H-Tyr-D-Ala-Gly-Phe-Leu-Arg-OH·CH3CO2H is an opioid-related hexapeptide incorporating aromatic and charged residues that influence backbone folding. The D-Ala substitution modulates stereochemical behavior and enzymatic susceptibility. Researchers use it to explore residue-dependent interactions, hydrogen bonding, and solvation effects. Its acetate form enhances handling and solubility.
H-Tyr-D-Ala-Gly-Phe-Leu-Arg-OH.CH3CO2H is a synthetic peptide compound composed of a specific sequence of amino acids, including tyrosine, D-alanine, glycine, phenylalanine, leucine, and arginine, with an acetyl counterion. As a research-grade peptide, it is valued for its defined structure and the incorporation of a D-amino acid residue, which can impart unique conformational and functional properties. Such peptides play a crucial role in advancing our understanding of peptide structure-activity relationships, receptor interactions, and the development of peptide-based biochemical tools. The presence of both L- and D-amino acids in the sequence makes this molecule particularly relevant for studies exploring stereochemistry-dependent biological phenomena and peptide stability.
Peptide receptor binding studies: Due to its precise amino acid composition and the inclusion of a D-amino acid, this peptide is frequently utilized in investigations of peptide-receptor interactions. Researchers employ it to probe binding affinities, elucidate selectivity profiles, and characterize the molecular determinants of ligand recognition in various receptor systems. The D-Ala residue can confer resistance to enzymatic degradation, enabling extended observation windows in binding assays and facilitating the study of receptor-ligand dynamics under physiologically relevant conditions.
Enzyme substrate specificity assays: The defined sequence and stereochemistry of this peptide make it an informative substrate in enzymology research. By assessing its susceptibility to proteolytic enzymes such as endopeptidases or exopeptidases, scientists can gain insights into enzyme specificity, catalytic mechanisms, and the influence of D-amino acid incorporation on peptide processing. Such studies are essential for mapping protease recognition motifs and for the rational design of enzyme-resistant peptide analogs.
Peptide structure-activity relationship (SAR) analysis: The unique sequence and stereochemical features of this peptide render it an excellent model for SAR investigations. Researchers can systematically modify individual residues or compare analogs to delineate how specific side chains and backbone configurations contribute to biological activity, stability, or receptor selectivity. These insights are fundamental for the optimization of peptide ligands in both basic research and the development of functional peptide probes.
Peptide synthesis and analytical method development: This compound serves as a reliable reference or standard in the optimization of solid-phase peptide synthesis protocols and the validation of analytical techniques such as high-performance liquid chromatography (HPLC) and mass spectrometry. Its well-characterized structure allows for the calibration of instrumentation, assessment of synthetic yields, and evaluation of peptide purity, supporting both routine quality control and advanced method development in peptide chemistry laboratories.
Biochemical assay development: The sequence and physicochemical properties of this peptide make it suitable for use as a model substrate, control, or probe in a range of biochemical assays. Whether employed to validate assay sensitivity, benchmark detection limits, or investigate peptide-protein interactions, it provides a consistent and reproducible tool for assay optimization and standardization, contributing to the reliability and comparability of experimental results across different research settings.
1. Implications of ligand-receptor binding kinetics on GLP-1R signalling
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