancerous cell lines. This newly identified KV10.1 inhibitor can be used as a tool to further characterize the oncogenic channel KV10.1 or as a scaffold for the design and synthesis of more potent and safer anticancer drugs. Full article
(This article belongs to the Special Issue Marine Invertebrate Toxins)

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