AcFWKYCV contains aromatic and hydrophobic residues flanked by cysteines capable of forming stabilizing disulfide bridges. The acetylated N-terminus modulates charge and folding behavior. Researchers analyze its structural transitions and binding interactions. Applications include peptide engineering, motif analysis, and structural-biophysics research.
CAT No: R2546
CAS No:342878-90-4
Synonyms/Alias:342878-90-4;ACFWKYCV;2-[[10-(4-aminobutyl)-19-(2-aminopropanoylamino)-16-benzyl-7-[(4-hydroxyphenyl)methyl]-13-(1H-indol-3-ylmethyl)-6,9,12,15,18-pentaoxo-1,2-dithia-5,8,11,14,17-pentazacycloicosane-4-carbonyl]amino]-3-methylbutanoic acid;Urotensin II-Related Peptide (human, mouse, rat) trifluoroacetate salt;PUT-4408-V;DA-58914;FU109712;Urotensin II-Related Peptide (Human, Rat);H-Ala-Cys-Phe-Trp-Lys-Tyr-Cys-Val-OH; H-ACFWKYCV-OH;Ala-Cys-Phe-Trp-Lys-Tyr-Cys-Val, Urotensin II-Related Peptide;(S)-2-((Z)-(((4R,5Z,7S,8Z,10S,11Z,13S,14Z,16S,17Z,19R)-13-((1H-indol-3-yl)methyl)-19-((Z)-((S)-2-amino-1-hydroxypropylidene)amino)-10-(4-aminobutyl)-16-benzyl-6,9,12,15,18-pentahydroxy-7-(4-hydroxybenzyl)-1,2-dithia-5,8,11,14,17-pentaazacycloicosa-5,;
Acfwkycv is a synthetic peptide compound characterized by its unique amino acid sequence and structural properties, making it a valuable tool in peptide research and biochemical investigations. As a member of the peptide family, it offers a defined framework for exploring sequence-specific interactions, structure-function relationships, and molecular recognition processes within biological systems. Its synthetic origin allows for precise control over composition and purity, supporting a broad range of experimental designs in both fundamental and applied research contexts. The sequence and conformational attributes of this peptide provide opportunities to model, probe, or modulate various biological pathways and molecular assemblies, reinforcing its relevance in contemporary biochemical studies.
Peptide structure-function analysis: Acfwkycv serves as an effective model for investigating the relationship between primary amino acid sequence and resultant three-dimensional conformation. Researchers utilize this peptide to examine how specific residue arrangements influence folding, stability, and intermolecular interactions, thereby gaining insights into the principles governing protein structure. These studies are instrumental in advancing the understanding of protein engineering, rational design, and the development of novel biomimetic materials.
Molecular interaction studies: The defined sequence of this peptide enables precise exploration of binding affinities and specificity with target proteins, enzymes, or receptors. Its use in binding assays, surface plasmon resonance, or fluorescence-based detection platforms facilitates the elucidation of key contact points and interaction domains. Such investigations help clarify mechanisms of molecular recognition and inform the design of peptide-based inhibitors, probes, or affinity reagents for biochemical and biotechnological applications.
Peptide synthesis optimization: Acfwkycv is frequently employed as a reference or test substrate in the development and validation of solid-phase peptide synthesis protocols. Its sequence complexity and physicochemical characteristics provide a robust benchmark for assessing coupling efficiency, deprotection strategies, and purification techniques. Optimization studies using this peptide contribute to improved yield, fidelity, and scalability in peptide manufacturing processes, directly benefiting research and industrial peptide production workflows.
Functional screening assays: In functional genomics and proteomics research, this peptide is utilized within high-throughput screening platforms to evaluate bioactivity, post-translational modifications, or enzyme-substrate specificity. Its application in such assays supports the identification of novel biological targets, elucidation of catalytic mechanisms, and mapping of functional domains within complex biological samples. These insights are critical for advancing fundamental knowledge and enabling the rational development of new biochemical tools.
Biophysical characterization: The well-defined nature of Acfwkycv makes it an ideal candidate for biophysical studies, including circular dichroism spectroscopy, nuclear magnetic resonance, and mass spectrometry. Through these analytical techniques, researchers can assess secondary structure content, conformational dynamics, and stability under diverse experimental conditions. Such characterization provides foundational data for understanding peptide behavior in solution, informing the design of advanced biomaterials, and supporting the development of analytical standards for peptide research.
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