Arthropod Venom Components and Their Potential Usage

Arthropod Venom Components and Their Potential Usage

0 Ungluers have Faved this Work
Thousands of arthropod species, ranging from arachnids (spiders and scorpions) to hymenopterans (ants, bees, and wasps) and myriapods (centipedes), are venomous and use their venoms for both defense and predation. These venoms are invariably harmful to humans, and some may cause serious injuries, e.g., those from scorpions, spiders, and wasps. Arthropods’ venoms are also known as rich sources of biologically active compounds and have attracted the attention of toxin researchers for years. In this century, venom component analysis has progressed considerable due to the advances in analytical techniques, in particular, mass spectrometry and next-generation deep (DNA and RNA) sequencing. As such, proteomic and peptidomic analyses using LC–MS have enabled the full analysis of venom 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, like chlorotoxin. Due to 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 collects 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.

This book is included in DOAB.

Why read this book? Have your say.

You must be logged in to comment.

Rights Information

Are you the author or publisher of this work? If so, you can claim it as yours by registering as an rights holder.


This work has been downloaded 54 times via ebook links.
  1. 18 - pdf (CC BY-NC-ND) at


  • acid-gated currents
  • acid-sensing ion channels
  • Acinetobacter baumannii
  • Alternative treatment
  • AMP
  • amphipathic ?-helix structure
  • ANT
  • antifeedant
  • antimicrobial peptide
  • antivenoms
  • Ants
  • Apoptosis
  • arthropod
  • automated patch-clamp
  • bee venom
  • Bees
  • Berberomeloe majalis
  • Bioinformatics
  • biotools
  • blister beetle
  • brown spider
  • cantharidin
  • Centruroides limpidus Karch
  • Chagas Disease
  • channel-like pore-forming activity
  • chemotherapy
  • Chronic Pain
  • cold allodynia
  • computational docking
  • cutaneous disease
  • de novo sequencing
  • Dinoponera quadriceps
  • directed disulfide bond formation
  • drug targets
  • envenomation
  • FMRF-amide
  • Formicidae
  • heart contractility
  • homology modelling
  • human African trypanosomiasis
  • hybrid immunogen
  • Hymenoptera
  • Hymenoptera venom
  • ICK peptide
  • ICK-like toxins
  • industrial biotechnology
  • insect immune system
  • insect neurotoxin
  • insecticidal peptide
  • ion channel structure
  • ixodicide
  • keratitis
  • knottins
  • leishmaniasis
  • linear cationic ?-helical peptide
  • Loxosceles
  • Loxosceles spp.
  • LTQ Orbitrap Hybrid Mass Spectrometer
  • LyeTxI-b
  • Malaria
  • mass spectrometric analysis
  • mass spectrometry analysis
  • mastoparan
  • mechanical allodynia
  • Mechanism
  • melittin
  • metalloproteases
  • myrmecology
  • n/a
  • natural antibiotics
  • NaV
  • Nav channel activity
  • Nav1.7
  • nematicide
  • neuropathic pain
  • neutralizing antibodies
  • novel therapeutics
  • oxaliplatin
  • Pain
  • pain target
  • Peptides
  • pH regulation
  • Pharmacology
  • phospholipases D
  • pilosulin-like peptide
  • piperidine heterocyclic amines
  • protein–peptide interactions
  • proteome
  • Proteomics
  • protons
  • recombinant toxins
  • scorpion
  • scorpion venom
  • Skin
  • small hive beetle
  • solitary wasp
  • spider toxin
  • spider venom
  • Staphylococcus aureus
  • stent
  • Tenebrio molitor
  • tertiapin
  • toxins
  • toxoplasmosis
  • transcriptome
  • venom
  • venom allergens
  • venom peptides
  • venom toxicity
  • virtual screening
  • voltage-gated sodium channel
  • Wasps


DOI: 10.3390/books978-3-03928-541-9


edition cover
edition cover


Copy/paste this into your site: