Vasopressin, N-(N-Gly-Gly)-8-Lys- introduces an N-terminal diglycine extension and lysine substitution at position eight, modifying charge distribution and ring dynamics. Researchers explore altered receptor affinity, folding patterns, and oxidative susceptibility. Applications include peptide-analogue design, structure-function studies, and cyclic-peptide modeling.
CAT No: R2591
CAS No:14943-47-6
Synonyms/Alias:Vasopressin, N-(N-gly-gly)-8-lys-;14943-47-6;Triglycyl-desglycine amide lysine vasopressin;N-(N-Glycylglycyl)-8-lysine vasopressin;Vasopressin, N-(N-glycylglycyl)-8-lysine-;Vasopressin, N-(N-glycylglycyl)-8-L-lysine-;DTXSID50164267;(2S)-1-[(4R,7S,10S,13S,16S,19R)-19-[[2-[(2-aminoacetyl)amino]acetyl]amino]-7-(2-amino-2-oxoethyl)-10-(3-amino-3-oxopropyl)-13-benzyl-16-[(4-hydroxyphenyl)methyl]-6,9,12,15,18-pentaoxo-1,2-dithia-5,8,11,14,17-pentazacycloicosane-4-carbonyl]-N-[(2S)-6-amino-1-[(2-amino-2-oxoethyl)amino]-1-oxohexan-2-yl]pyrrolidine-2-carboxamide;DTXCID1086758;
Vasopressin, N-(N-Gly-Gly)-8-Lys- is a synthetic peptide analog derived from the naturally occurring antidiuretic hormone vasopressin, featuring a unique modification at the eighth lysine residue with an N-(N-Gly-Gly) extension. As a member of the peptide hormone family, this compound is structurally engineered to facilitate targeted research into peptide-receptor interactions, structure-activity relationships, and signaling pathways associated with vasopressin analogs. Its distinctive sequence variation offers researchers a valuable tool for dissecting the molecular determinants of receptor selectivity and biological activity in neuroendocrine systems. The compound's relevance extends to studies focused on peptide modification, receptor pharmacology, and the development of novel peptide-based probes.
Peptide-receptor interaction studies: The modified structure of N-(N-Gly-Gly)-8-Lys-vasopressin provides a strategic platform for investigating the binding affinity and selectivity of vasopressin analogs at vasopressin receptor subtypes, such as V1a, V1b, and V2. By introducing the Gly-Gly extension at the lysine position, researchers can probe the impact of N-terminal modifications on ligand-receptor recognition, offering insights into the spatial and chemical requirements for optimal receptor engagement. Such studies are pivotal for elucidating the structural basis of peptide hormone signaling and for guiding the rational design of selective receptor modulators.
Structure-activity relationship (SAR) analysis: The unique modification present in this analog enables detailed SAR investigations, allowing scientists to systematically assess how specific sequence alterations influence biological activity and receptor response. Using this compound as a model, researchers can map the contributions of the N-terminal extension to the peptide's conformational dynamics, stability, and functional efficacy. These findings support the broader effort to understand the determinants of peptide hormone activity and to optimize analogs for enhanced research applications.
Peptide synthesis methodology development: Owing to its non-standard modification, N-(N-Gly-Gly)-8-Lys-vasopressin serves as a challenging template for testing and refining synthetic strategies in solid-phase peptide synthesis. The presence of a dipeptide extension at a lysine residue offers a practical system for evaluating coupling efficiencies, protecting group strategies, and purification protocols relevant to complex peptide analogs. Such work advances the field of synthetic peptide chemistry by providing benchmarks for yield, fidelity, and scalability in the assembly of modified peptide hormones.
Pharmacological assay calibration: In receptor binding and signaling assays, this analog can be employed as a reference or test ligand to calibrate assay sensitivity and specificity for vasopressin receptor studies. Its defined modification allows for comparative analyses with native and other synthetic analogs, facilitating the validation of assay platforms and the interpretation of ligand-receptor interaction data. This application is particularly valuable in the context of high-throughput screening and pharmacological profiling of peptide ligands.
Biophysical characterization of peptide conformation: The introduction of an N-(N-Gly-Gly) group at the eighth lysine residue provides a distinctive system for exploring the conformational properties of modified peptides using techniques such as circular dichroism, NMR spectroscopy, and molecular modeling. By analyzing how the dipeptide extension influences secondary structure, folding, and solvent interactions, researchers can gain deeper understanding of the relationship between sequence modification and peptide biophysics. These studies contribute to the knowledge base required for the rational engineering of peptide-based research tools and probes.
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