83595-73-7

Upstream product

• 74939-29-0 H-Val-Gly-OBzl*TFA 
• 66714-34-9 Boc-Ala-ONB 
• 15761-38-3 L-N-Boc-Ala 
• 74221-51-5 L-valylglycine benzyl ester hydrochloride 
• 13734-41-3 t-Boc-L-valine 
• 64918-37-2 Boc-L-Val-Gly-OBzl 
• 74939-28-9 H-Val-Gly-OBn 

Downstream Products

• 83595-75-9 H-Ala-Val-Gly-OBzl trifluoroacetic acid salt 

Relevant academic research and scientific papers

Development of supramolecular organo-gel based on tripeptide skeletons

Boc-Ser-Val-Gly-OCH2Ph (31) showed high gelation abilities in the aromatic solvents, particularly in toluene. The minimum gelation concentration of 31 in toluene was 10 mg/ml, suggesting that 2500 molecules of toluene were immobilized by each m

Kinetic studies on oxidation of Gly-Val-Gly, Gly-Phe-Ply and Ala-Val-Gly using Mn(III)

The fragments of elastin sequences, glycyl-valyl-glycine (GVG), glycyl-phenylalanyl-glycine (GFG) and alanyl-valyl-glycine (AVG) have been synthesized by classical solution phase method and characterized. Kinetics of oxidation of these tripeptides (TP) by Mn(III) has been studied in the presence of sulphate ions in acidic medium at 25°C. The reaction follows spectrophotometrically at Λmax 500 nm. A first order dependence of rate on both [Mn(III)] and [TP] has been observed. The rate is independent of concentrations of reduction product, Mn(II) and hydrogen ions. Effects of varying dielectric constant of the medium and addition of anions such as sulphate, chloride and perchlorate have been studied. Activation parameters have been evaluated using Arrhenius and Erying plots. The oxidation products are isolated and characterized. A tentative mechanism involving the reaction of TP with Mn(III) in the rate-limiting step is suggested. The effect of hydrophobicity of amino acids on the rate of oxidation is discussed.

Syntheses and biological activities of bombesin analogs modified in the C-terminal dipeptide part

Bombesin receptor antagonists are possible therapeutic agents due to their ability to act as inhibitors of cellular proliferation. On the basis of our hypothesis on the mechanism of action of gastrin associating an activating enzyme system to the receptor and on the results reported in the litterature, we have synthesized bombesin analogues which have been modified in the C-terminal Leu13-Leu14 amide part. We have shown that modification in the C-terminal part of the bombesin strongly affected the biological activity in rat pancreatic acini. The most potent compound which is described here, H-D-Phe-Gln-Trp-Ala-Val-Gly-His-Leu-Ψ/(CH2)Leu-NH2, was able to recognize the bombesin receptor on rat pancreatic acini (Ki 4.3 nM) and antagonized the bombesin stimulated amylase secretion (Ki 7.7 nM).

New Protecting Groups for the Indole Ring of Tryptophan in Peptide Synthesis: 2,4,6-Trimethoxybenzenesulfonyl and 4-Methoxy-2,3,6-trimethylbenzenesulfonyl Groups

Five substituted benzenesulfonyl groups, p-toluenesulfonyl, p-methoxybenzenesulfonyl, 2,4-dimethoxybenzenesulfonyl, 2,4,6-trimethoxybenzenesulfonyl, and 4-methoxy-2,3,6-trimethylbenzenesulfonyl, were introduced at Nin of tryptophan and their protecting group properties were investigated.Among them, 2,4,6-trimethoxybenzenesulfonyl and 4-methoxy-2,3,6-trimethylbenzenesulfonyl are stable to trifluoroacetic acid, but can be readily removed by hydrogen fluoride or methanesulfonic acid, and suppress decomposition and modification of the tryptophan residue during peptide synthesis.These protecting groups were successfully used in syntheses of bombesin, a potent analog of luteinizing hormone-releasing hormone by the solution method and dynorphin by the solid-phase method.Keywords-peptide synthesis; tryptophan; protecting group; 2,4,6-trimethoxybenzenesulfonyl group; 4-methoxy-2,3,6-trimethylbenzenesulfonyl group