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 carbohydrate-peptide conjugate that has garnered significant attention in the fields of biochemical research and molecular biology. Engineered by incorporating a glycine-glycine moiety at the eighth lysine position of vasopressin, this analog offers unique structural properties that differentiate it from native vasopressin and other peptide derivatives. The introduction of a carbohydrate group at a strategic site not only enhances the molecule's stability and solubility but also modulates its interaction with receptors and enzymes. Researchers value this compound for its potential to serve as a model system in the study of peptide-carbohydrate interactions, receptor binding dynamics, and post-translational modification effects. Its distinct features make it a versatile tool for exploring a variety of biochemical processes and cellular mechanisms.
Receptor Binding Studies: In the context of receptor binding assays, the modified vasopressin analog provides a powerful means to investigate the impact of glycosylation on ligand-receptor interactions. By substituting the eighth residue with a glycine-glycine-lysine motif, scientists are able to observe changes in binding affinity, selectivity, and downstream signaling compared to the native peptide. This enables a deeper understanding of how structural modifications influence the pharmacodynamics and efficacy of peptide hormones. The analog's unique structure is particularly useful for dissecting the contributions of specific amino acid residues and carbohydrate groups to receptor recognition and activation, thereby facilitating the rational design of next-generation peptide therapeutics and research probes.
Enzymatic Degradation Research: The carbohydrate modification present in N-(N-Gly-Gly)-8-Lys-vasopressin makes it an ideal substrate for studying proteolytic resistance and enzymatic degradation pathways. Researchers utilize this compound to evaluate how glycosylation shields peptide backbones from protease activity, thus prolonging peptide half-life in biological systems. Such studies are instrumental in elucidating the mechanisms by which glycopeptides evade enzymatic breakdown, providing valuable insights for the development of more stable peptide-based molecules for research applications. Additionally, comparisons with unmodified vasopressin help to pinpoint the specific contributions of the glycine-glycine-lysine modification to overall peptide stability.
Cell Signaling Pathway Analysis: The synthetic analog's altered structure allows for the detailed analysis of cell signaling cascades initiated by vasopressin receptor activation. By employing this glycopeptide in in vitro cellular models, researchers can track the activation of second messenger systems, such as cyclic AMP or calcium influx, and evaluate how structural modifications affect signal transduction efficiency. These studies are crucial for mapping the molecular determinants of receptor-mediated signaling and for identifying potential targets for modulating these pathways in various physiological contexts. The analog's distinct properties also provide a means to explore receptor subtype specificity and biased agonism, expanding the toolkit available for dissecting complex signaling networks.
Glycopeptide Structure-Activity Relationship (SAR) Studies: N-(N-Gly-Gly)-8-Lys-vasopressin serves as a valuable scaffold for structure-activity relationship investigations focused on glycopeptides. By comparing the biological activities of this analog with other peptide variants, scientists can systematically assess how specific carbohydrate modifications influence functional properties such as receptor activation, internalization, and downstream effects. These SAR studies inform the rational design of peptide analogs with tailored properties for research purposes, enabling the fine-tuning of molecular interactions within biological systems. The analog's defined structure and modifiable sites make it an excellent candidate for iterative synthesis and testing in SAR workflows.
Peptide Transport and Bioavailability Research: The incorporation of a glycine-glycine-lysine moiety on vasopressin provides a model system for exploring the effects of glycosylation on peptide transport and cellular uptake. Investigators use this compound to examine how carbohydrate modifications alter membrane permeability, interaction with transporters, and distribution within biological matrices. Such research is vital for understanding the principles governing peptide absorption, distribution, and retention, which has broad implications for the design of effective peptide-based research tools. By elucidating the impact of glycosylation on bioavailability, scientists can better predict and optimize the behavior of peptide conjugates in complex biological environments.
In summary, the applications of vasopressin, N-(N-Gly-Gly)-8-Lys-, span a diverse range of research areas, including receptor binding studies, enzymatic degradation research, cell signaling pathway analysis, glycopeptide structure-activity relationship investigations, and peptide transport and bioavailability research. Its unique carbohydrate-peptide structure offers distinct advantages for probing molecular interactions, assessing stability and signaling, and advancing the understanding of glycopeptide function in biological systems. Through these varied applications, the analog continues to support innovative research and contributes to the evolving landscape of peptide science.
1. Emu oil in combination with other active ingredients for treating skin imperfections
5. Immune responses to homocitrulline-and citrulline-containing peptides in rheumatoid arthritis
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More