Publication Date:
2023-12-21
Description:
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.
Keywords:
R5-920
;
RA1190-1270
;
n/a
;
spider toxin
;
hybrid immunogen
;
channel-like pore-forming activity
;
venom peptides
;
chemotherapy
;
piperidine heterocyclic amines
;
computational docking
;
insect immune system
;
venom
;
toxoplasmosis
;
wasps
;
ion channel structure
;
mechanical allodynia
;
Dinoponera quadriceps
;
natural antibiotics
;
bees
;
acid-gated currents
;
nematicide
;
novel therapeutics
;
toxins
;
protons
;
Hymenoptera venom
;
ants
;
chronic pain
;
heart contractility
;
transcriptome
;
drug targets
;
skin
;
peptides
;
LTQ Orbitrap Hybrid Mass Spectrometer
;
cantharidin
;
Centruroides limpidus Karch
;
pilosulin-like peptide
;
mechanism
;
scorpion
;
stent
;
homology modelling
;
amphipathic ?-helix structure
;
Berberomeloe majalis
;
mass spectrometric analysis
;
phospholipases D
;
Nav1.7
;
biotools
;
metalloproteases
;
myrmecology
;
Tenebrio molitor
;
antifeedant
;
ixodicide
;
virtual screening
;
Loxosceles
;
acid-sensing ion channels
;
small hive beetle
;
knottins
;
Nav channel activity
;
envenomation
;
pharmacology
;
Staphylococcus aureus
;
spider venom
;
scorpion venom
;
insecticidal peptide
;
Formicidae
;
AMP
;
de novo sequencing
;
tertiapin
;
leishmaniasis
;
brown spider
;
proteome
;
keratitis
;
Acinetobacter baumannii
;
neuropathic pain
;
bee venom
;
bioinformatics
;
ICK peptide
;
human African trypanosomiasis
;
automated patch-clamp
;
Hymenoptera
;
antimicrobial peptide
;
LyeTxI-b
;
linear cationic ?-helical peptide
;
melittin
;
Chagas disease
;
mass spectrometry analysis
;
neutralizing antibodies
;
apoptosis
;
protein–peptide interactions
;
malaria
;
pH regulation
;
voltage-gated sodium channel
;
venom toxicity
;
insect neurotoxin
;
solitary wasp
;
oxaliplatin
;
arthropod
;
mastoparan
;
cold allodynia
;
pain target
;
cutaneous disease
;
pain
;
NaV
;
proteomics
;
industrial biotechnology
;
ant
;
directed disulfide bond formation
;
antivenoms
;
blister beetle
;
venom allergens
;
ICK-like toxins
;
Loxosceles spp.
;
alternative treatment
;
recombinant toxins
;
FMRF-amide
;
bic Book Industry Communication::M Medicine
Language:
English
Format:
application/octet-stream
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