Oxytocin, Glu(4)- introduces a targeted residue substitution that alters charge distribution and intramolecular packing within the cyclic peptide. Researchers explore the impact on ring conformation and binding characteristics. Structural behavior varies predictably across solvent conditions. Uses include motif-function research, cyclic-peptide engineering, and biophysical analysis.
CAT No: R2352
CAS No:4314-67-4
Synonyms/Alias:Oxytocin, glu(4)-;4-Glu-oxytocin;4314-67-4;Oxytocin, glutamic acid(4)-;Oxytocin, 4-L-glutamicacid- (8CI,9CI);Oxytocin, 4-L-glutamic acid-;3-[(4R,7S,10S,16S,19R)-19-amino-7-(2-amino-2-oxoethyl)-4-[(2S)-2-[[(2S)-1-[(2-amino-2-oxoethyl)amino]-4-methyl-1-oxopentan-2-yl]carbamoyl]pyrrolidine-1-carbonyl]-13-[(2S)-butan-2-yl]-16-[(4-hydroxyphenyl)methyl]-6,9,12,15,18-pentaoxo-1,2-dithia-5,8,11,14,17-pentazacycloicos-10-yl]propanoic acid;SCHEMBL15512041;
Oxytocin, Glu(4)- is a synthetic peptide analog of the naturally occurring neuropeptide oxytocin, distinguished by the substitution of glutamic acid at the fourth position in its amino acid sequence. As a modified peptide, it retains the core cyclic nonapeptide structure typical of oxytocin but introduces a targeted alteration that can influence its receptor interactions, stability, and biological activity. This analog is of significant interest in biochemical research due to its potential to elucidate the structure-activity relationships governing peptide hormone function, receptor specificity, and signal transduction mechanisms. Its precise modification provides a valuable tool for dissecting the molecular determinants of oxytocin's physiological and pharmacological roles in mammalian systems.
Peptide structure-activity relationship studies: The Glu(4)-modified oxytocin analog is extensively utilized in investigations aimed at understanding how specific amino acid substitutions affect peptide conformation and biological activity. By incorporating glutamic acid at the fourth residue, researchers can assess the impact of this change on peptide folding, receptor binding affinity, and downstream signaling. Such studies are essential for mapping the critical residues that govern oxytocin's interaction with its G protein-coupled receptor and for identifying determinants of agonist or antagonist behavior.
Receptor selectivity profiling: In receptor pharmacology, this modified peptide serves as a selective probe for distinguishing the binding characteristics of oxytocin and vasopressin receptor subtypes. The introduction of a negatively charged glutamate side chain at position four enables detailed analysis of how side-chain properties influence receptor subtype selectivity and ligand-receptor dynamics. These insights are valuable for the rational design of peptide ligands with tailored specificity for therapeutic or investigative purposes.
Peptide stability and degradation studies: The Glu(4)-substituted analog provides a model system for examining how sequence modifications affect peptide stability, susceptibility to enzymatic degradation, and metabolic fate. By comparing its stability profile to that of native oxytocin, researchers can identify structural features that confer resistance or sensitivity to peptidases, informing strategies for enhancing peptide half-life in experimental settings.
Analytical method development: The unique physicochemical properties of this analog, such as altered charge and hydrophobicity, make it a suitable standard or reference compound for optimizing analytical techniques. It is frequently employed in the calibration and validation of high-performance liquid chromatography (HPLC), mass spectrometry, and capillary electrophoresis methods used for peptide quantification, purity assessment, and structural characterization. Its defined sequence modification aids in distinguishing it from endogenous peptides during complex sample analysis.
Peptide-protein interaction studies: The Glu(4) variant of oxytocin is also valuable in probing the molecular determinants of peptide-protein interactions beyond receptor binding. By introducing a specific charge and side-chain geometry at a key position, the analog can be used to investigate how such modifications influence binding to carrier proteins, cell surface molecules, or peptide transporters. These studies contribute to a broader understanding of peptide trafficking, bioavailability, and cellular uptake mechanisms relevant to neuropeptide biology and peptide drug development.
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