Product Description | YCQKWLWTCDSERKCCEDMVCRLWCKKRL is a linear 30-amino acid peptide derived from the venom of the tarantula Grammostola spatulata (GsAF-I). It functions as a potent modulator of voltage-gated ion channels, particularly tetrodotoxin (TTX)-sensitive sodium channels (NaV) and KV11.1 potassium channels. Venom-derived peptides like GsAF-I are of interest for their analgesic, anticancer, and ion-channel modulatory properties, providing templates for drug development and neurophysiological studies. Molecular details
- Sequence: Y-C-Q-K-W-L-W-T-C-D-S-E-R-K-C-C-E-D-M-V-C-R-L-W-C-K-K-R-L, linear sequence
- Length: 30 residues
- Molecular Formula: C160H245N47O41S7
- Molecular Weight: ~3926.0 Da
- Structural Features: The native peptide contains six cysteines forming three disulfide bonds, characteristic of spider-venom ICK (inhibitor cystine knot) peptides. This motif stabilizes the peptide structure, enhancing affinity for ion channels and proteolytic stability. Functional roles & mechanism
GsAF-I selectively inhibits TTX-sensitive NaV channels and KV11.1 channels, modulating neuronal excitability and cardiac repolarization. The peptide interacts with voltage sensor domains and pore regions of the channels, altering gating kinetics. Such modulatory effects explain the peptide’s analgesic and neuroactive properties and its potential to investigate ion-channel physiology. Applications
- Neuroscience research: Studying ion-channel gating, neuronal excitability, and synaptic transmission.
- Drug discovery: Template for analgesics targeting NaV channels or modulators of cardiac KV11.1 channels.
- Venom-derived therapeutics: Development of bioactive peptides for pain management and potentially anticancer applications. References
1. Kuhn-Nentwig L, et al. “Anticancer, antimicrobial, and analgesic activities of spider venoms.” PMC6060684, 2018. |
Scientific Background | GsAF-I Spider Venom Peptide is a 29-residue synthetic peptide with the sequence Tyr-Cys-Gln-Lys-Trp-Leu-Trp-Thr-Cys-Asp-Ser-Glu-Arg-Lys-Cys-Cys-Glu-Asp-Met-Val-Cys-Arg-Leu-Trp-Cys-Lys-Lys-Arg-Leu. The sequence contains 6 cysteine residues, providing potential thiol/disulfide chemistry when the thiol is available; contains 4 Lys and 3 Arg residues, contributing cationic character; contains 4 aromatic residues that can contribute to hydrophobic or aromatic interactions. These sequence-derived properties describe the reagent chemically; no specific receptor, enzyme, pathway, disease association, or biological activity is assigned without product-specific experimental evidence. |
Experimental Notes | Sequence-derived chemical properties support reagent selection and experimental planning but do not establish biological function. Solubility, aggregation, adsorption, conjugation efficiency, and assay performance should be validated under the intended experimental conditions. |
