α-Conotoxin ImI is a disulfide-rich, cysteine-constrained peptide from cone snail venom targeting nicotinic receptor subtypes in research settings. Its compact fold and defined loop architecture enable high-affinity binding. Researchers examine structure-activity relationships via NMR and mutagenesis. Applications include ion-channel mapping, neurotoxin motif analysis, and conformational-stability studies.
CAT No: PI-024
CAS No:156467-85-5
Synonyms/Alias:alpha-Conotoxin imi;alpha-Ctx-imi;156467-85-5;Gly-cys-cys-ser-asp-pro-arg-cys-ala-trp-arg-cys-NH2;DTXSID10166085;Glycyl-cysteinyl-cysteinyl-seryl-asparginyl-prolyl-arginyl-cysteinyl-alanyl-tryptophyl-arginyl-cysteinamide;L-Cysteinamide, glycyl-L-cysteinyl-L-cysteinyl-L-seryl-L-alpha-aspartyl-L-prolyl-L-arginyl-L-cysteinyl-L-alanyl-L-tryptophyl-L-arginyl-, cyclic (2-8),(3-12)-bis(disulfide);alpha-CTX IMI;CHEMBL500076;DTXCID7088576;
Alpha-conotoxin ImI is a disulfide-rich peptide toxin derived from the venom of the marine cone snail *Conus imperialis*. As a member of the alpha-conotoxin family, it is characterized by its highly specific antagonistic activity toward neuronal nicotinic acetylcholine receptors (nAChRs), particularly the α7 subtype. Its unique sequence, compact structure, and potent receptor selectivity have made it an indispensable tool in neuropharmacological research and receptor characterization. The ability of alpha-conotoxin ImI to modulate synaptic transmission by targeting ligand-gated ion channels has driven significant advances in the understanding of cholinergic signaling pathways, making it a compound of considerable interest to neuroscientists and molecular pharmacologists.
Receptor pharmacology: Alpha-conotoxin ImI is widely employed in studies aimed at dissecting the pharmacological properties of neuronal nAChRs, especially those containing the α7 subunit. By serving as a highly selective antagonist, it allows researchers to differentiate between receptor subtypes in complex tissue preparations or heterologous expression systems. This specificity is instrumental in elucidating the functional roles of α7 nAChRs in synaptic transmission, neuroplasticity, and signal transduction, providing insights that are critical for both basic neuroscience and the development of novel modulators of cholinergic function.
Ion channel research: The peptide's capability to modulate ligand-gated ion channels makes it a valuable probe in electrophysiological and biophysical studies. Alpha-conotoxin ImI is routinely used to characterize the biophysical properties of nAChRs, such as ion selectivity, conductance, and gating kinetics. Its application enables precise mapping of receptor pharmacodynamics and assists in understanding the molecular mechanisms underlying ion channel regulation in neuronal and non-neuronal cells.
Structure-activity relationship (SAR) studies: Due to its well-defined structure and potent activity, alpha-conotoxin ImI serves as a model scaffold in SAR investigations. Researchers utilize it to explore the impact of specific amino acid substitutions, disulfide bond arrangements, and post-translational modifications on receptor binding and selectivity. Such studies are pivotal for designing novel peptide analogs with improved pharmacological profiles or altered receptor specificity, advancing the field of peptide-based neuropharmacology.
Neurochemical pathway mapping: The selective inhibition of α7 nAChRs by this peptide provides a means to delineate the role of these receptors in various neurochemical circuits. By applying alpha-conotoxin ImI in in vitro or ex vivo systems, investigators can map cholinergic pathways, assess receptor distribution, and study the downstream effects of receptor blockade on neurotransmitter release and synaptic integration. This approach is particularly valuable for unraveling the contributions of cholinergic signaling to cognitive processes, sensory integration, and neural development.
Peptide engineering and synthesis: Owing to its compact, cysteine-rich framework, alpha-conotoxin ImI is frequently used as a template in peptide synthesis and engineering. Its structural motifs serve as benchmarks for developing synthetic methodologies, optimizing disulfide bond formation, and exploring strategies for enhancing peptide stability. Furthermore, the peptide's amenability to chemical modification makes it a preferred candidate for generating labeled or conjugated derivatives, facilitating advanced studies in receptor imaging, ligand-receptor interaction assays, and bioanalytical applications.
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