Toxin C(13)S(2)C(3) is a cysteine-rich toxin peptide variant where selective Cys-to-Ser replacements shift disulfide topology. Such substitutions alter folding pathways, stability, and channel-recognition profiles. Researchers analyze its three-dimensional structure and bioactivity relative to native toxin. Applications include disulfide engineering, ion-channel mapping, and toxin-structure studies.
CAT No: R2600
CAS No:74504-53-3
Synonyms/Alias:Toxin C13S2C3;alpha-Dendrotoxin;74504-53-3;Toxin C-S2-C;Toxin C(13)S(2)C(3);FD108355;
Toxin C(13)S(2)C(3) is a synthetic peptide compound that mimics a specific structural motif found in certain naturally occurring toxins. As a member of the peptide toxin family, it features a defined sequence and distinct disulfide bridge arrangement, enabling researchers to explore its biochemical properties and functional interactions in a controlled laboratory setting. Its unique configuration makes it a valuable tool for investigating ion channel modulation, receptor binding, and protein-protein interactions, supporting advanced research in molecular pharmacology, neurobiology, and peptide structure-activity relationships.
Ion Channel Modulation Studies: Synthetic peptide toxins such as Toxin C(13)S(2)C(3) are widely utilized in research focused on the modulation of voltage-gated or ligand-gated ion channels. By providing a structurally defined ligand, this peptide enables precise characterization of channel subtypes, gating mechanisms, and pharmacological sensitivities. Its selective binding properties facilitate the dissection of ion channel function in excitable cells, supporting the identification of critical domains involved in channel activation, inactivation, or blockade.
Receptor Binding Analysis: The defined sequence and disulfide connectivity of Toxin C(13)S(2)C(3) make it an excellent molecular probe for studying receptor-ligand interactions. Researchers employ this peptide to map binding sites, quantify affinity, and assess receptor specificity, particularly for membrane proteins involved in signal transduction. Its use in radioligand binding assays, fluorescence-based detection, or surface plasmon resonance experiments allows for detailed kinetic and thermodynamic analysis of peptide-receptor engagement.
Structure-Activity Relationship (SAR) Research: Toxin C(13)S(2)C(3) serves as a model system for systematic structure-activity relationship studies, enabling modifications at specific residues to elucidate the contributions of side chains, backbone conformation, and disulfide bridges to biological activity. By comparing native and engineered analogs, researchers can identify determinants of potency, selectivity, and stability, informing the rational design of novel bioactive peptides or therapeutic leads.
Peptide Synthesis and Analytical Method Development: The well-characterized nature of this peptide toxin provides a benchmark for optimizing solid-phase peptide synthesis protocols and validating analytical techniques such as high-performance liquid chromatography (HPLC) and mass spectrometry. Its defined sequence and folding requirements challenge synthetic and purification workflows, aiding in the development of robust methods for producing complex, cysteine-rich peptides with correct disulfide connectivity.
Protein-Protein Interaction Mapping: Toxin C(13)S(2)C(3) is frequently applied in studies aimed at elucidating protein-protein interactions, particularly those involving membrane-bound targets or extracellular domains. By acting as a molecular probe, it can help identify interaction partners, characterize binding interfaces, and reveal conformational changes upon complex formation. These insights contribute to a deeper understanding of cellular signaling pathways and the molecular basis of toxin action, supporting broader applications in functional proteomics and drug discovery.
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