Product Name | Ac-FVKILRYENEVLQLEEDEDF- NH2 |
Product Quantity | 4 mg |
Catalog Number | 5235 |
Category | Peptide |
Molecular Weight | 2569.85 |
Formula | C117H177N27O38 |
Sequence | Ac-FVKILRYENEVLQLEEDEDF- NH2 |
Purity | >95% |
Modifications | Acetylation, Amidation |
Product Description | FVKILRYENEVLQLEEDEDF (βadp1). This 20-amino-acid peptide maps to the Ig-like extracellular domain of the voltage-gated sodium channel β1 subunit (SCN1B). It is specifically located within residues 1–20 of the Ig loop and has been named βadp1. Structural modeling and docking studies demonstrate that βadp1 binds to the adhesion interface of the β1 Ig domain, functioning as a competitive inhibitor of β1-mediated intercellular adhesion. Functional & Experimental Applications - Inhibition of Intercellular Adhesion: βadp1 significantly and dose-dependently reduces junctional electrical resistance in cell monolayers overexpressing the sodium channel β1 subunit, but has no effect in parental cells lacking β1.
- Implications for Cardiac Electrophysiology: β1-mediated adhesion at the perinexus—the region adjacent to gap junctions—is critical for action potential propagation between cardiomyocytes. By interfering with this adhesion, βadp1 provides insight into novel targets for anti-arrhythmic strategies
βadp1 (FVKILRYENEVLQLEEDEDF) is a thoughtfully designed peptide derived from the cell adhesion domain of the sodium channel β1 subunit. By inhibiting β1-mediated junctional adhesion, it serves as a powerful tool to dissect mechanisms of electrical coupling in cardiomyocytes and holds promise as a molecular probe for exploring arrhythmia-targeted therapies. |
Scientific Background | Ac-FVKILRYENEVLQLEEDEDF- NH2 is a 24-residue synthetic peptide with the sequence Ala-Cys-Phe-Val-Lys-Ile-Leu-Arg-Tyr-Glu-Asn-Glu-Val-Leu-Gln-Leu-Glu-Glu-Asp-Glu-Asp-Phe-Asn-His. N-terminal acetylation neutralizes the terminal alpha-amino group; C-terminal amidation removes the terminal carboxylate charge. The sequence contains 1 cysteine residue, which can support thiol-selective conjugation or disulfide chemistry when the thiol group is available; contains multiple acidic residues (2 Asp and 5 Glu), contributing negative charge at neutral pH; contains 3 aromatic residues (Phe/Trp/Tyr), which can contribute to hydrophobic or aromatic interactions. No specific receptor, enzyme, pathway, disease association, or biological activity is assigned to this peptide without product-specific experimental evidence. |
Research Applications | - thiol-selective conjugation or immobilization studies
- LC-MS/HPLC analytical method development
- sequence-specific assay controls
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Experimental Notes | Sequence-derived chemical properties are provided to support reagent selection and experimental planning. They do not establish a biological function. Solubility, aggregation, adsorption, conjugation efficiency, and assay performance should be validated under the intended experimental conditions. |