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Argipressin, also known as arginine vasopressin (AVP) or [Arg8]-vasopressin, is a nine-residue neurohypophysial peptide that activates V1a, V1b and V2 vasopressin receptors. The mature sequence contains an intramolecular Cys1-Cys6 disulfide bond and terminates in Gly-NH₂.
Although commonly associated with renal water conservation and vascular tone, AVP also provides a useful experimental system for comparing receptor-subtype signaling because its three principal receptors couple to distinct intracellular pathways and occur in different physiological contexts.
Product Information
| Property | Specification |
|---|---|
| Product Name | Argipressin Acetate |
| Catalog No. | AS2504 |
| Peptide Identity | Arginine Vasopressin / AVP / [Arg8]-Vasopressin |
| Sequence | Cys-Tyr-Phe-Gln-Asn-Cys-Pro-Arg-Gly-NH₂ |
| One-Letter Sequence | CYFQNCPRG-NH₂ |
| Peptide Length | 9 amino-acid residues |
| Peptide Formula | C46H65N15O12S2 |
| Peptide Moiety Molecular Weight | Approximately 1084.23 Da |
| Disulfide Bond | Cys1-Cys6 |
| C-Terminus | Gly-NH₂ |
| Primary Receptors | V1a / AVPR1A, V1b / AVPR1B, V2 / AVPR2 |
| Salt Form | Acetate; exact counterion composition should be determined from lot-specific documentation |
A Posterior Pituitary Peptide with Three Receptor Pathways
Arginine vasopressin is synthesized in hypothalamic neurons and transported to the posterior pituitary for storage and release. Its experimental effects are mediated principally through three G protein-coupled receptor subtypes: V1a, V1b and V2.
The receptors share a common endogenous ligand but differ substantially in tissue distribution and signal transduction. This makes AVP useful for studying how one short cyclic peptide can generate distinct responses through related GPCRs.
V1a, V1b and V2 Receptor Signaling
| Receptor | Major Signaling Route | Representative Research Context |
|---|---|---|
| V1a / AVPR1A | Gq/11 → phospholipase C → intracellular Ca2+ | Vascular smooth muscle and cardiovascular signaling |
| V1b / AVPR1B | Gq/11 → phospholipase C → intracellular Ca2+ | Anterior pituitary corticotroph and neuroendocrine regulation |
| V2 / AVPR2 | Gs → adenylyl cyclase → cAMP | Renal collecting-duct water transport |
Because V1a and V1b predominantly couple to phospholipase C pathways while V2 activates Gs/cAMP signaling, receptor expression should be specified whenever AVP potency or cellular responses are compared between experimental systems.
V1b Receptor and Pituitary Signaling
The V1b receptor provides an important reason to study Argipressin specifically within pituitary and neuroendocrine research. AVPR1B is expressed prominently in anterior pituitary corticotroph cells, where vasopressin can modulate ACTH release and interact functionally with corticotropin-releasing hormone signaling.
This activity is distinct from the renal V2 pathway and from the vascular actions associated with V1a. Experiments focused on the hypothalamic–pituitary–adrenal axis should therefore distinguish V1b-mediated responses from the other vasopressin receptor subtypes.
V2 Receptor and Water-Transport Research
In renal collecting-duct principal cells, V2 receptor activation increases cAMP and regulates trafficking of aquaporin-2 water channels. This pathway provides a well-defined model for studying Gs-coupled receptor signaling, membrane-protein trafficking and epithelial water transport.
We recommend reporting receptor subtype, cellular background and stimulation time when comparing V2 signaling with V1-family responses because the downstream readouts are mechanistically different.
Disulfide Ring and C-Terminal Amidation
The Cys1-Cys6 disulfide bridge creates a cyclic six-residue region at the N-terminal portion of the molecule, while Pro7-Arg8-Gly9-NH₂ forms the short C-terminal tail.
Arg8 is a defining feature of arginine vasopressin and differentiates this mammalian peptide from lysine-containing vasopressin variants found in some other species. The terminal Gly-NH₂ is also part of the mature molecular identity and should be preserved when native-sequence receptor activity is the experimental objective.
Argipressin and Oxytocin Receptor-Family Pharmacology
Vasopressin and oxytocin belong to a closely related family of cyclic nonapeptides, and their receptors also share substantial structural similarity. As a result, receptor selectivity is not absolute under every assay condition.
High ligand concentrations or differences in receptor expression can increase cross-receptor responses. We therefore recommend using receptor-selective controls when experiments are intended to distinguish vasopressin-receptor signaling from oxytocin-receptor activity.
Acetate Form and Molecular-Weight Calculations
The formula C46H65N15O12S2 and molecular weight of approximately 1084.23 Da describe the Argipressin peptide moiety itself.
If the supplied material contains acetate counterion, its total dry mass can include additional acetate and residual water. Counterion stoichiometry should therefore be taken from lot-specific analytical documentation when precise molar concentration is required.
For quantitative receptor assays, we recommend calculating concentration from actual peptide content rather than assuming that the entire lyophilized mass consists of peptide moiety.
Experimental and Analytical Considerations
Correct disulfide formation is part of the intended Argipressin structure. A reduced peptide containing free Cys1 and Cys6 residues is not structurally equivalent to native AVP.
For receptor-binding, signaling or quantitative biochemical studies, molecular identity should be assessed together with chromatographic purity. Our Peptide Quality Control capabilities support analytical HPLC and mass spectrometry according to the selected specification.
Research Applications
Argipressin can support vasopressin receptor pharmacology, intracellular Ca2+ assays, cAMP signaling, renal water-transport studies, vascular smooth-muscle research, pituitary V1b signaling and neuroendocrine pathway investigations.
Related endocrine and neuroactive research materials can be explored in our Pituitary Hormones collection.
Receptor-selective analogs, residue substitutions, labeled derivatives and other vasopressin-family sequences can be evaluated through our Chemical Peptide Synthesis capabilities.
Frequently Asked Questions
Is Argipressin the same peptide as arginine vasopressin?
Yes. Argipressin is the pharmaceutical and biochemical name commonly used for arginine vasopressin, also abbreviated AVP or [Arg8]-vasopressin.
Which vasopressin receptors does Argipressin activate?
Its principal targets are V1a, V1b and V2 receptors. V1a and V1b predominantly signal through Gq/11-linked phospholipase C pathways, whereas V2 primarily couples to Gs and cAMP production.
Why is Argipressin relevant to pituitary research?
V1b receptors are prominently expressed in anterior pituitary corticotroph cells and participate in vasopressin-dependent regulation of ACTH secretion and hypothalamic–pituitary–adrenal signaling.
Does 1084.23 Da include acetate?
No. Approximately 1084.23 Da is the molecular weight of the Argipressin peptide moiety. Acetate counterion and residual water must be considered separately when total material composition is required.