Oxytocin antiparallel dimer features two oxytocin chains aligned in an antiparallel configuration held by disulfide linkages. Researchers explore its multimeric folding, steric complementarity, and extended binding surfaces. The dimeric form provides a unique model for cooperative structural behavior.
CAT No: R2293
CAS No:20054-93-7
Synonyms/Alias:Oxytocin antiparallel dimer;20054-93-7;HY-P3222;DA-56525;CS-0169713;G18220;
Oxytocin antiparallel dimer is a specialized peptide compound consisting of two oxytocin molecules arranged in an antiparallel configuration. As a structural variant of the well-characterized neuropeptide oxytocin, this dimeric form exhibits distinct physicochemical properties and potential biological implications compared to its monomeric counterpart. The unique dimerization pattern offers valuable opportunities for investigating peptide-peptide interactions, conformational dynamics, and the functional consequences of oligomerization within peptide hormone systems. Its well-defined structure makes it a significant tool for researchers studying the molecular underpinnings of peptide assembly, receptor engagement, and the modulation of peptide activity in both in vitro and ex vivo settings.
Peptide aggregation studies: The antiparallel dimer serves as a robust model for exploring the mechanisms of peptide aggregation and oligomerization. By providing a chemically precise dimeric species, it enables detailed investigations into intermolecular forces, hydrogen bonding patterns, and the influence of dimerization on peptide stability. Such studies are essential for understanding how peptide hormones aggregate under physiological or stress conditions, which has implications for both fundamental biochemistry and the development of peptide-based biopharmaceuticals.
Receptor binding research: The distinctive arrangement of the oxytocin antiparallel dimer allows for the examination of how dimerization affects receptor recognition and signaling. Researchers can utilize this dimeric form to probe receptor binding affinities, specificity, and the potential for altered signal transduction compared to the monomer. These insights contribute to a deeper understanding of peptide-receptor interactions and can inform the rational design of peptide analogs or modulators with tailored activity profiles.
Analytical method development: The well-characterized structure of the antiparallel dimer makes it an excellent reference standard or calibration compound in advanced analytical techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and nuclear magnetic resonance (NMR) spectroscopy. Its use supports the validation and optimization of analytical workflows designed to detect, quantify, or characterize peptide dimers and higher-order assemblies in complex biological samples.
Peptide stability and formulation studies: Investigating the stability of the oxytocin antiparallel dimer under various environmental conditions assists researchers in elucidating the factors that influence peptide dimerization and degradation. Such studies are particularly relevant in the context of developing stable peptide formulations for research applications, as they reveal the impact of pH, temperature, and excipients on dimer integrity and aggregation propensity.
Structure-activity relationship (SAR) investigations: The defined antiparallel configuration of the dimer provides a unique scaffold for SAR studies aimed at correlating peptide structure with biological function. By comparing the functional properties of the dimer with those of monomeric oxytocin and other oligomeric forms, researchers can dissect the contributions of dimerization to activity, selectivity, and downstream signaling pathways. These findings are valuable for advancing the field of peptide engineering and for understanding the broader principles governing peptide hormone function.
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