An effective and selective competitive antagonist for α3β2 subunit-containing nicotinic receptors (IC50 = 0.5 - 3.5 nM at α3β2 expressed in Xenopus oocytes), and also potently blocks β3-containing neuronal nicotinic receptors.
CAT No: R0920
CAS No:175735-93-0
Synonyms/Alias:175735-93-0;AKOS024456535;PD079152;
α-Conotoxin MII is a peptide neurotoxin derived from the venom of the marine cone snail species Conus magus. As a member of the α-conotoxin family, this small, disulfide-rich peptide is renowned for its potent and selective inhibition of neuronal nicotinic acetylcholine receptors (nAChRs), particularly the α3β2 and α6-containing subtypes. Its unique structural features and high receptor specificity make it an invaluable molecular tool for dissecting cholinergic signaling pathways in the central nervous system. Researchers leverage its well-characterized binding properties to probe synaptic transmission, receptor pharmacology, and the functional diversity of nAChR subtypes, thereby advancing fundamental neurobiological understanding.
Neuropharmacology research: α-Conotoxin MII is widely employed in neuropharmacological studies to selectively block specific nAChR subtypes in neuronal preparations. By inhibiting α3β2 and α6-containing receptors, it allows investigators to delineate the contributions of these channels to synaptic transmission, neurotransmitter release, and neural circuit modulation. Its use facilitates the mapping of cholinergic pathways implicated in processes such as pain perception, reward, and neurodegeneration, enabling targeted exploration of receptor function without off-target effects on other cholinergic subtypes.
Receptor subtype characterization: The peptide serves as a critical ligand for distinguishing among closely related nAChR subtypes in both native tissues and recombinant expression systems. Its high affinity and selectivity permit precise pharmacological profiling, supporting the identification and quantification of receptor populations in complex biological samples. Such studies are essential for understanding the molecular diversity of nAChRs and for developing subtype-selective modulators for research applications.
Structure-function analysis: α-Conotoxin MII is frequently utilized in structure-activity relationship investigations aimed at elucidating the determinants of ligand-receptor interactions within the nAChR family. By introducing targeted modifications to the peptide sequence or employing it as a reference ligand, researchers can probe the molecular basis of binding affinity and selectivity. These insights inform the rational design of novel conotoxin analogs and contribute to the broader field of peptide-based neuropharmacology.
Electrophysiological studies: The compound is a valuable tool in electrophysiological experiments, such as patch-clamp recordings, for isolating and analyzing the functional properties of specific nAChR subtypes in neurons or heterologous systems. Its application enables the selective inhibition of target channels, thereby clarifying their roles in membrane excitability, synaptic integration, and neuronal signaling dynamics. Such data are critical for constructing accurate models of cholinergic neurotransmission in both health and disease.
Peptide-based probe development: Owing to its well-defined structure and receptor specificity, α-Conotoxin MII serves as a template for the development of novel peptide-based probes and affinity reagents. Researchers exploit its scaffold to design fluorescently labeled or chemically modified analogs for use in imaging, receptor localization, and affinity purification protocols. These tools expand the experimental repertoire available for studying nAChR biology and facilitate high-resolution investigations of receptor distribution and function in diverse biological systems.
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