μ-Conotoxin K IIIA is a cysteine-rich, disulfide-stabilized peptide used to probe voltage-gated sodium channel interactions. Its rigid structure supports highly selective binding studies. Researchers analyze folding pathways, solvent effects, and binding kinetics. Applications include neuropeptide research, channel-mapping studies, and structural biophysics.
CAT No: R2557
CAS No:884469-67-4
Synonyms/Alias:mu-Conotoxin K IIIA;UNII-390H5GUO40;CHEMBL2402969;390H5GUO40;884469-67-4;Ccncsskwcrdhsrcc-NH2 cyclic (1->9),(2->15),(4->16);L-Cysteinamide, L-cysteinyl-L-cysteinyl-L-asparaginyl-L-cysteinyl-L-seryl-L-seryl-L-lysyl-L-tryptophyl-L-cysteinyl-L-arginyl-L-alpha-aspartyl-L-histidyl-L-seryl-L-arginyl-L-cysteinyl-, cyclic (1->9),(2->15),(4->16)-tris(disulfide);mu-Conotoxin KIIIA;BDBM50492340;DA-68915;
mu-Conotoxin K IIIA is a peptide neurotoxin originally isolated from the venom of the marine cone snail *Conus kinoshitai*. As a member of the μ-conotoxin family, it is characterized by a compact structure stabilized by multiple disulfide bridges, conferring high specificity and affinity for voltage-gated sodium channels, particularly those of the Nav1 family. This peptide has garnered significant attention in neurobiological research due to its potent and selective inhibition of skeletal muscle sodium channels, making it a valuable molecular tool for dissecting ion channel function, neuronal excitability, and synaptic transmission. Its well-defined sequence and mechanism of action have positioned it as an essential reagent in the study of excitable tissues and sodium channelopathies.
Electrophysiological studies: mu-Conotoxin K IIIA is widely employed in electrophysiological investigations to selectively block Nav1.4 sodium channels in skeletal muscle preparations. By inhibiting these channels, researchers can isolate and characterize other ionic currents in muscle fibers or heterologous expression systems. The specificity of this peptide allows for precise delineation of sodium channel subtypes and their respective contributions to action potential generation and propagation, facilitating a deeper understanding of muscle excitability and related pathophysiology.
Ion channel pharmacology: The peptide serves as a reference ligand in ion channel pharmacology, enabling the validation and calibration of new assays targeting voltage-gated sodium channels. Its well-characterized binding profile is instrumental in screening potential modulators, benchmarking assay sensitivity, and elucidating structure-activity relationships within the sodium channel family. The use of μ-conotoxins in such studies supports the identification of novel channel modulators and advances the development of next-generation research tools.
Neurotoxin mechanism research: mu-Conotoxin K IIIA is utilized to investigate the molecular determinants of neurotoxin-channel interactions. By employing site-directed mutagenesis and comparative binding studies, researchers can map critical residues involved in toxin recognition and channel inhibition. These studies not only clarify the structural basis for subtype selectivity but also inform broader neurotoxin research, contributing to the understanding of peptide-protein interactions at the atomic level.
Peptide structure-function analysis: The unique disulfide-rich scaffold of mu-Conotoxin K IIIA makes it a model system for exploring the relationship between peptide structure and biological activity. Through synthetic modification, isotopic labeling, and NMR or crystallographic studies, scientists can probe the conformational stability, folding pathways, and dynamics of disulfide-bonded peptides. Insights gained from such analyses inform the rational design of engineered peptides with enhanced stability, selectivity, or modified pharmacological profiles for research applications.
Tool for synaptic transmission studies: By selectively inhibiting sodium channels involved in action potential initiation, mu-Conotoxin K IIIA provides a means to dissect the contribution of presynaptic and postsynaptic sodium currents to neurotransmitter release and synaptic plasticity. Its application in neuromuscular junction models and cultured neurons enables precise manipulation of excitability, offering critical insights into the mechanisms underlying synaptic integration, signal propagation, and channelopathies affecting neuromuscular function.
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