H-Asp-Tyr-Lys-(Asp)₄-Lys repeated motifs create a highly acidic peptide interspersed with basic residues, forming a polyelectrolyte-like structure. The sequence enables studies of charge distribution, electrostatic complex formation, and phosphorylation mimicry. Researchers evaluate its conformational flexibility and ion-binding behavior. Applications include biophysical analysis, polymer-peptide modeling, and charge-driven assembly.
CAT No: R2380
CAS No:921765-76-6
Synonyms/Alias:H-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-OH;921765-76-6;3x DYKDDDDK Tag;
H-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-OH is a synthetic peptide composed of aspartic acid, tyrosine, and lysine residues arranged in a distinctive sequence. This polypeptide is characterized by its repetitive structure, which imparts unique physicochemical properties such as enhanced hydrophilicity and potential for multivalent interactions. Researchers value this peptide for its ability to mimic certain structural motifs found in native proteins, making it an intriguing candidate for studies involving protein-protein interactions, molecular recognition, and materials science. The presence of multiple aspartic acid residues confers a highly anionic character, which can facilitate binding to positively charged biomolecules or inorganic surfaces. Its modular architecture also allows for straightforward customization, making it a versatile tool in experimental design.
Protein Interaction Studies: H-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-OH is frequently employed in protein interaction studies due to its repetitive and charged sequence. The abundant aspartic acid and lysine residues enable the peptide to form electrostatic interactions with a variety of proteins, which is particularly useful in mapping binding sites or characterizing the specificity of protein-ligand associations. By incorporating this peptide into binding assays, researchers can elucidate mechanisms of affinity and selectivity, contributing to a deeper understanding of molecular recognition processes.
Biomaterials Development: The unique sequence of this peptide lends itself to applications in biomaterials development. Its high density of charged amino acids can promote adhesion to metal ions or inorganic substrates, making it suitable for use as a surface-modifying agent. In the context of tissue engineering or nanotechnology, the peptide can be integrated into hydrogels, scaffolds, or coatings to enhance biocompatibility or to introduce specific functionalities. Its modular nature allows for the design of hybrid materials that combine biological and synthetic elements, opening avenues for innovation in smart materials and biointerfaces.
Enzyme Substrate Engineering: Researchers utilize this synthetic peptide as a model substrate in enzyme assays, particularly for kinases, proteases, or other modifying enzymes that recognize specific amino acid motifs. The repetitive sequence and defined structure provide a reliable platform for monitoring enzymatic activity, enabling the optimization of assay conditions or the identification of novel enzyme inhibitors. By systematically varying the peptide sequence or incorporating labeled residues, scientists can dissect enzyme specificity and kinetics with high precision.
Analytical Method Development: In analytical chemistry and bioassay development, H-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-OH serves as a valuable standard or probe. Its well-defined composition and predictable behavior under various analytical conditions make it suitable for calibrating mass spectrometry, high-performance liquid chromatography (HPLC), or capillary electrophoresis systems. The peptide's robust signal response and stability facilitate the validation of analytical methods, ensuring reproducibility and accuracy in quantitative studies.
Cellular Uptake and Delivery Research: The structural features of this peptide, particularly its charged residues and potential for forming secondary structures, have prompted investigations into its role as a carrier in cellular uptake and delivery studies. By conjugating it to bioactive molecules or nanoparticles, researchers can assess mechanisms of cellular internalization, endosomal escape, or targeted delivery. These studies inform the design of more efficient delivery systems for research applications, leveraging the peptide's intrinsic properties to enhance cellular interaction and transport.
Peptide-based Sensor Development: H-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-OH has also found utility in the development of peptide-based sensors. Its sequence can be engineered to respond to specific analytes or environmental changes, such as pH shifts or the presence of metal ions. By immobilizing the peptide on sensor surfaces or integrating it into signal transduction systems, scientists can create sensitive and selective detection platforms for various research and diagnostic applications. The versatility and adaptability of this peptide make it a valuable asset in advancing sensor technology and broadening the scope of analytical tools available to the scientific community.
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4. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
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