SCYLLATOXIN [Tyr2]-

Product Name:SCYLLATOXIN [Tyr2]-

Purity:95%

Molar Mass:3447

Storage:Store at -20 degrees Celsius

Target:SK channels

Application:

[Tyr2]-Scyllatoxin is a synthetic analog of the scorpion toxin scyllatoxin, modified at the second amino acid position with tyrosine (Tyr). This peptide toxin is known for its ability to inhibit specific potassium channels, particularly small-conductance calcium-activated potassium channels (SK channels). By blocking these channels, [Tyr2]-Scyllatoxin affects cellular excitability and neurotransmitter release, making it a valuable tool in research focused on the role of SK channels in neurophysiology and cardiac function. Its high specificity and modified structure enhance its utility in studies exploring the regulation of neuronal activity, synaptic plasticity, and the development of therapeutic agents targeting SK channel-related disorders.

Current Research:

Scyllatoxin [Tyr2] is a modified peptide toxin derived from Leiurus quinquestriatus hebraeus, the Israeli scorpion. This peptide is a variant of Scyllatoxin, with a substitution of tyrosine at position 2. It belongs to the class of short-chain scorpion toxins known for their high specificity toward potassium (K?) ion channels. Its sequence is stabilized by disulfide bridges, ensuring structural rigidity and functional precision.

Mechanism of Action
Scyllatoxin [Tyr2] specifically targets small-conductance calcium-activated potassium (SK) channels. By binding to the extracellular vestibule of these channels, it blocks K? ion flow, disrupting the maintenance of the afterhyperpolarization phase in neurons. This inhibition affects neuronal firing patterns, making the peptide an essential tool for studying SK channel function in excitability and synaptic plasticity.

Research Applications
The substitution of tyrosine at position 2 alters the binding dynamics of Scyllatoxin [Tyr2], offering unique properties for experimental applications. It is frequently used to:

Investigate SK Channel Physiology: This modified toxin provides insights into the role of SK channels in regulating neuronal excitability, firing precision, and calcium-dependent feedback mechanisms.

Develop Ion Channel Therapeutics: Scyllatoxin [Tyr2] serves as a model for designing channel-specific drugs to treat conditions like epilepsy, ataxia, and other channelopathies.

High-Throughput Screening: Its robust and well-characterized interaction with SK channels makes it valuable in pharmacological assays aimed at identifying novel modulators.

Structural Insights
Scyllatoxin [Tyr2] retains the disulfide-stabilized alpha-beta fold typical of scorpion toxins. The Tyr2 modification enhances its binding affinity and specificity, offering a unique angle for exploring toxin-channel interactions.

Conclusion
Scyllatoxin [Tyr2] stands out as a versatile tool in neurophysiology and pharmacology. Its tailored specificity for SK channels and robust performance in experimental settings make it an invaluable asset in ion channel research and drug discovery.

Reference:

Auguste, P., Hugues, M., Grave, B., Gesquiere, J. C., Maes, P., Tartar, A., ... & Lazdunski, M. (1990). Leiurotoxin I (scyllatoxin), a peptide ligand for Ca2 (+)-activated K+ channels. Chemical synthesis, radiolabeling, and receptor characterization.?