Argipressin (Dimer, Antiparallel) consists of two argipressin molecules arranged in an antiparallel orientation, forming a higher-order assembly. Dimerization influences hydrodynamic properties, local conformation, and multivalent binding behavior. Researchers probe its aggregation dynamics and receptor-interaction profiles. Applications include supramolecular peptide studies, multivalent ligand design, and structural biophysics.
CAT No: Z10-101-168
Synonyms/Alias:2[L-cystyl-L-tyrosyl-L-phenylalanyl-L-glutaminyl-L-asparginyl-L-cystyl-L-prolyl-L-arginyl-glycinamide] (inter-disulfide bridges between 1 | 6’ and 1’ | 6 cysteines); Desmopressin Dimer(Antiparallel); Antiparallel Dimer-AVP; Anti-Parallel Dimer-Vasopressin; N0001-015255;
Argipressin(Dimer, Antiparallel) is a synthetic peptide compound featuring two argipressin units arranged in an antiparallel dimeric configuration. As a derivative of the neurohypophyseal hormone vasopressin, this molecule is structurally engineered to explore the effects of dimerization and orientation on peptide-receptor interactions, conformational stability, and biological activity. Its unique antiparallel dimeric architecture provides a valuable model for investigating peptide folding, intermolecular associations, and the modulation of functional properties in peptide-based systems. Researchers utilize this compound to deepen understanding of peptide structure-function relationships, receptor binding dynamics, and the design of next-generation peptide therapeutics, making it an important tool in both fundamental and applied peptide science.
Peptide-receptor interaction studies: In the context of receptor binding research, the antiparallel dimeric form of argipressin serves as a sophisticated probe to dissect the influence of peptide multimerization and orientation on vasopressin receptor engagement. By comparing the binding affinities and selectivity profiles of the dimeric versus monomeric forms, scientists can elucidate the structural determinants that govern receptor recognition and activation. Such insights are critical for advancing peptide-based drug design, particularly in the development of selective agonists or antagonists targeting vasopressin and related receptors.
Conformational analysis and peptide folding research: The antiparallel dimeric structure of this compound provides a distinctive system for studying peptide folding, intermolecular interactions, and conformational dynamics. Using techniques such as nuclear magnetic resonance (NMR) spectroscopy, circular dichroism (CD), or X-ray crystallography, researchers can analyze how dimerization in an antiparallel orientation affects secondary and tertiary structure. These studies contribute to a broader understanding of peptide stability, folding pathways, and the physicochemical principles underlying peptide assembly.
Peptide engineering and design: Argipressin(Dimer, Antiparallel) is employed as a reference molecule in the field of peptide engineering, where it aids in the rational design of dimeric or multimeric peptide constructs with tailored bioactivity. By examining the functional consequences of antiparallel versus parallel dimer arrangements, scientists can optimize peptide sequences for enhanced stability, receptor specificity, or controlled biological responses. This knowledge is instrumental in the creation of novel peptide-based biomaterials, molecular probes, or research tools.
Analytical method development: The unique structural features of the antiparallel dimer make it a suitable standard or model compound for developing and validating analytical techniques used in peptide research. Chromatographic, spectroscopic, and mass spectrometric methods can be optimized using this molecule to ensure accurate detection, quantification, and characterization of complex peptide assemblies. Its well-defined dimeric nature enables benchmarking of analytical performance in the context of higher-order peptide structures.
Structure-activity relationship (SAR) investigations: By systematically comparing the biological and physicochemical properties of the antiparallel dimer with other argipressin analogues, researchers can map the structure-activity relationships that underpin peptide function. These comparative studies reveal how dimer orientation and molecular architecture influence receptor activation, signal transduction, and downstream effects. The resulting SAR data guide the selection and optimization of peptide candidates for further biochemical or pharmacological research, supporting innovation in peptide science and technology.
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