Tyrosylglutaminyl-alpha-glutamylalanylphenylalanylarginylarginylphenylalanylphenylalanylglycylprolylvaline forms a peptide dominated by aromatic and basic motifs that promote structured folding. The sequence provides a model for studying hydrophobic stacking, charge distribution, and binding equilibria. Researchers examine its conformational transitions and stability. Applications include peptide engineering, motif analysis, and biophysical characterization.
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CAT No: R2645
CAS No:129356-77-0
Synonyms/Alias:Tyrosylglutaminyl-alpha-glutamylalanylphenylalanylarginylarginylphenylalanylphenylalanylglycylprolylvaline;129356-77-0;Tyrosylglutaminyl-alpha-glutamylalanylphenylalanylarginylarginylphenylalanylphenylalanylglycylprolylvaline;(Tyr38,Phe42.46)-Osteocalcin (38-49) (human);DTXSID60583182;DA-69298;FT110387;H-Tyr-Gln-Glu-Ala-Phe-Arg-Arg-Phe-Phe-Gly-Pro-Val-OH; H-YQEAFRRFFGPV-OH;
Tyrosylglutaminyl-alpha-glutamylalanylphenylalanylarginylarginylphenylalanylphenylalanylglycylprolylvaline is a synthetic peptide composed of a distinctive sequence of amino acids, designed to offer unique structural and functional properties for advanced research applications. Its complex arrangement incorporates both hydrophilic and hydrophobic residues, which allows it to interact with a diverse range of biomolecules and cellular components. The presence of multiple aromatic and basic side chains endows the peptide with versatile binding capabilities, making it a valuable tool for probing protein-protein interactions, molecular recognition, and signal transduction pathways. The robust design of Tyrosylglutaminyl-alpha-glutamylalanylphenylalanylarginylarginylphenylalanylphenylalanylglycylprolylvaline ensures stability under various experimental conditions, supporting its integration into a wide array of biochemical and biophysical protocols.
Peptide-Protein Interaction Studies: Tyrosylglutaminyl-alpha-glutamylalanylphenylalanylarginylarginylphenylalanylphenylalanylglycylprolylvaline is frequently utilized in studies aiming to elucidate the mechanisms of peptide-mediated protein recognition. Its sequence allows for the exploration of binding affinities and specificities with target proteins, facilitating the mapping of interaction domains and the identification of critical contact residues. By leveraging its distinctive side chains, researchers can dissect the contributions of hydrophobic, aromatic, and charged interactions in complex formation, advancing the understanding of molecular recognition in biological systems.
Enzyme Substrate Characterization: The peptide serves as a model substrate in enzymology research, particularly for proteases and peptidases that recognize specific amino acid motifs. By monitoring the cleavage patterns and kinetics of Tyrosylglutaminyl-alpha-glutamylalanylphenylalanylarginylarginylphenylalanylphenylalanylglycylprolylvaline, investigators can assess enzyme specificity, catalytic efficiency, and inhibitor potency. Such studies are instrumental in the development of novel enzyme inhibitors and the refinement of biochemical assays for high-throughput screening.
Cellular Signaling Pathway Analysis: Tyrosylglutaminyl-alpha-glutamylalanylphenylalanylarginylarginylphenylalanylphenylalanylglycylprolylvaline is incorporated into cellular assays to investigate its potential modulatory effects on signal transduction cascades. Its structure enables it to mimic or disrupt natural peptide ligands, providing a means to probe receptor activation, downstream effector engagement, and feedback regulation. Through such applications, researchers can delineate the roles of specific peptide motifs in cellular communication and regulatory networks.
Structural Biology and Conformational Studies: The defined sequence of Tyrosylglutaminyl-alpha-glutamylalanylphenylalanylarginylarginylphenylalanylphenylalanylglycylprolylvaline makes it an ideal candidate for structural investigations using techniques such as nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography. These studies offer insights into peptide folding, secondary structural elements, and dynamic conformational changes in response to environmental cues or binding partners. Understanding these structural properties contributes to rational design strategies for therapeutic and diagnostic peptides.
Biomaterial and Nanotechnology Research: In the field of biomaterials, Tyrosylglutaminyl-alpha-glutamylalanylphenylalanylarginylarginylphenylalanylphenylalanylglycylprolylvaline is explored for its ability to self-assemble or integrate into larger supramolecular constructs. Its amphiphilic nature and sequence-specific interactions support the creation of peptide-based hydrogels, coatings, and nanostructures with tailored mechanical and functional properties. These materials are subsequently employed in biosensing, drug delivery, and tissue engineering initiatives, highlighting the peptide's versatility beyond traditional biochemical applications.
Peptide-based Molecular Probes: Tyrosylglutaminyl-alpha-glutamylalanylphenylalanylarginylarginylphenylalanylphenylalanylglycylprolylvaline is also adapted for use as a molecular probe in various analytical platforms. By labeling it with fluorescent or affinity tags, scientists can track its distribution, monitor binding events, and quantify molecular interactions in complex biological samples. This application supports the development of sensitive detection assays and the validation of novel targets in proteomics and cell biology research, further establishing the peptide as an indispensable tool in contemporary scientific exploration.
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