CTX 1211 is a peptide-like research scaffold derived from toxin-inspired sequence motifs used to probe ion-channel or receptor interactions. Hydrophobic and charged residues are arranged to yield structured binding interfaces. Researchers examine its conformational ensemble and activity in electrophysiological or binding assays. Applications include toxin-mimetic design, channel-mapping studies, and structure-activity exploration.
CAT No: R2865
Synonyms/Alias:N-acetyl-L-arginyl-L-cysteinyl-D-alanyl-L-arginyl-D-phenylalanyl-L-arginyl-L-tryptophyl-L-cysteinamide (2->8)-disulfide trifluoroacetic acid
CTX 1211 is a synthetic peptide compound engineered for advanced biochemical research applications, particularly within the fields of neurobiology and ion channel studies. As a member of the conotoxin family, CTX 1211 is characterized by its unique disulfide-rich structure and high specificity for certain voltage-gated ion channels. Its molecular architecture enables precise modulation of neuronal signaling pathways, making it an invaluable tool for probing the function and pharmacology of membrane proteins. The compound's distinct sequence and conformational stability provide researchers with a reliable platform for dissecting complex biological processes at the molecular level.
Ion Channel Research: CTX 1211 serves as a potent and selective modulator of voltage-gated ion channels, particularly those implicated in neuronal excitability and synaptic transmission. Its ability to interact with specific channel subtypes allows researchers to delineate the physiological and pharmacological roles of these membrane proteins. By employing this peptide in electrophysiological assays, investigators can elucidate channel gating mechanisms, identify binding sites, and characterize subtype-selective interactions, thereby advancing the understanding of ion channel function in both healthy and diseased states.
Neuropharmacology Studies: The peptide's high affinity and selectivity for neuronal targets make it a valuable probe in neuropharmacological research. CTX 1211 can be utilized to investigate the molecular basis of neurotransmission, synaptic plasticity, and neurotoxicity. Its application enables detailed mapping of neuronal circuitry and assessment of how ion channel modulation impacts cellular signaling. Researchers can further employ the compound in screening assays to evaluate the effects of novel small molecules or biologics on channel activity, facilitating the discovery of new pharmacological modulators.
Peptide Structure-Activity Relationship Analysis: CTX 1211 is frequently used as a model system for structure-activity relationship (SAR) studies within the conotoxin class. Its well-defined sequence and disulfide bond pattern provide an excellent framework for systematic mutagenesis and synthetic modification. By analyzing the impact of specific amino acid substitutions or chemical alterations, scientists can gain critical insights into the determinants of channel selectivity, binding affinity, and peptide stability. These findings inform the rational design of next-generation peptide modulators with improved properties.
Biochemical Tool Development: The unique properties of CTX 1211 support its integration into a range of assay systems and biochemical toolkits. Its application extends to the development of fluorescence-based detection assays, affinity purification reagents, and biosensors for real-time monitoring of ion channel activity. The peptide's robust binding characteristics and defined molecular target profile make it an ideal candidate for constructing high-specificity biochemical probes, which are essential for both basic research and high-throughput screening platforms.
Synthetic Peptide Optimization: CTX 1211 also plays a pivotal role in advancing peptide synthesis methodologies. Its complex folding and multiple disulfide bridges present a challenging yet instructive template for optimizing solid-phase peptide synthesis, folding protocols, and purification strategies. Researchers utilize the peptide to validate synthetic approaches, benchmark folding efficiency, and assess the scalability of production processes. Insights gained from these optimization efforts contribute to the broader field of peptide engineering, enabling the development of structurally complex bioactive peptides for diverse applications.
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