Cn2 Toxin is a scorpion venom peptide stabilized by multiple disulfide bonds, producing a rigid scaffold suited for ion-channel interrogation. The structured loops formed by cysteines generate selective channel-binding surfaces. Researchers characterize its conformational constraints using electrophysiology and spectroscopy. Applications include toxin engineering, ion-channel mapping, and disulfide-rich peptide analysis.
CAT No: R2845
Synonyms/Alias:beta-scorpion toxin Cn2; beta-mammal toxin Cn2; Toxin 2; Toxin II.9.2.2; GTPL2632
Cn2 toxin is a well-characterized peptide toxin derived from the venom of the scorpion Centruroides noxius, notable for its high specificity towards voltage-gated sodium channels, particularly Nav1.6 subtypes. As a member of the α-scorpion toxin family, it modulates channel inactivation kinetics, making it a valuable molecular probe in neurophysiological and ion channel research. The unique structure and functional properties of Cn2 toxin have established its importance for dissecting the mechanisms of sodium channel gating, mapping channel subunit interactions, and exploring the molecular pharmacology of excitable membranes. Its defined peptide sequence and established activity profile support its use in a range of experimental and analytical applications within neurobiology, electrophysiology, and toxinology.
Electrophysiological studies: Cn2 toxin is widely employed as a tool in electrophysiological assays to investigate the functional dynamics of voltage-gated sodium channels. By selectively binding to receptor site 3 on the channel, it inhibits fast inactivation, resulting in prolonged sodium current. This property enables researchers to analyze channel gating mechanisms, characterize inactivation-deficient mutants, and study the physiological consequences of altered sodium channel kinetics in neuronal and muscular preparations. Its application is particularly relevant for patch-clamp experiments and voltage-clamp protocols aimed at dissecting channel subtype specificity and pharmacological modulation.
Neuropharmacology research: As a potent modulator of sodium channel activity, Cn2 toxin serves as a reference compound for screening and characterizing potential sodium channel blockers or modulators. Its defined mechanism of action allows for the differentiation of compound effects on channel inactivation versus activation, providing a robust platform for drug discovery efforts targeting neurological disorders associated with sodium channel dysfunction. The use of this peptide toxin in competitive binding and functional assays aids in identifying novel ligands and elucidating structure-activity relationships for channel-targeted therapeutics.
Structural and biophysical analysis: The well-defined interaction between Cn2 toxin and sodium channels makes it an ideal molecular probe for structural studies. Researchers utilize this toxin in conjunction with techniques such as cryo-electron microscopy and X-ray crystallography to visualize channel-toxin complexes at high resolution. These studies contribute to the detailed mapping of toxin binding sites, elucidation of channel conformational states, and understanding of gating transitions, thereby advancing knowledge of channel architecture and function at the molecular level.
Peptide engineering and synthesis: The sequence and structure of Cn2 toxin provide a template for the design and synthesis of novel peptide analogs with altered specificity or potency. Synthetic variants and site-directed mutants are generated to probe structure-function relationships, optimize pharmacological properties, or develop new research tools for ion channel studies. The peptide's amenability to chemical modification supports investigations into toxin engineering, molecular evolution, and the development of tailored probes for advanced neurobiological applications.
Toxinology and comparative venom research: Cn2 toxin is frequently utilized in comparative studies of scorpion venom composition and function. Its activity profile and sequence serve as benchmarks for the identification and classification of related α-toxins from other scorpion species. By enabling the functional annotation of venom components and facilitating evolutionary analyses, it supports broader investigations into venom diversity, adaptation, and the ecological roles of peptide toxins in predator-prey interactions. This comparative approach enhances the understanding of toxin evolution and the molecular basis of venom efficacy.
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