Special Issue "Sea Anemone Toxins"

Guest Editor
Prof. Dr. Hiroshi Nagai
Department of Ocean Science, Tokyo University of Marine Science and Technology, 4-5-7 Konan, Minato-ku, Tokyo 108-8477, Japan
E-Mail: nagai@kaiyodai.ac.jp

Dear Colleagues,

The sea anemones belong to the phylum Cnidaria. The distinguishing feature of cnidarians is nematocysts, specialized venomous organs that the animals use mainly for capturing prey and protecting themselves from predators. This means all the cnidarians have venom. So far, a number of polypeptide toxins have been isolated and characterized from the sea anemones. Among these studies, ion-channel toxins and pore forming toxins have been characterized. Some ion channel toxins are revealed to be useful tools for biomedical and physiological science. The recent reports showed that sea anemones, including their toxins, are still attractive sources for novel bioactive compounds. This special issue will focus on biological activity, mode of action, ecological significance, isolation and characterization of bioactive compounds including toxins from the sea anemones.

Prof. Dr. Hiroshi Nagai
Guest Editor

Submission

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• Cnidaria
• sea anemone
• biological activity
• venom
• toxin
• bioactive compounds
• polypeptide

Type of Paper: Article
Title: Molecular Modeling Interactions Among Sea Anemone Toxins and Kv1 Channels
Authors: A. Sabogal-Arango ^†, S. D. Garcia-Suarez ^†, G. E. Barreto, J. Gonzalez and Ludis Del Rosario Morales Alvarez *
Affiliation: Departamento de Nutrición y Bioquímica, Facultad de Ciencias, Pontificia Universidad Javeriana, Bogotá D.C, Colombia
^† These authors contributed equally to this work.
*   Author to whom correspondence should be addressed; E-Mail: ludis.morales@javeriana.edu.co.
Abstract: Sea anemone neurotoxins are peptides of which more than forty have been previously isolated and their atomic structures assessed. These toxins interact with Na+-K+ channels, resulting in specific alterations on their functions. These interactions are important for the treatment of nearly eighty autoimmune disorders. The aim of this study was to predict, the interaction complex toxins-Kv1, by homology modeling, molecular-docking, and computational alanine scanning. Our results show ten new predictive structural models of neurotoxins and binding-energy hot-spots in channel-neurotoxin interface. This knowledge may be useful to understand this interaction complex, and how this new information will serve as an input for the design of more promising drugs.
Keywords: sea anemones; neurotoxins; Kv1 channel; modeling; docking; energy minimization

Type of Paper: Review
Title: Sea Anemone Neurotoxins: A Computational Approach
Authors: A. Sabogal-Arango ^†, S. D. Garcia-Suarez ^†, G. E. Barreto, J. Gonzalez and Ludis Del Rosario Morales Alvarez
Affiliation: Departamento de Nutrición y Bioquímica, Facultad de Ciencias, Pontificia Universidad Javeriana, Bogotá D.C, Colombia
^† These authors contributed equally to this work.
Abstract: Recent attention has been devoted to sea anemone neurotoxins because of their function on blocking voltage gate potassium channels (Kv), showing a considerable hope for the treatment of autoimmune diseases, such as Multiple Sclerosis. Previous experimental paradigms demonstrate how neurotoxins are useful by reducing associated symptoms of this disease; however little information is available on how these neurotoxins might interact with Kv channel. Recent advances on computational methods are deemed to find specific peptides interaction in order to design better and specific drugs for treating diseases. Therefore, this review aims at discussing on how sea anemone toxins interact with potassium channels using bioinformatics tools, and how this may be considered a target for future drug design approach.
Keywords: sea anemone neurotoxins; Kv channel; bioinformatic; multiple sclerosis