35748-51-7

Basic information

• Product Name: PRESSINOIC ACID
• Synonyms: H-Cys-Tyr-Phe-Gln-Asn-Cys-OH, (Disulfide bond);L-Cys(1)-L-Tyr-L-Phe-L-Gln-L-Asn-L-Cys(1)-OH
• CAS NO: 35748-51-7
• Molecular Formula: C₃₃H₄₂N₈O₁₀S₂
• Molecular Weight: 774.873
• Mol File: 35748-51-7.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 1373°Cat760mmHg
• Flash Point: 784.2°C
• Appearance: /
• Density: 1.325g/cm³
• Vapor Pressure: 0mmHg at 25°C
• Refractive Index: 1.577
• CAS DataBase Reference: PRESSINOIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: PRESSINOIC ACID(35748-51-7)
• EPA Substance Registry System: PRESSINOIC ACID(35748-51-7)

Safety Data

• Hazardous Substances Data: 35748-51-7(Hazardous Substances Data)

Usage

Enzyme inhibitor

This cyclic hexapeptide (FW = 774.86 g/mol; CAS 35748-51-7) corresponds to the N-terminal six amino acyl residues of vasopressin. If Phe-3 is replaced with Ile, the resulting cyclic hexapeptide, known as tocinoic acid. is identical to the N-terminal six amino acid residues of oxytocin. Pressinoic acid has no known pressor activity, perhaps as result of the loss of the carboxy-terminal tripeptide and/or the incorrect orientation of the Asn-5 side-chain This hexapeptide also activates pineal acetyl-CoA hydrolase and has a potent corticotrophin-releasing activity. Target(s): serotonin N-acetyltransferase.

InChI:InChI=1/C33H42N8O10S2/c34-20-15-52-53-16-25(33(50)51)41-32(49)24(14-27(36)44)40-29(46)21(10-11-26(35)43)37-30(47)23(12-17-4-2-1-3-5-17)39-31(48)22(38-28(20)45)13-18-6-8-19(42)9-7-18/h1-9,20-25,42H,10-16,34H2,(H2,35,43)(H2,36,44)(H,37,47)(H,38,45)(H,39,48)(H,40,46)(H,41,49)(H,50,51)/t20-,21-,22-,23?,24-,25-/m0/s1

Upstream product

• 108607-43-8 Benzyloxycarbonyl-S-benzylcysteinyl-tyrosyl-phenylalanyl-glutaminyl-asparaginyl-S-benzylcysteine phenylhydrazide 
• 108607-52-9 Benzyloxycarbonyl-S-benzylcysteinyl-tyrosyl-phenylalanyl-glutamine Phenylhydrazide 
• 108607-53-0 Benzyloxycarbonyl-S-benzylcysteinyl-tyrosyl-phenylalanyl-glutamine 
• 108607-50-7 Benzyloxycarbonyl-S-benzylcysteinyl-tyrosyl-phenylalanine 
• 108607-49-4 Benzyloxycarbonyl-S-benzylcysteinyl-tyrosyl-phenylalanine phenylhydrazide 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 108517-79-9 Benzyloxycarbonyl-S-benzylcysteinyl-tyrosyl-phenylalanine methyl ester 
• 16152-80-0 benzyloxycarbonyl-S-benzylcysteinyl-tyrosine ethyl ester 
• 39621-64-2 S-benzyl-N-[(benzyloxy)carbonyl]cysteinyltyrosine 
• 106897-47-6 pressinoic acid (dithiol) 
• 108607-44-9 Benzyloxycarbonyl-S-benzylcysteinyl-tyrosyl-phenylalanyl-glutaminyl-asparaginyl-S-benzylcysteine 

Downstream Products

• 106897-47-6 pressinoic acid (dithiol) 

Relevant articles and documents

A study to develop platinum(iv) complex chemistry for peptide disulfide bond formation

Platinum(iv) complexes with a heterocyclic ligand and an ancillary ligand have been investigated and applied for treating various tumour cell lines. Another application of the Pt(iv) complexes in forming peptide disulfide bonds was investigated in this work. For development of Pt(iv) complex chemistry for disulfide bond formation in peptides, two Pt(iv) complexes, [PtCl2(phen)(en)]Cl2 and [PtCl2(bpy)(en)]Cl2, were synthesized and characterized using elemental analysis, ESI-MS and NMR. Subsequently, they were investigated as oxidants for the formation of disulfide bonds in various peptides. Excellent purities and yields of disulfide-containing peptides were achieved when the reactions were carried out in aqueous solution. The reactions were completed rapidly in a wide range of pH values even in acidic medium at room temperature. An intramolecular disulfide bond was formed in each of the peptides in a solution containing two dithiol-containing peptides, making the Pt(iv) complexes useful for generating disulfide-containing peptide libraries. In addition, the two Pt(iv) complexes can be used as oxidants for the synthesis of disulfide bonds on a resin, which is a more convenient method to synthesize disulfide-containing peptides through automation.

SYNTHESIS OF PRESSINOIC ACID BY ENZYMATICALLY CATALYZED FORMATION OF PEPTIDE BONDS

Three fully enzymatic syntheses of the 1-6 vasopressin hexapeptide were investigated using papain, α-chymotrypsin and thermolysin.Best results were obtained with thermolysin in the 2 + 4 fragment condensation.The α-chymotrypsin-catalysed 3 + 3 condensatio