113-79-1 Usage
Description
Argipressine, also known as [Arg8]-Vasopressin, is the predominant form of mammalian vasopressin, an antidiuretic hormone. It is a nonapeptide containing an arginine at residue 8 and two disulfide-linked cysteines at residues 1 and 6. Argipressine is available under the brand name Pitressin (Parke-Davis).
Uses
Used in Hormone Therapy:
Argipressine is used as an antidiuretic hormone for the treatment of diabetes insipidus, a condition characterized by excessive urination and thirst. It helps regulate water balance in the body by reducing urine output.
Used in Immunocytochemistry:
Argipressine solution is used as an antigen for preparing preadsorbed antisera, which are essential for immunocytochemistry techniques. This application aids in the study and visualization of specific cellular structures and functions.
Used in Cell Culture Research:
In L6 cell culture of the C5 subclone, Argipressine is used for differentiation studies. This helps researchers understand the mechanisms of cell differentiation and its role in various biological processes.
Used in Vasopressin Tannate Preparation:
Argipressine is a key component in the formulation of vasopressin tannate (Pitressin Tannate), a water-insoluble tannate of vasopressin administered intramuscularly for its prolonged duration of action. This slow release of vasopressin is particularly useful for patients with diabetes insipidus, but it should never be used intravenously.
Indications
ADH (vasopressin) is released primarily in response to
increases in plasma osmolarity or decreases in blood
volume. It produces its antidiuretic activity in the kidney,
causing the cortical and medullary parts of the collecting
duct to become more permeable to water,
thereby increasing water reabsorption, reducing serum
osmolarity, and increasing its volume. It produces this
effect by binding to a subset of vasopressin receptors called V2 that have relatively high affinity
for the hormone. ADH also has actions at sites other
than the kidney. V2 receptors also mediate an increase
in circulating levels of two proteins involved in blood
coagulation: factor VIII and von Willebrand’s factor.At
higher concentrations, ADH interacts with V1 receptors
to cause a general constriction of most blood vessels. It
also interacts with V3 (or V1b) receptors to increase
ACTH release, although the major control of ACTH release
occurs through corticotropin-releasing hormone.
Hazard
A poison.
Biochem/physiol Actions
[Arg8]-Vasopressin solution also known as Antidiuretic hormone, Arginine vasopressin or beta-Hypophamine is a selective and potent vasopressor agent that stabilizes the cardiocirculatory function in normal human as well as in patients suffering from catecholamine-resistant vasodilatory shock. It stimulates three acid-base transporters and hence increases the capability of the cell to regulate pH.
Mechanism of action
ADH itself is available for injections (Pitressin) but
has a half-life of about 15 minutes. Desmopressin
(DDAVP) is an analogue without an amino group at
the first amino acid and with D-arginine instead of Larginine.
This analogue is more stable and has very little
pressor activity. Desmopressin can be given subcutaneously
or nasally, and the effects last for 12 hours.
Clinical Use
Because it is stable, desmopressin is preferred for
treatments especially if pressor effects are not desired.
The primary indication for therapy is central diabetes
insipidus, a disorder that results when ADH secretion is
reduced and that is characterized by polydipsia,
polyuria, and dehydration. Desmopressin is also used to
reduce primary nocturnal enuresis, or bedwetting, in
children. It is useful in people with mild hemophilia A
or with some types of von Willebrand’s disease, in which
von Willebrand’s factor is present at low levels. In these
cases, desmopressin is given when excessive bleeding
occurs or before surgery to help reduce bleeding indirectly
by increasing the amounts of coagulation factors.
A possible adverse effect of desmopressin is water intoxication
if too much is taken.
ADH antagonists, including nonpeptide analogues
that may be taken orally, have been developed with
specificity for each of the receptor types. In the future,
those that block V1 receptors may be useful in treating
hypertension, and those that block V2 receptors may be
useful in any condition of excessive water retention or
hyponatremia, for which so far there is no satisfactory
therapeutic treatment.
Safety Profile
A poison by intravenous route.When heated to decomposition it emits toxic vapors ofNOx and SOx.
Check Digit Verification of cas no
The CAS Registry Mumber 113-79-1 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 1,1 and 3 respectively; the second part has 2 digits, 7 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 113-79:
(5*1)+(4*1)+(3*3)+(2*7)+(1*9)=41
41 % 10 = 1
So 113-79-1 is a valid CAS Registry Number.
InChI:InChI=1/C46H65N15O12S2.C2H4O2/c47-27-22-74-75-23-33(45(73)61-17-5-9-34(61)44(72)56-28(8-4-16-53-46(51)52)39(67)54-21-37(50)65)60-43(71)32(20-36(49)64)59-40(68)29(14-15-35(48)63)55-41(69)31(18-24-6-2-1-3-7-24)58-42(70)30(57-38(27)66)19-25-10-12-26(62)13-11-25;1-2(3)4/h1-3,6-7,10-13,27-34,62H,4-5,8-9,14-23,47H2,(H2,48,63)(H2,49,64)(H2,50,65)(H,54,67)(H,55,69)(H,56,72)(H,57,66)(H,58,70)(H,59,68)(H,60,71)(H4,51,52,53);1H3,(H,3,4)/t27-,28-,29-,30-,31-,32-,33-,34-;/m0./s1
113-79-1Relevant articles and documents
Building bridges for highly selective, potent and stable oxytocin and vasopressin analogs
Beard, Rhiannon,Stucki, Andy,Schmitt, Muriel,Py, Gabrielle,Grundschober, Christophe,Gee, Antony D.,Tate, Edward W.
