Pyroglutamyl-glutamyl-proline amide

Pyroglutamyl-glutamyl-proline amide integrates a pyroglutamate cap with acidic and cyclic residues that influence backbone curvature. The peptide serves as a stable motif for hydrogen-bond and ring-conformation studies. Researchers analyze its behavior in enzymatic recognition and solvent interactions. Applications include structural modeling, peptide processing studies, and motif-function evaluation.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
Pyroglutamyl-glutamyl-proline amide(CAS 85541-78-2)

CAT No: R2506

CAS No:85541-78-2

Synonyms/Alias:85541-78-2;(Glu2)-TRH;pyroglutamyl-glutamyl-proline amide;Pglu-glu-pro-amide;pGlu-Glu-Pro-NH2;PYR-GLU-PRO-NH2;[Glu2]-TRH;NMJ3YG49SE;(4S)-5-[(2S)-2-carbamoylpyrrolidin-1-yl]-5-oxo-4-[[(2S)-5-oxopyrrolidine-2-carbonyl]amino]pentanoic acid;Pglu-glu-pronh2;Glp-glu-pronh2;Pyroglutamyl-glutamyl-prolineamide;PyroGLU-GLU-PRO AMIDE;Fertilization promoting peptide;Pyroglutamyl-glutamyl-prolinamide;(Glu2)-TRH Pyr-Glu-Pro-NH2;MFCD00076815;pGlu-Glu-Pro Amide;GLP-GLU-PRO-NH2;UNII-NMJ3YG49SE;pyroglutamylglutamylprolineamide;SCHEMBL1373186;CHEMBL3895280;CHEBI:183942;DTXSID501006105;HY-P3960;DA-69328;FG108676;CS-0634436;L-Prolinamide, 5-oxo-L-prolyl-L-alpha-glutamyl-;L-PROLINAMIDE, 5-OXO-L-PROLYL-L-.ALPHA.-GLUTAMYL-;(S)-5-((S)-2-carbamoylpyrrolidin-1-yl)-5-oxo-4-((S)-5-oxopyrrolidine-2-carboxamido)pentanoic acid;4-{[Hydroxy(5-hydroxy-3,4-dihydro-2H-pyrrol-2-yl)methylidene]amino}-5-{2-[hydroxy(imino)methyl]pyrrolidin-1-yl}-5-oxopentanoic acid;

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M.F/Formula
C15H22N4O6
M.W/Mr.
354.36
Sequence
One Letter Code:XEP
Three Letter Code:H-Pyr-Glu-Pro-NH2

Pyroglutamyl-glutamyl-proline amide is a synthetic tripeptide compound that has garnered significant attention in biochemical research due to its unique structural configuration and potential biological activities. As a member of the pyroglutamyl peptide family, this molecule is characterized by the presence of a pyroglutamyl residue at the N-terminus, which imparts increased metabolic stability and resistance to enzymatic degradation. The sequence further incorporates glutamyl and proline residues, both of which are known to contribute to diverse physiological processes and molecular interactions. Because of these features, Pyroglutamyl-glutamyl-proline amide serves as a valuable tool in a variety of experimental and research settings, enabling scientists to probe peptide function, receptor interactions, and cellular signaling pathways. Its amide-capped C-terminus further enhances its utility by minimizing susceptibility to exopeptidase activity, making it a robust candidate for studies that require prolonged peptide activity or stability in biological systems.

Peptide Structure-Activity Relationship Studies: Pyroglutamyl-glutamyl-proline amide is frequently utilized in investigations aimed at elucidating the relationship between peptide structure and biological function. Researchers employ this tripeptide to systematically analyze how modifications in amino acid sequence, terminal capping, or backbone configuration influence binding affinity, receptor selectivity, and downstream signaling. By incorporating the pyroglutamyl moiety, scientists can assess the impact of N-terminal cyclization on peptide stability and bioactivity, facilitating the rational design of novel peptide analogs for basic science and therapeutic research.

Enzyme Substrate Profiling: The tripeptide is often adopted as a substrate or probe in enzymology studies, particularly those focused on peptidases and proteases that recognize or process pyroglutamyl-containing peptides. By monitoring the cleavage or resistance of Pyroglutamyl-glutamyl-proline amide in the presence of specific enzymes, researchers can characterize substrate specificity, elucidate enzyme mechanisms, and screen for potential inhibitors. This application is especially valuable in the context of understanding post-translational modification pathways and the regulation of peptide-mediated signaling events.

Receptor Binding and Signal Transduction Research: In the field of molecular pharmacology, the compound is deployed in assays designed to investigate peptide-receptor interactions and the subsequent activation of intracellular signaling cascades. Its defined sequence and enhanced stability make it suitable for use in competitive binding assays, receptor profiling studies, and the mapping of ligand recognition motifs. Through such experiments, scientists gain insights into the determinants of receptor selectivity and the structural requirements for agonist or antagonist activity, advancing knowledge of peptide-mediated communication in physiological and pathological contexts.

Cellular Uptake and Transport Studies: Pyroglutamyl-glutamyl-proline amide provides a model system for examining the mechanisms of peptide uptake, transport, and intracellular distribution. By labeling the tripeptide with fluorescent or isotopic tags, researchers can track its movement across cellular membranes, evaluate the role of specific transporters, and quantify intracellular accumulation. These studies are critical for understanding how peptide drugs and signaling molecules are internalized and trafficked within cells, informing strategies for targeted delivery and improved bioavailability.

Analytical Method Development: The unique chemical properties of Pyroglutamyl-glutamyl-proline amide make it a practical standard or reference compound in the development and validation of analytical methods for peptide quantification and characterization. Techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and capillary electrophoresis benefit from the compound's defined sequence and stability, which allow for the calibration of instruments, optimization of separation protocols, and assessment of detection limits. This application supports efforts to advance peptide analytics in both research and industrial laboratories.

In summary, Pyroglutamyl-glutamyl-proline amide stands out as a versatile tripeptide tool for probing structure-activity relationships, profiling enzyme specificity, dissecting receptor-ligand interactions, studying peptide transport mechanisms, and supporting analytical method development. Its robust chemical configuration, resistance to degradation, and compatibility with diverse experimental systems enable researchers to address fundamental questions in peptide chemistry, molecular biology, and biochemistry, thereby contributing to the advancement of scientific discovery across multiple disciplines.

InChI
InChI=1S/C15H22N4O6/c16-13(23)10-2-1-7-19(10)15(25)9(4-6-12(21)22)18-14(24)8-3-5-11(20)17-8/h8-10H,1-7H2,(H2,16,23)(H,17,20)(H,18,24)(H,21,22)/t8-,9-,10-/m0/s1
InChI Key
HYZBGWLLSXSYLX-GUBZILKMSA-N

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