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Arthropod Venom Components and Their Potential Usage

This special issue belongs to the section “Animal Venoms“.

Special Issue Information

Dear Colleagues,

Thousands of arthropod species, ranging from arachnids (spiders and scorpions) to hymenopterans (ants, bees, and wasps) and myriapods (centipedes), are venomous and utilize their venoms for both defending themselves and predating preys. These venoms are invariably harmful to humans, and some may cause serious injuries, e.g., those from scorpions, spiders, and wasps. On the other hand, arthropods’ venoms have been known as rich sources of biologically active compounds and have attracted the attention of toxin researchers for years. Especially in this century, venom component analysis has progressed much more than ever because of the great advances of analytical techniques, in particular, mass spectrometry and next-generation deep (DNA and RNA) sequencing. As such, proteomic and peptidomic analyses utilizing LC–MS, as well as transcriptomics - alone or in combination with proteomics, have made it possible to fully analyze venoms’ components, revealing a variety of novel peptide and protein toxins sequences and scaffolds, potentially useful as pharmacological research tools and for the development of highly selective peptide ligands and therapeutic leads. Because of their specificity for numerous ion-channel subtypes, including voltage- and ligand-gated ion channels, arthropod neurotoxins have been investigated to dissect and treat neurodegenerative diseases and control epileptic syndromes. This Special Issue will collect information on such progress, encouraging contributions on the chemical and biological characterization of venom components, not only peptides and proteins but also small molecules, their mechanisms of action, and the development of venom-derived peptide leads.

Prof. Dr. Katsuhiro Konno
Prof. Dr. Gandhi Rádis-Baptista
Guest Editors

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Keywords

  • venom components
  • peptide toxins
  • protein toxins
  • proteomics
  • peptidomics
  • transcriptome
  • venomics
  • peptide ligand
  • peptide engineering
  • venom-derived peptide leads

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Toxins - ISSN 2072-6651