H-Asp-Arg-Gly-Val-Tyr-Ile-His-Pro-Phe-OH arranges acidic, basic, aromatic, and hydrophobic residues to create a versatile model for folding studies. The peptide supports examination of hydrogen bonding, charge distribution, and side-chain packing. Researchers assess its binding properties across varied environments. Applications include motif exploration, biophysical studies, and synthetic peptide design.
CAT No: R2440
CAS No:812644-79-4
Synonyms/Alias:TRV056;812644-79-4;HY-P3137;AKOS040758362;DA-68379;CS-0148149;G18155;
H-Asp-Arg-Gly-Val-Tyr-Ile-His-Pro-Phe-OH is a synthetic nonapeptide composed of a specific sequence of nine amino acids, designed to facilitate advanced studies in peptide biochemistry and molecular biology. As a structured linear peptide, it serves as a valuable tool for investigating sequence-dependent biochemical interactions, receptor binding dynamics, and structure-activity relationships. Its defined composition enables researchers to explore peptide-mediated mechanisms, making it particularly significant for elucidating the roles of short peptide motifs in cellular signaling, protein-protein interactions, and enzymatic recognition.
Peptide structure-function analysis: The nonapeptide's precise amino acid sequence enables detailed examination of how specific residue arrangements influence biological activity, folding, and molecular recognition. By incorporating this peptide into experimental models, researchers can dissect the contributions of individual side chains and sequence patterns to binding affinity, conformational stability, and interaction specificity. Such studies are fundamental for understanding the molecular basis of peptide function in both natural and engineered contexts.
Receptor binding and ligand screening: Due to its tailored sequence, this nonapeptide is frequently employed in receptor-ligand binding assays aimed at identifying and characterizing peptide-responsive receptors. Its use in competitive binding studies or affinity profiling helps delineate the selectivity and kinetics of peptide-receptor interactions. These insights are crucial for mapping signaling pathways, validating molecular targets, and informing the design of novel bioactive peptides with improved receptor specificity.
Peptide synthesis and modification research: The nonapeptide serves as an exemplary substrate for method development in solid-phase peptide synthesis and post-synthetic modification protocols. Researchers utilize it to optimize coupling strategies, assess side-chain protection schemes, and evaluate the efficiency of peptide cyclization or labeling reactions. Its defined sequence and manageable length make it an ideal candidate for benchmarking synthetic yields and exploring new chemistries in peptide engineering.
Protease substrate studies: As a well-characterized peptide, it is often used as a substrate in enzymatic assays to investigate the specificity and kinetics of proteolytic enzymes. By monitoring the cleavage patterns and reaction rates, scientists gain valuable data on protease selectivity, active site preferences, and inhibitor screening. Such applications are vital for understanding proteolytic processing in physiological and pathological contexts, as well as for developing protease-targeted research tools.
Analytical method calibration: The nonapeptide's defined composition and purity make it suitable for use as a standard or calibration reference in mass spectrometry, high-performance liquid chromatography (HPLC), and related analytical techniques. Employing it in these contexts allows for the validation of instrument performance, quantification protocols, and peptide identification workflows. Accurate calibration with such peptides underpins reliable analytical results in peptide research, quality control, and biomarker discovery applications.
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