Selective antagonist of α3β4 nicotinic acetylcholine receptors
CAT No: R1921
CAS No:216299-21-7
Synonyms/Alias:Alpha-Conotoxin AuIB;216299-21-7;A-CONOTOXIN AUIB;CHEMBL5434420;alpha-Conotoxin AuIB TFA;GTPL3973;BDBM50618165;AKOS024457439;DA-68901;Q27074396;
Chemical Name:2-[53-[(2-aminoacetyl)amino]-18-(2-amino-2-oxoethyl)-27-benzyl-6-carbamoyl-21-(1-hydroxyethyl)-48-(hydroxymethyl)-45-[(4-hydroxyphenyl)methyl]-24-methyl-8,11,17,20,23,26,29,32,38,44,47,50,52-tridecaoxo-3,4,55,56-tetrathia-7,10,16,19,22,25,28,31,37,43,46,49,51-tridecazapentacyclo[28.20.7.012,16.033,37.039,43]heptapentacontan-9-yl]acetic acid
α-Conotoxin AuIB is a disulfide-rich peptide toxin originally isolated from the venom of the marine cone snail *Conus auricularis*. As a member of the α-conotoxin family, it is characterized by its selective affinity for specific subtypes of nicotinic acetylcholine receptors (nAChRs), particularly those containing the α3β4 subunit composition. Its unique structural motifs and well-defined disulfide connectivity make it a highly valuable molecular tool for dissecting ligand-receptor interactions and for probing the functional diversity of ion channels in neurobiological research. The high degree of subtype selectivity and potent inhibitory activity have established α-Conotoxin AuIB as a reference compound in the study of neuronal signaling pathways and receptor pharmacology.
Neuropharmacology research: α-Conotoxin AuIB is widely utilized for the selective inhibition of α3β4 nAChRs in neural tissue preparations and recombinant expression systems. By providing a means to block specific receptor subtypes without affecting others, it enables researchers to delineate the physiological and pharmacological roles of these channels in synaptic transmission, neuronal excitability, and neurotransmitter release. Its use is particularly relevant in studies aimed at understanding the contributions of nAChRs to central and peripheral nervous system function.
Ion channel characterization: As a highly selective peptide ligand, α-Conotoxin AuIB serves as a critical tool for characterizing the biophysical and pharmacological properties of nicotinic acetylcholine receptor subtypes. In electrophysiological assays and ligand binding studies, it facilitates the identification and functional profiling of receptor isoforms, supporting the mapping of receptor distribution and the elucidation of structure-activity relationships. This application is essential for advancing knowledge of ion channel diversity and for validating targets in neurobiology.
Peptide structure-function analysis: The defined sequence and disulfide connectivity of α-Conotoxin AuIB make it an exemplary model for investigating the relationship between peptide structure and receptor binding specificity. Through site-directed mutagenesis, synthetic analog development, and conformational analysis, researchers can use this peptide to explore the determinants of molecular recognition, stability, and bioactivity. Insights gained from such studies inform the rational design of novel ligands with tailored selectivity profiles.
Pharmacological screening: Synthetic α-Conotoxin AuIB is commonly employed in high-throughput screening platforms to assess the activity of candidate compounds or natural extracts on nAChR function. By serving as a benchmark inhibitor, it allows for the comparative evaluation of antagonist potency, selectivity, and mechanism of action. This application supports the discovery and validation of new modulators of nicotinic receptors, which are of interest in both basic research and early-stage drug discovery efforts.
Venom peptide research and evolutionary studies: As a representative of the conotoxin superfamily, α-Conotoxin AuIB is instrumental in comparative studies investigating the molecular evolution, diversity, and adaptive significance of venom-derived peptides. Its inclusion in phylogenetic analyses and functional assays contributes to a broader understanding of peptide toxin evolution, conotoxin gene families, and the ecological roles of venom components in predator-prey interactions. Such research not only advances evolutionary biology but also expands the repertoire of bioactive peptides available for biotechnological applications.
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