Oxytocin free acid

Oxytocin Free Acid is the non-amidated form of the cyclic nonapeptide, leaving a free carboxyl terminus. The change in terminal charge influences overall dipole, solubility, and hydrogen-bond patterns. Researchers compare its conformation and receptor-binding features with C-terminally amidated analogs. Applications include cyclic-peptide structure studies, acid-amide effects analysis, and analog design.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
Oxytocin free acid(CAS 24346-32-5)

CAT No: R2383

CAS No:24346-32-5

Synonyms/Alias:Oxytocin free acid;24346-32-5;Oxytocin (free acid);2-[[(2S)-2-[[(2S)-1-[(4R,7S,10S,13S,16S,19R)-19-amino-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]pyrrolidine-2-carbonyl]amino]-4-methylpentanoyl]amino]acetic acid;HY-P3216;AS-86440;CS-0169706;G77862;H-CYS-TYR-ILE-GLN-ASN-CYS-PRO-LEU-GLY-OH;[(2S)-2-{[(2S)-1-[(4R,7S,10S,13S,16S,19R)-19-amino-13-[(2S)-butan-2-yl]-10-(2-carbamoylethyl)-7-(carbamoylmethyl)-16-[(4-hydroxyphenyl)methyl]-6,9,12,15,18-pentaoxo-1,2-dithia-5,8,11,14,17-pentaazacycloicosane-4-carbonyl]pyrrolidin-2-yl]formamido}-4-methylpentanamido]acetic acid;

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M.F/Formula
C43H65N11O13S2
M.W/Mr.
1008.2
Sequence
One Letter Code:CYIQNCPLG
Three Letter Code:H-Cys(1)-Tyr-Ile-Gln-Asn-Cys(1)-Pro-Leu-Gly-OH

Oxytocin free acid, a naturally occurring nonapeptide hormone, is a widely studied carbohydrate compound notable for its distinct structure and significant biological roles. Comprising a sequence of nine amino acids, this peptide is distinguished by its unique disulfide bond, which imparts structural stability and biological specificity. As the free acid form, it represents the carboxyl-terminated variant of oxytocin, making it particularly relevant in research settings that require precise molecular forms for biochemical and pharmacological studies. Its solubility and compatibility with various analytical techniques enable researchers to explore its multifaceted actions without the confounding effects of additional salt forms or impurities. The availability of oxytocin as a free acid provides advanced opportunities for investigation into its mechanisms, receptor interactions, and downstream signaling pathways, supporting both fundamental and applied scientific research.

Neuroscience research: Oxytocin free acid is extensively utilized in neuroscience to elucidate the molecular and cellular mechanisms underlying social behavior, emotional regulation, and neuroendocrine signaling. By applying this peptide to in vitro neuronal cultures or in vivo models, researchers can dissect its influence on synaptic plasticity, neurotransmitter release, and neural circuitry modulation. Studies often focus on its interaction with the oxytocin receptor, a G-protein coupled receptor, to understand how oxytocinergic signaling contributes to complex behaviors such as bonding, stress response, and social recognition. The free acid form allows for precise dosing and minimal interference from extraneous ions, enhancing the reliability of experimental outcomes and facilitating the development of new hypotheses regarding neuropeptide function.

Receptor binding assays: The free acid variant of oxytocin is a preferred ligand in receptor binding assays aimed at characterizing the affinity, selectivity, and kinetics of oxytocin receptors. Utilizing radiolabeled or fluorescently tagged oxytocin free acid, researchers can conduct competitive binding studies to map receptor distribution, evaluate ligand-receptor interactions, and screen for potential modulators or antagonists. These assays are critical for drug discovery efforts targeting the oxytocinergic system, as they provide quantitative insights into how structural modifications or analogs may alter receptor engagement. The high purity and defined structure of the free acid form ensure consistent and interpretable results across different experimental platforms.

Peptide synthesis and analog development: Oxytocin free acid serves as a foundational scaffold in the chemical synthesis of peptide analogs and derivatives. Its well-characterized sequence and terminal carboxyl group enable chemists to perform site-specific modifications, such as residue substitution, cyclization, or conjugation with functional moieties. These synthetic efforts are pivotal for probing structure-activity relationships, enhancing peptide stability, or tailoring pharmacokinetic profiles for research applications. The availability of this compound in its free acid form streamlines synthetic workflows, reduces the need for additional deprotection steps, and supports the generation of libraries of novel oxytocin analogs for further study.

Analytical method development: In analytical chemistry, oxytocin free acid is employed as a reference standard or calibration compound for the development and validation of quantitative assays. Techniques such as high-performance liquid chromatography (HPLC), mass spectrometry (MS), and capillary electrophoresis (CE) rely on well-defined standards to ensure accuracy and reproducibility. By incorporating this peptide into assay protocols, laboratories can optimize detection sensitivity, linearity, and specificity for oxytocin and related peptides in complex biological matrices. The free acid form is particularly advantageous for method development due to its compatibility with a wide range of solvents and detection systems, contributing to the advancement of robust analytical platforms.

Cell signaling studies: Researchers investigating intracellular signaling pathways frequently utilize oxytocin free acid to activate or inhibit specific cascades downstream of the oxytocin receptor. By treating cultured cells or tissue explants with controlled concentrations of the peptide, scientists can monitor changes in second messenger levels, phosphorylation events, and gene expression profiles. These studies shed light on the diverse physiological effects mediated by oxytocinergic signaling, including modulation of calcium flux, MAPK activation, and transcriptional regulation. The use of the free acid form ensures that observed effects are attributable to the peptide itself, free from confounding influences of counter-ions or stabilizing agents, thereby enhancing the fidelity of cell signaling research and supporting the discovery of novel molecular targets.

InChI
InChI=1S/C43H65N11O13S2/c1-5-22(4)35-42(66)48-26(12-13-32(45)56)38(62)50-29(17-33(46)57)39(63)52-30(20-69-68-19-25(44)36(60)49-28(40(64)53-35)16-23-8-10-24(55)11-9-23)43(67)54-14-6-7-31(54)41(65)51-27(15-21(2)3)37(61)47-18-34(58)59/h8-11,21-22,25-31,35,55H,5-7,12-20,44H2,1-4H3,(H2,45,56)(H2,46,57)(H,47,61)(H,48,66)(H,49,60)(H,50,62)(H,51,65)(H,52,63)(H,53,64)(H,58,59)/t22-,25-,26-,27-,28-,29-,30-,31-,35-/m0/s1
InChI Key
NFBCSRNZYJJWNB-DSZYJQQASA-N

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