113-81-5

Basic information

• Product Name: deamino-[Arg⁸]-vasopressin
• Synonyms: deamino-[Arg⁸]-vasopressin
• CAS NO: 113-81-5
• Molecular Weight: 1069.23
• Mol File: 113-81-5.mol
• Article Data: 6

Chemical Properties

• CAS DataBase Reference: deamino-[Arg⁸]-vasopressin(CAS DataBase Reference)
• NIST Chemistry Reference: deamino-[Arg⁸]-vasopressin(113-81-5)
• EPA Substance Registry System: deamino-[Arg⁸]-vasopressin(113-81-5)

Safety Data

• Hazardous Substances Data: 113-81-5(Hazardous Substances Data)

Upstream product

• 58928-35-1 Mpa(Bzl)-Tyr(Bzl)-Phe-Gln-Asn-Cys(Bzl)-Pro-D-Arg(TOS)-Gly-NH₂ 
• 6752-21-2 C₄₆H₆₆N₁₄O₁₂S₂ 

Relevant articles and documents

Cyclic Peptide Formation in Reduced Solvent Volumes via In-Line Solvent Recycling by Organic Solvent Nanofiltration

Cyclic peptides have found numerous and wide ranging applications that include drug molecules, nanomaterials, and chiral chromatography stationary phases. However, in the crucial cyclization step, high dilution conditions are often required, resulting in large volumes of solvent being consumed to prepare relatively small quantities of product. This paper demonstrates the synthesis of a cyclic nonapeptide with in-line solvent recycling via organic solvent nanofiltration (OSN) resulting in a significant reduction in the solvent load of the reaction and concomitant improvement in process mass intensification (PMI). The membrane was used to remove the reaction product from the reaction vessel, as the cyclic peptide product shows limited stability in the presence of an excess of reaction reagent. In comparison to the standard batch reaction, no loss in yield or product purity was observed for the OSN process tested. The proof-of-concept study outlined in this paper was performed on a real active pharmaceutical ingredient (API), and the technique used is widely applicable and flexible.

The use of hydrogen peroxide for closing disulfide bridges in peptides

The use of hydrogen peroxide for the formation of disulfide bridges was studied in 15 peptides of various lengths and structures. The oxidation of peptide thiols by hydrogen peroxide was shown to proceed under mild conditions without noticeable side reactions of Trp, Tyr, and Met residues. Yields of the corresponding cyclic disulfides were high and mostly exceeded those obtained with other oxidative agents, in particular, iodine. It was established that the use of hydrogen peroxide in organic medium also provided sufficiently high yields when large-scale syntheses of oxytocin and octreotide (up to 10 g) were carried out.

Synthesis and biological activities of some known arginine-vasopressin (AVP) analogues as precursors of tritiated derivatives

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