Toxin II (Anemonia sulcata) presents a compact, cysteine-rich peptide noted for its stable disulfide framework. The rigid fold supports studies of ion-channel interaction motifs and structural constraints. Researchers investigate its conformational stability across varied conditions. Applications include toxin-motif mapping, structural biology, and molecular-recognition research.
CAT No: R2507
CAS No:60748-45-0
Synonyms/Alias:Toxin II (anemonia sulcata);Sea anemone toxin II;anemonia toxin II;SE toxin II;60748-45-0;anemone toxin ATX-II;Av2 sea anemone toxin;sea anemone toxin Av2;ATX II;Anemonia Sulcata Toxin II;toxin ii, anemonia sulcata;DTXSID30897228;DTXCID901326618;69071-93-8;
Toxin II (Anemonia sulcata) is a peptide neurotoxin derived from the venom of the Mediterranean sea anemone, Anemonia sulcata. As a member of the sea anemone toxin family, it is characterized by its potent and selective interactions with voltage-gated sodium channels in excitable membranes. The structural features of this peptide, including its disulfide bond-stabilized conformation, confer both high affinity and specificity for particular sodium channel subtypes. Due to these unique biochemical properties, toxin II has become a valuable molecular tool in neurophysiological research, ion channel pharmacology, and the broader study of membrane excitability and signal transduction.
Electrophysiological studies: One of the primary applications of this peptide lies in its use as a probe for electrophysiological experiments investigating voltage-gated sodium channels. By binding to neurotoxin receptor site 3 on sodium channels, it inhibits channel inactivation and prolongs action potentials in nerve and muscle cells. Researchers utilize these effects to dissect the gating mechanisms of sodium channels, map channel subunit topology, and differentiate among channel isoforms in various tissues. Its well-defined and reproducible modulatory action offers a precise means to interrogate the functional roles of sodium channels under physiological and pathophysiological conditions.
Ion channel pharmacology: In the field of ion channel drug discovery, toxin II serves as a benchmark ligand for screening and characterizing novel compounds targeting sodium channels. Because its binding site and mechanism are well understood, it is frequently employed in competitive binding assays, structure-activity relationship studies, and the validation of channel modulators. This enables researchers to assess the selectivity and potency of candidate molecules, facilitating the development of more specific ion channel modulators for research and industrial applications.
Neurobiology research: The peptide's ability to modulate neuronal excitability makes it an indispensable tool for exploring the molecular underpinnings of nerve impulse generation and propagation. By selectively altering sodium channel function, it allows scientists to investigate the contributions of different channel subtypes to neuronal firing patterns, synaptic transmission, and network activity. Such studies are crucial for advancing the understanding of fundamental neurobiological processes and for modeling diseases associated with sodium channel dysfunction.
Structure-function analysis: Toxin II is widely used in studies aiming to elucidate the structural determinants of peptide-toxin interactions with their protein targets. Through site-directed mutagenesis, molecular modeling, and biophysical assays, researchers employ this peptide to map critical residues involved in channel binding and to probe conformational changes upon toxin association. These insights inform both the design of synthetic analogs with tailored properties and the broader understanding of peptide-protein recognition mechanisms.
Peptide synthesis and engineering: Beyond its direct use as a research tool, the structural features of toxin II have inspired efforts in peptide synthesis and engineering. Its stable scaffold and defined bioactivity make it a template for the design of novel peptides with improved pharmacological profiles or altered target specificity. Synthetic chemists and protein engineers use it as a model for developing new bioactive molecules, which can be applied in fundamental research, biosensor development, and the creation of molecular probes for advanced analytical techniques.
1. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
2. Implications of ligand-receptor binding kinetics on GLP-1R signalling
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