Jingzhaotoxin-XII is a spider-venom peptide stabilized by multiple disulfide bridges, producing a compact, highly folded scaffold. Residues are arranged to recognize specific ion channels with high affinity. Researchers use electrophysiological assays and structural methods to define channel-binding epitopes. Applications include toxin-motif engineering, ion-channel pharmacology, and disulfide-rich peptide design.
CAT No: R2868
Jingzhaotoxin-XII is a peptide toxin originally isolated from the venom of the Chinese tarantula Chilobrachys jingzhao. As a member of the spider toxin family, it is characterized by a distinctive disulfide-rich structure that imparts high stability and specificity toward voltage-gated ion channels. This peptide is of considerable interest within neuropharmacology and ion channel research due to its ability to modulate neuronal excitability and synaptic transmission. Its unique mode of action and well-defined molecular composition make it a valuable resource for advancing studies in neurobiology, toxinology, and the development of ion channel-targeted tools.
Ion channel modulation: Jingzhaotoxin-XII is widely utilized in the investigation of voltage-gated sodium and potassium channels, serving as a potent and selective modulator. Its peptide structure enables precise binding to specific channel subtypes, allowing researchers to dissect the functional roles of these channels in neuronal signaling. By inhibiting or altering channel activity, the toxin provides a powerful means to study the mechanisms underlying electrical excitability, neurotransmission, and the pathophysiology of channelopathies in both in vitro and ex vivo models.
Neuropharmacological tool development: Owing to its high affinity and specificity for certain neuronal ion channels, this peptide has become an important molecular probe in neuropharmacological research. Scientists employ it to map the distribution, pharmacological properties, and physiological contributions of target channels in central and peripheral nervous systems. Its application facilitates the identification of channel subtypes involved in pain perception, synaptic plasticity, and excitotoxicity, thereby contributing to the elucidation of complex neural circuits and signaling pathways.
Structure-function relationship studies: The well-defined three-dimensional fold and stable disulfide framework of Jingzhaotoxin-XII make it an exemplary model for exploring peptide-channel interactions at the molecular level. Researchers leverage its structural characteristics to investigate how specific amino acid residues contribute to channel binding and selectivity. Insights gained from these studies inform the rational design of novel peptide-based modulators and enhance understanding of the molecular determinants governing toxin-ion channel specificity.
Peptide engineering and synthetic biology: The robust scaffold and bioactivity of this spider toxin peptide provide a template for the development of engineered analogs with tailored properties. Through site-directed mutagenesis, chemical synthesis, or recombinant expression, scientists can generate variants to optimize selectivity, potency, or pharmacokinetic characteristics. Such engineered peptides are valuable for expanding the toolkit of ion channel modulators and for probing the structure-activity relationships critical to peptide-based drug discovery and synthetic biology applications.
Venom peptide research and evolutionary studies: As a representative of spider-venom-derived peptides, Jingzhaotoxin-XII contributes to comparative studies of toxin evolution, structure, and function. Its inclusion in venom profiling and phylogenetic analyses aids in decoding the molecular diversity and adaptive significance of spider toxins. These investigations not only enhance understanding of venom evolution but also support the discovery of novel bioactive peptides with potential applications across neurobiology, pharmacology, and biotechnology.
2. The spatiotemporal control of signalling and trafficking of the GLP-1R
3. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
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