H-Pyr-His-Trp-Ser-D-Tyr-D-Trp-Leu-Arg-Pro-NHEt.TFA

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.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
H-Pyr-His-Trp-Ser-D-Tyr-D-Trp-Leu-Arg-Pro-NHEt.TFA(CAS 1426173-46-7)

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;

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cGMP Peptide
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  • IND and NDA support
  • Drug master files (DMF) filing
M.F/Formula
C66H84F3N17O14
M.W/Mr.
1396.5
Sequence
One Letter Code:XHWSYWLRP
Three Letter Code:H-Pyr-His-Trp-Ser-D-Tyr-D-Trp-Leu-Arg-Pro-NHEt.TFA

H-Pyr-His-Trp-Ser-D-Tyr-D-Trp-Leu-Arg-Pro-NHEt.TFA is a synthetic peptide comprising both L- and D-amino acids, engineered for advanced research applications in peptide science and molecular biology. Its unique sequence, which incorporates noncanonical D-residues alongside canonical L-amino acids, offers valuable structural diversity and resistance to enzymatic degradation. The presence of a C-terminal ethylamide modification and trifluoroacetate salt form further enhances its solubility and stability, making it a versatile tool for probing structure-function relationships and receptor interactions in biochemical research. As a research-use-only compound, it enables precise studies into peptide signaling, receptor binding, and structure-based drug design.

Peptide receptor binding studies: Due to its defined amino acid sequence and structural modifications, this peptide serves as a model ligand for investigating interactions with G protein-coupled receptors (GPCRs) and other peptide-binding proteins. Researchers can use it to map binding sites, assess affinity and selectivity, and elucidate conformational requirements for receptor activation or inhibition. Its inclusion of D-amino acids can provide insights into how chirality affects receptor recognition, potentially informing the design of more selective or stable ligands.

Structure-activity relationship (SAR) analysis: The alternating sequence of L- and D-amino acids, combined with the C-terminal ethylamide group, makes this peptide a valuable template for SAR studies. By systematically modifying individual residues or terminal groups, scientists can determine which structural features are critical for biological activity or stability. Such research supports the rational design of next-generation analogs with improved pharmacokinetic or pharmacodynamic properties for laboratory investigations.

Enzymatic stability and metabolic profiling: Synthetic peptides containing D-amino acids are frequently employed to investigate the impact of stereochemistry on proteolytic resistance. This compound's configuration enables researchers to assess its degradation profile in the presence of various proteases, thereby providing data on metabolic stability. These insights are essential for developing peptide-based probes or modulators with enhanced in vivo half-life for research purposes.

Peptide synthesis and methodology development: The complex sequence and post-synthetic modifications present in this peptide make it an ideal standard for evaluating and optimizing solid-phase peptide synthesis (SPPS) protocols. It can be used to benchmark coupling efficiency, assess racemization, and validate purification strategies. Such methodological studies are critical for advancing peptide chemistry and ensuring reproducibility in the synthesis of complex bioactive peptides.

Biophysical and structural studies: The unique sequence and modifications of this peptide allow it to serve as a model system for analyzing secondary structure formation, aggregation behavior, and peptide-membrane interactions. Techniques such as circular dichroism, NMR spectroscopy, or fluorescence assays can be employed to characterize its conformational properties in solution or in the presence of lipid bilayers. These investigations contribute to a deeper understanding of peptide folding, stability, and function in biomimetic environments.

InChI
InChI=1S/C64H83N17O12.C2HF3O2/c1-4-68-62(92)53-16-10-24-81(53)63(93)46(15-9-23-69-64(65)66)74-56(86)47(25-35(2)3)75-58(88)49(27-37-30-70-43-13-7-5-11-41(37)43)77-57(87)48(26-36-17-19-40(83)20-18-36)76-61(91)52(33-82)80-59(89)50(28-38-31-71-44-14-8-6-12-42(38)44)78-60(90)51(29-39-32-67-34-72-39)79-55(85)45-21-22-54(84)73-45;3-2(4,5)1(6)7/h5-8,11-14,17-20,30-32,34-35,45-53,70-71,82-83H,4,9-10,15-16,21-29,33H2,1-3H3,(H,67,72)(H,68,92)(H,73,84)(H,74,86)(H,75,88)(H,76,91)(H,77,87)(H,78,90)(H,79,85)(H,80,89)(H4,65,66,69);(H,6,7)/t45-,46-,47-,48+,49+,50-,51-,52-,53-;/m0./s1
InChI Key
MQSBDALSNXYZTH-WUTRMYCASA-N

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