N-Acetyloxytocin is an oxytocin derivative with an N-terminal acetyl group influencing polarity and hydrogen-bond accessibility. Researchers use it to study modified folding, receptor-contact surfaces, and conformational transitions. The peptide's structure supports high-resolution biophysical assays.
CAT No: R2297
CAS No:10551-48-1
Synonyms/Alias:N-Acetyloxytocin;10551-48-1;Oxytocin, N-acetyl-;N(alpha)-Acetyloxytocin;(2S)-1-[(4R,7S,10S,13S,16S,19R)-19-acetamido-7-(2-amino-2-oxoethyl)-10-(3-amino-3-oxopropyl)-13-[(2S)-butan-2-yl]-16-[(4-hydroxyphenyl)methyl]-6,9,12,15,18-pentaoxo-1,2-dithia-5,8,11,14,17-pentazacycloicosane-4-carbonyl]-N-[(2S)-1-[(2-amino-2-oxoethyl)amino]-4-methyl-1-oxopentan-2-yl]pyrrolidine-2-carboxamide;N-Acetyl Oxystin;SCHEMBL16790726;HY-P3219;CS-0169709;N-Acetyl Oxystin; Oxytocin Imp. E (EP): N-Acetyloxytocin; Oxytocin, N-acetyl- (8CI, 9CI, ACI); 1,2-Dithia-5,8,11,14,17-pentaazacycloeicosane, cyclic peptide deriv. (ZCI); Oxytocin, 1-(N-acetylcysteine) (7CI);
N-Acetyloxytocin is a chemically modified peptide derivative of oxytocin, distinguished by the acetylation of its N-terminal amino group. As a synthetic analog of the naturally occurring neuropeptide, it retains the characteristic nonapeptide backbone while exhibiting altered physicochemical properties due to the acetyl modification. This structural adjustment can influence its receptor binding affinity, metabolic stability, and overall bioactivity, making it a valuable tool for scientific investigations into peptide function, signaling pathways, and peptide-based drug design. Researchers utilize N-Acetyloxytocin to explore the nuanced roles of oxytocin analogs in diverse biochemical and physiological contexts, particularly where modifications to peptide structure are hypothesized to impact biological outcomes.
Peptide receptor binding studies: N-Acetyloxytocin is frequently employed in receptor binding assays to elucidate the structural determinants of ligand-receptor interactions within the oxytocin/vasopressin receptor family. By comparing the binding profiles of acetylated and non-acetylated forms, researchers can dissect the contribution of the N-terminal modification to receptor selectivity, affinity, and downstream signaling. These insights are crucial for advancing the understanding of peptide-receptor specificity and for guiding the rational design of novel peptide ligands with tailored pharmacological properties.
Peptide stability and metabolism research: The acetylation of the N-terminus in N-Acetyloxytocin confers increased resistance to certain proteolytic enzymes, making it a valuable model for studying peptide degradation pathways. Investigators use this analog to assess how structural modifications influence peptide half-life and susceptibility to enzymatic cleavage in various biological matrices. Such studies inform the development of more stable peptide therapeutics and enhance the understanding of metabolic processing in both in vitro and ex vivo systems.
Structure-activity relationship (SAR) analysis: As a modified peptide, N-Acetyloxytocin serves as a critical probe in SAR studies aimed at correlating specific chemical modifications with changes in biological activity. By systematically evaluating the functional consequences of N-terminal acetylation, scientists can map key determinants of agonist or antagonist activity, receptor subtype selectivity, and downstream signaling efficacy. These findings contribute to the broader field of peptide optimization for research and development purposes.
Peptide synthesis and analytical benchmarking: The compound is widely used as a reference standard and benchmarking tool in synthetic peptide chemistry. Its defined structure and unique modification make it an ideal candidate for validating synthetic methodologies, optimizing purification protocols, and calibrating analytical instrumentation such as HPLC and mass spectrometry. Laboratories engaged in peptide synthesis or quality control often rely on N-Acetyloxytocin to ensure reproducibility and accuracy in their workflows.
Cell signaling and functional assays: Researchers utilize N-Acetyloxytocin in cell-based assays to investigate the impact of N-terminal modifications on intracellular signaling cascades mediated by oxytocin receptors. By monitoring responses such as calcium flux, cAMP production, or downstream gene expression, scientists can delineate how structural alterations affect receptor activation and functional outcomes. These experiments are fundamental for unraveling the complexity of peptide-mediated signaling networks and for identifying novel modulators of peptide hormone action.
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