Charybdotoxin is a peptide found in the venom of the scorpion Leiurus quinquestriatus. Specific inhibitor of the big conductance Ca2+-activated K+ channel.
CAT No: R1820
CAS No:95751-30-7
Synonyms/Alias:CHARYBDOTOXIN;CTX Toxin;95751-30-7;Quinquestriatus Toxin;Lqh alpha IT Recombinant;115422-61-2;Charybdotoxin (reduced);CHARYBDOTOXIN (Native);ChTX;Toxin, CTX;Toxin, Quinquestriatus;DTXSID30897182;ChTx-a;ChTX-Lq1;DTXCID701326593;Potassium channel toxin alpha-KTx 1.1;DA-51822;FC110443;Pyr-Phe-Thr-Asn-Val-Ser-Cys-Thr-Thr-Ser-Lys-Glu-Cys-Trp-Ser-Val-Cys-Gln-Arg-Leu-His-Asn-Thr-Ser-Arg-Gly-Lys-Cys-Met-Asn-Lys-Lys-Cys- Arg-Cys-Tyr-Ser-OH; pE-FTNVSCTTSKECWSVCQRLHNTSRGKCMNKKCRCYS-OH;
Charybdotoxin is a peptide neurotoxin originally isolated from the venom of the scorpion Leiurus quinquestriatus hebraeus. As a 37-amino acid peptide, it is renowned for its high-affinity and selective inhibition of various voltage-gated potassium channels, particularly those of the Kv1 family, as well as some calcium-activated potassium channels. Its well-characterized structure and specific channel-blocking activity have made it an indispensable molecular tool in neurophysiology, ion channel research, and pharmacological studies. The unique binding properties and sequence-defined structure of charybdotoxin underpin its significance in advancing the understanding of ion channel function and regulation in excitable cells.
Electrophysiological research: Charybdotoxin is widely utilized in electrophysiological investigations to dissect the functional roles of specific potassium channels in neuronal and muscle tissues. By selectively blocking Kv1.2, Kv1.3, and certain large-conductance Ca2+-activated K+ channels (BK channels), it enables researchers to isolate and characterize the contribution of these channels to membrane potential regulation, action potential shaping, and synaptic transmission. Its application in patch-clamp studies allows for precise modulation of channel activity, facilitating the elucidation of channel gating mechanisms and pharmacological sensitivities.
Ion channel pharmacology: The peptide serves as a reference inhibitor in ion channel pharmacology, supporting the identification and functional classification of potassium channel subtypes. By providing a benchmark for channel blockade, charybdotoxin assists in the screening and validation of novel channel modulators, including small molecules and biologics. Its high specificity and well-mapped binding interface allow for the comparative assessment of channel inhibitor potency and selectivity, which is crucial for drug discovery and the development of channel-targeted therapeutics.
Peptide structure-function studies: Charybdotoxin is frequently employed as a model system in peptide structure-function research. Its defined sequence, disulfide-rich tertiary structure, and well-characterized channel interactions make it ideal for mutagenesis studies, conformational analysis, and peptide engineering. Researchers use it to probe the molecular determinants of ion channel recognition, investigate structure-activity relationships, and design modified peptides with altered selectivity or stability for experimental applications.
Neuroscience research: The neurotoxic properties of charybdotoxin are exploited in neuroscience to explore the physiological and pathophysiological roles of potassium channels in neuronal excitability, synaptic integration, and signal propagation. By modulating channel activity in brain slices, cultured neurons, or heterologous expression systems, it enables the study of potassium channel contributions to processes such as neurotransmitter release, synaptic plasticity, and network oscillations. Its use provides critical insights into the molecular underpinnings of neuronal signaling and the potential consequences of channel dysfunction.
Toxin-receptor interaction analysis: Charybdotoxin is a valuable probe for investigating the molecular interactions between peptide toxins and their ion channel targets. Its application in binding assays, crystallography, and computational modeling supports the mapping of toxin-channel interfaces, identification of key contact residues, and elucidation of binding kinetics. Such studies advance the broader understanding of peptide-protein recognition, inform rational design of channel modulators, and contribute to the development of biosensors or diagnostic tools based on selective channel blockade.
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