, p. 3039 - 3045 (2018/03/29)
Oxytocin (OT) is an exciting potential therapeutic agent, but it is highly sensitive to modification and suffers extensive degradation at elevated temperature and in vivo. Here we report studies towards OT analogs with favorable selectivity, affinity and potency towards the oxytocin receptor (OTR), in addition to improving stability of the peptide by bridging the disulfide region with substituted dibromo-xylene analogs. We found a sensitive structure-activity relationship in which meta-cyclized analogs (dOTmeta) gave highest affinity (50 nM Ki), selectivity (34-fold), and agonist potency (34 nM EC50, 87-fold selectivity) towards OTR. Surprisingly, ortho-cyclized analogs demonstrated OTR and vasopressin V1a receptor subtype affinity (220 nM and 69 nM, respectively) and pharmacological activity (294 nM and 35 nM, respectively). V1a binding and selectivity for ortho-cyclized peptides could be improved 6-fold by substituting a neutral residue at position 8 with a basic amino acid, providing potent antagonists (14 nM IC50) that displayed no activation of the OTR. Furthermore, xylene-bridged analogs demonstrated increased stability compared to OT at elevated temperature, demonstrating promising therapeutic potential for these analogs which warrants further study.
Trans-Dichlorotetracyanoplatinate(IV) as a Reagent for the Rapid and Quantitative Formation of Intramolecular Disulfide Bonds in Peptides
Shi, Tiesheng,Rabenstein, Dallas L.
, p. 4590 - 4595 (2007/10/03)
Oxidation of cysteine thiol groups by trans-dichlorotetracyanoplatinate(IV) to form intramolecular peptide disulfide bonds has been studied for a series of dithiol peptides ranging from 4 to 15 amino acid residues in length. The dithiol peptides are rapidly and quantitatively transformed to their intramolecular disulfide forms by a slight excess of [Pt(CN)4Cl2]2-, as shown by HPLC. Quantitative analyses by HPLC and by spectrophotometric titration confirm a [Pt(IV)]:[dithiol peptide] stoichiometry of 1:1. Under the low pH conditions used, oxidation to form a 38-membered ring in the case of reduced somatostatin is as rapid as that to form much smaller rings, suggesting that ring closure is not the rate-determining step. The oxidation rates increase as the pH is increased. Time-resolved spectra show two isosbestic points, indicating that no peptide-platinum intermediates accumulate to a significant amount. A reaction mechanism similar to that for reduction of [Pt(CN)4Cl2]2- by monothiols is proposed. [Pt(CN)4Cl2]2- is a mild oxidant and essentially substitution inert; its reduction product, [Pt(CN)4Cl2]2-, is stable, has no redox chemistry with peptides, and does not form complexes with peptides. Moreover, [Pt(CN)4Cl2]2- and [Pt(CN)4Cl2]2- are nontoxic and readily separable from peptides by HPLC, and the cost of the Pt(IV) complex is negligible compared with that of peptides. The only unwanted side reaction observed with [Pt(CN)4Cl2]2- is oxidation of the sulfur of methionine to the sulfoxide form. These characteristics and the results of this study suggest that [Pt(CN)4Cl2]2- is an excellent reagent for the formation of intramolecular peptide disulfide bonds.
Thiol/disulfide exchange reactions of captopril and penicillamine with arginine vasopressin and oxytocin
Rabenstein, Dallas L.,Yeo, Pauline L.
, p. 109 - 118 (2007/10/02)
The kinetics and equilibria of the reaction of the thiol-containing drugs captopril (D-3-mercapto-2-methylpropanoyl-L-proline, CpSH) and penicillamine (β, β-dimethylcysteine, PSH) with the disulfide bonds of the neurohypophyseal peptide hormones arginine vasopressin (AVP) and oxytocin (OT) have been characterized. CpSH reacts with AVP and OT by thiol/disulfide interchange to form two peptide-CpSH mixed disulfides, which in turn react with another molecule of CpSH to form the reduced peptide and CpSSCp. Forward and reverse rate constants and the equilibrium constant are reported for both steps in the reaction of CpSH with AVP and OT at pH 7.00. The rate constant for the first step (k1) is much larger than that for the second step (k2). Also, once formed, the peptide-CpSH mixed disulfides rapidly undergo intramolecular thiol/disulfide interchange with reformation of the cyclic peptide and CpSH. PSH reacts with AVP and OT by the same two-step reaction sequence; however, the rate of the second step is very slow due to steric hindrance from the methyl groups of PSH and the PSH moiety of the peptide-PSH mixed disulfides. Using rate constants determined in this study and PSH levels in the plasma of patients on PSH therapy, it is predicted that in vivo reduction of the disulfide bonds of AVP and OT by PSH and CpSH has little effect on the plasma half-lives of AVP or OT.
