H-Pyr-His-Trp-Ser-D-Tyr-D-Trp-Leu-Arg-Pro-NHEt·TFA carries pyroglutamate, D-residues, and an N-ethylamide terminus to tune stability and receptor interaction. Aromatic side chains contribute to π-stacking and spectroscopic signals. Researchers evaluate its conformational ensemble and proteolytic resistance. Applications include analog-optimization work, receptor-binding investigations, and neuropeptide-mimetic studies.
CAT No: R2584
CAS No:1426173-46-7
Synonyms/Alias:1426173-46-7;H-Pyr-His-Trp-Ser-D-Tyr-D-Trp-Leu-Arg-Pro-NHEt.TFA;FD109428;(Des-Gly10,D-Tyr5,D-Trp6,Pro-NHEt 9)-LHRH trifluoroacetate salt;Pyr-His-Trp-Ser-D-Tyr-D-Trp-Leu-Arg-Pro-NHEt; pE-HWS(dY)(dW)LRP-NHEt;
H-Pyr-His-Trp-Ser-D-Tyr-D-Trp-Leu-Arg-Pro-NHEt.TFA is a synthetic decapeptide featuring a unique sequence that incorporates both L- and D-amino acids, as well as a C-terminal ethylamide modification and a trifluoroacetate salt form. The structural design of this peptide offers enhanced resistance to enzymatic degradation, increased receptor specificity, and improved bioavailability in experimental systems. Researchers value its multifaceted biochemical properties, which make it a versatile tool in the study of peptide-receptor interactions, signaling pathways, and molecular recognition processes. Its precise amino acid arrangement enables targeted investigation of structure-activity relationships, facilitating the exploration of novel mechanisms in peptide-based research. The inclusion of non-standard amino acids and terminal modifications further expands its potential for innovative applications in various scientific fields, particularly those involving neuropeptide analogs and receptor modulation.
Peptide-receptor interaction studies: H-Pyr-His-Trp-Ser-D-Tyr-D-Trp-Leu-Arg-Pro-NHEt.TFA serves as a robust model for elucidating the binding dynamics between peptides and their cognate receptors. By utilizing this compound, researchers can dissect the contributions of specific amino acid residues to receptor affinity and selectivity. The presence of both D- and L-amino acids allows for the investigation of stereochemical effects on binding, while the ethylamide C-terminus can influence overall peptide conformation. These features make it an ideal candidate for mapping receptor binding sites and understanding the molecular determinants of ligand recognition in in vitro systems.
Signal transduction pathway analysis: The synthetic peptide's ability to mimic or modulate endogenous peptide ligands renders it valuable in deciphering intracellular signaling cascades. Scientists can employ it to activate or inhibit specific receptors in cultured cells, thereby delineating downstream signaling events such as second messenger production, phosphorylation patterns, or gene expression changes. Its stability in biological media ensures consistent experimental outcomes, enabling detailed kinetic and dose-response studies that shed light on the complexities of cellular communication networks.
Pharmacological screening and drug discovery: As a structurally optimized peptide analog, H-Pyr-His-Trp-Ser-D-Tyr-D-Trp-Leu-Arg-Pro-NHEt.TFA is frequently used in high-throughput screening platforms to identify novel modulators of peptide-responsive receptors. Its unique sequence provides a template for the rational design of next-generation compounds with improved efficacy or selectivity. By serving as a reference ligand, it aids in the assessment of structure-activity relationships and the identification of lead candidates for further development in preclinical research settings.
Enzyme substrate specificity assays: The inclusion of non-canonical amino acids in the peptide sequence makes it an informative substrate for profiling the activity of peptide-processing enzymes such as proteases and peptidases. Researchers can monitor the stability and cleavage patterns of the compound in the presence of various enzymes, thereby gaining insights into substrate recognition motifs and catalytic mechanisms. Such studies contribute to a deeper understanding of proteolytic regulation in physiological and pathophysiological contexts.
Molecular probe development: The stability and receptor-targeting characteristics of this decapeptide enable its use as a molecular probe in biochemical and biophysical assays. Scientists can conjugate it with fluorescent or affinity tags to visualize receptor localization, quantify binding kinetics, or isolate receptor complexes from cell lysates. These applications support the development of advanced tools for studying protein-protein interactions and receptor dynamics in living cells or tissue extracts, broadening the scope of peptide-based investigative methodologies.
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