N,N'-dimethyl-Gly-Desmopressin

N,N'-Dimethyl-Gly-Desmopressin includes dimethylated glycine modifications that alter terminal charge and backbone flexibility within the desmopressin framework. Such changes impact hydrogen bonding, solubility, and recognition by receptors or enzymes. Researchers use it to explore the effects of N-methylation on peptide stability. Applications include analog-design studies, conformational analysis, and degradation-pathway evaluation.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: R2864

Synonyms/Alias:Mpr-Tyr-Phe-Gln-Asn-Cys-Pro-D-Arg-Gly-N(Me)2 (Disulfide Bridge Mpr1-Cys6)

Custom Peptide Synthesis
cGMP Peptide
  • Registration of APIs
  • CMC information required for an IND
  • IND and NDA support
  • Drug master files (DMF) filing
M.F/Formula
C48H68N14O12S2
M.W/Mr.
1097.28

N,N'-dimethyl-Gly-Desmopressin is a synthetic peptide analogue structurally related to vasopressin, engineered through specific modifications to enhance its biochemical properties and functional selectivity. As a derivative of desmopressin, this compound incorporates N,N'-dimethylation and a glycine substitution, conferring altered receptor affinity and metabolic stability. Its unique structure makes it a valuable tool for probing peptide-receptor interactions, dissecting signaling pathways, and supporting peptide-based research in neuroendocrinology and renal physiology. The compound's design enables researchers to investigate the nuanced roles of peptide analogues in cellular signaling and receptor modulation, broadening the understanding of peptide hormone function and facilitating innovation in peptide chemistry.

Receptor binding studies: Researchers utilize N,N'-dimethyl-Gly-Desmopressin to investigate the binding characteristics and selectivity of vasopressin and oxytocin receptor subtypes. The compound's structural modifications allow for comparative analyses of ligand-receptor affinity, helping to delineate the contributions of specific amino acid residues and functional groups to receptor recognition and activation. These studies are essential for mapping receptor pharmacology and identifying determinants of selectivity, which underpin the rational design of next-generation peptide ligands.

Signal transduction research: In cellular and molecular experiments, this peptide analogue serves as a probe to elucidate downstream signaling cascades initiated by vasopressin receptor activation. Its altered profile enables scientists to dissect G-protein coupled receptor (GPCR) mediated pathways, such as those regulating cyclic AMP production or intracellular calcium mobilization. By comparing responses elicited by desmopressin derivatives, researchers gain insights into structure-activity relationships and the molecular mechanisms governing peptide hormone signaling.

Peptide structure-activity relationship analysis: The incorporation of N,N'-dimethylated glycine residues in the peptide backbone provides an opportunity to evaluate how specific chemical modifications influence biological activity and metabolic stability. Researchers employ this compound in systematic SAR studies to assess the impact of methylation and amino acid substitution on peptide conformation, receptor interaction, and enzymatic degradation. These findings inform the design of novel peptide analogues with tailored pharmacological properties for research applications.

Peptide synthesis and analytical method development: N,N'-dimethyl-Gly-Desmopressin serves as a reference standard and model compound in the development and optimization of synthetic protocols for modified peptides. Its defined structure and physicochemical properties make it suitable for validating chromatographic, spectrometric, and purification techniques commonly used in peptide chemistry laboratories. The compound is also valuable in method validation for quantifying peptide analogues in complex matrices, supporting quality control and analytical research.

Neuroendocrine research: The compound's functional similarity to vasopressin analogues enables its use in studies exploring the regulation of water homeostasis, osmoregulation, and neurohypophyseal hormone signaling. It facilitates the investigation of peptide-mediated communication in the central nervous system and peripheral tissues, providing a controlled means to probe the physiological and biochemical effects of synthetic peptide variants. Researchers leverage these insights to deepen understanding of hormone action, receptor dynamics, and the broader implications of peptide modification in neuroendocrine systems.

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