Ala-lys-arg-his-his-gly-tyr-lys-arg-lys-phe-his-NH2 is a histidine-rich peptide with extensive charged and aromatic content enabling diverse structural states. Researchers apply it to analyze metal-binding behavior, hydrogen-bond patterns, and conformational adaptability. The C-terminal amide stabilizes the peptide backbone.
CAT No: R2289
CAS No:190673-58-6
Synonyms/Alias:Ala-lys-arg-his-his-gly-tyr-lys-arg-lys-phe-his-NH2;190673-58-6;Ala-lys-arg-his-his-gly-tyr-lys-arg-lys-phe-his-NH2;P-113;B6WQB8NCPA;UNII-B6WQB8NCPA;L-Histidinamide, L-alanyl-L-lysyl-L-arginyl-L-histidyl-L-histidylglycyl-L-tyrosyl-L-lysyl-L-arginyl-L-lysyl-L-phenylalanyl-;DA-76535;E80525;Q27274445;C-AKRHHGYKRKFH-NH2
Ala-lys-arg-his-his-gly-tyr-lys-arg-lys-phe-his-NH2 is a synthetic peptide sequence that has garnered attention in biochemical and molecular research due to its unique arrangement of amino acids and functional groups. The presence of multiple basic residues, aromatic side chains, and a terminal amide group imparts distinctive physicochemical properties, making it a versatile tool for a variety of experimental applications. Researchers value this peptide for its solubility, stability under physiological conditions, and its ability to interact with a range of biological molecules. Its sequence, rich in lysine, arginine, and histidine, suggests potential roles in mimicking or modulating protein-protein and protein-nucleic acid interactions, facilitating studies that require precise molecular recognition and binding. The inclusion of glycine and phenylalanine further enhances its flexibility and interaction profile, broadening its utility in both structural and functional assays.
Protein-Protein Interaction Studies: Ala-lys-arg-his-his-gly-tyr-lys-arg-lys-phe-his-NH2 serves as a valuable probe in the investigation of protein-protein interactions, particularly those involving basic and aromatic amino acid motifs. By incorporating this peptide into binding assays, researchers can dissect the contributions of specific residue clusters to the affinity and specificity of macromolecular complexes. Its sequence enables the modeling of interaction hotspots commonly found in regulatory proteins, thereby providing insights into the mechanisms that govern signal transduction, enzyme regulation, or scaffold assembly. The peptide's ability to compete with or disrupt native interactions is instrumental in uncovering new therapeutic targets or elucidating the structural basis of disease-associated mutations.
Enzyme Substrate or Inhibitor Design: The unique arrangement of amino acids in this peptide makes it an excellent candidate for use as a substrate or competitive inhibitor in enzymatic studies. Enzymologists can utilize the peptide to probe the substrate specificity of proteases, kinases, or other modifying enzymes that recognize basic or aromatic residues. By monitoring cleavage, modification, or binding events, it becomes possible to characterize enzyme kinetics, map active sites, and screen for potential modulators. This approach is particularly useful in drug discovery, where understanding enzyme selectivity and activity is crucial for the development of small molecule inhibitors or peptide-based therapeutics.
Cellular Uptake and Trafficking Research: Due to its abundance of basic residues, particularly lysine and arginine, the peptide is well-suited for studies on cellular uptake mechanisms, such as endocytosis or membrane translocation. Scientists employ this sequence to mimic cell-penetrating peptides, evaluating how charge distribution and sequence context influence internalization efficiency. Fluorescently labeled versions can be tracked in live cells to monitor subcellular localization, trafficking pathways, and the dynamics of intracellular delivery. Such studies are essential for the rational design of drug delivery systems, gene therapy vectors, or molecular imaging agents.
Biophysical and Structural Analysis: The peptide's defined sequence and chemical properties make it an ideal model system for biophysical studies, including circular dichroism, NMR spectroscopy, and crystallography. Researchers exploit its capacity to adopt specific secondary structures or to interact with nucleic acids, lipids, or metal ions under controlled conditions. These experiments yield valuable data on folding dynamics, conformational stability, and intermolecular forces, contributing to a deeper understanding of peptide and protein chemistry. Insights gained from these studies inform the design of novel biomaterials, biosensors, or molecular scaffolds.
Epitope Mapping and Antibody Production: As a synthetic antigen, Ala-lys-arg-his-his-gly-tyr-lys-arg-lys-phe-his-NH2 is frequently used in immunological research to map epitopes or generate sequence-specific antibodies. Its well-defined structure allows for precise identification of antibody binding sites, facilitating the development of highly specific detection reagents for use in ELISA, Western blotting, or immunoprecipitation. By conjugating the peptide to carrier proteins or surfaces, immunologists can elicit robust immune responses, enabling the isolation and characterization of monoclonal or polyclonal antibodies. These tools are indispensable for probing protein expression, localization, and function in complex biological samples, advancing both basic and applied research in the life sciences.
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