151937-33-6

Basic information

• Product Name: 1,Cys(SH)⁶>-oxytocin
• Synonyms: 1,Cys(SH)⁶>-oxytocin
• CAS NO: 151937-33-6
• Molecular Weight: 1080.3
• Mol File: 151937-33-6.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: 1,Cys(SH)⁶>-oxytocin(CAS DataBase Reference)
• NIST Chemistry Reference: 1,Cys(SH)⁶>-oxytocin(151937-33-6)
• EPA Substance Registry System: 1,Cys(SH)⁶>-oxytocin(151937-33-6)

Safety Data

• Hazardous Substances Data: 151937-33-6(Hazardous Substances Data)

Downstream Products

• 50-56-6 oxytocin 

Relevant articles and documents

Nature-inspired dimerization as a strategy to modulate neuropeptide pharmacology exemplified with vasopressin and oxytocin

Vasopressin (VP) and oxytocin (OT) are cyclic neuropeptides that regulate fundamental physiological functionsviafour G protein-coupled receptors, V1aR, V1bR, V2R, and OTR. Ligand development remains challenging for these receptors due to complex structure-activity relationships. Here, we investigated dimerization as a strategy for developing ligands with novel pharmacology. We regioselectively synthesised and systematically studied parallel, antiparallel and N- to C-terminal cyclized homo- and heterodimer constructs of VP, OT and dVDAVP (1-deamino-4-valine-8-d-arginine-VP). All disulfide-linked dimers, except for the head-to-tail cyclized constructs, retained nanomolar potency despite the structural implications of dimerization. Our results support a single chain interaction for receptor activation. Dimer orientation had little impact on activity, except for the dVDAVP homodimers, where an antagonist to agonist switch was observed at the V1aR. This study provides novel insights into the structural requirements of VP/OT receptor activation and spotlights dimerization as a strategy to modulate pharmacology, a concept also frequently observed in nature.

Counterion exchange process for peptides

The invention encompasses a process for purifying a peptide comprising loading a peptide onto a RP-HPLC column; washing the column with an aqueous solution of a pharmaceutically acceptable counterion salt; and eluting the peptide from the column with a solvent mixture of a organic solvent and an acid of the pharmaceutically acceptable counterion, wherein the aqueous solution has a pH of at least about 6.