δ-Ava7-Atosiban is a modified atosiban analogue featuring δ-Ava substitution to adjust conformational and physicochemical properties. The change influences backbone flexibility, hydrophobic surface, and receptor-contact regions. Researchers compare its structural ensemble and binding behavior with the parent peptide. Applications include analog-optimization work, SAR exploration, and peptide-structure refinement.
CAT No: R2849
Synonyms/Alias:(4R,7S,10S,13S,16R)-N-(5-(((S)-5-amino-1-((2-amino-2-oxoethyl)amino)-1-oxopentan-2-yl)amino)-5-oxopentyl)-7-(2-amino-2-oxoethyl)-13-((S)-sec-butyl)-16-(4-ethoxybenzyl)-10-((R)-1-hydroxyethyl)-6,9,12,15,18-pentaoxo-1,2-dithia-5,8,11,14,17-pentaazacycloicosane-4-carboxamide
δ-Ava7-Atosiban is a synthetic peptide derivative engineered to investigate the biochemical mechanisms underlying oxytocin and vasopressin receptor modulation. As a structurally modified analog of the well-characterized oxytocin/vasopressin antagonist Atosiban, δ-Ava7-Atosiban incorporates non-standard amino acid substitutions to enhance its receptor selectivity and stability in experimental systems. Its unique sequence design makes it a valuable tool for dissecting the roles of peptide hormones in cellular signaling and receptor-ligand interactions, supporting advanced research in neuroendocrinology, pharmacology, and receptor biology.
Receptor Binding Studies: δ-Ava7-Atosiban serves as a potent molecular probe for evaluating the binding affinities and selectivity profiles of oxytocin and vasopressin receptors, particularly the OXTR and V1a/V1b subtypes. By introducing specific modifications such as the δ-Ava7 residue, researchers can assess how structural changes influence ligand-receptor interactions and downstream signaling events. This peptide is frequently utilized in in vitro binding assays, radioligand displacement experiments, and surface plasmon resonance analyses to elucidate the molecular determinants of receptor specificity.
Signal Transduction Research: The compound's ability to selectively antagonize peptide hormone receptors makes it instrumental in mapping intracellular signaling cascades triggered by oxytocin and vasopressin. By blocking receptor activation, δ-Ava7-Atosiban allows scientists to differentiate between direct and indirect signaling effects, facilitating the study of G-protein coupled receptor (GPCR) pathways, second messenger systems, and regulatory mechanisms that control hormone-mediated cellular responses. Its application is particularly relevant in models that dissect the crosstalk between neuropeptide signaling networks.
Peptide Structure-Activity Relationship (SAR) Analysis: As a designer peptide with targeted sequence modifications, δ-Ava7-Atosiban is highly valuable in SAR studies aimed at optimizing peptide therapeutics and receptor modulators. Researchers employ this analog to systematically evaluate how specific amino acid substitutions affect biological activity, receptor affinity, and metabolic stability. Data generated from such studies contribute to the rational design of next-generation peptide antagonists with improved pharmacological profiles.
Neuroendocrine Pathway Investigation: The use of δ-Ava7-Atosiban extends to the exploration of neuroendocrine regulatory mechanisms, where it acts as a selective antagonist to dissect the physiological and biochemical roles of oxytocin and vasopressin. In ex vivo tissue preparations, organotypic cultures, or recombinant cell systems, the peptide enables precise modulation of hormone signaling, supporting studies on stress response, social behavior, and homeostatic regulation. Its application is integral to understanding the complexity of neuropeptide function in both central and peripheral contexts.
Peptide Stability and Metabolism Studies: The structural modifications present in δ-Ava7-Atosiban, such as the incorporation of δ-amino acids, provide an opportunity to investigate the impact of sequence alterations on peptide stability and metabolic resistance. Researchers utilize this analog to assess degradation kinetics in serum, tissue homogenates, or enzymatic systems, generating insights into strategies for enhancing peptide half-life and bioavailability in experimental settings. These findings are critical for advancing the design of robust peptide-based research tools and molecular probes.
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