42567-71-5

Upstream product

• 2778-34-9 ethyl [(2S)-2-(benzyloxycarbonylamino)-3-phenylpropanoylamino]acetate 
• 30189-51-6 ethyl (N-tert-butoxycarbonyl-L-phenylalanyl)glycinate 
• 1161-13-3 N-Cbz-L-Phe 
• 623-33-6 glycine ethyl ester hydrochloride 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 

Downstream Products

• 2073-59-8 ethyl N-benzyloxycarbonylglycyl-L-phenylalanylglycinate 
• 201789-81-3 N-(methyl 3,4,6-tri-O-acetyl-2-amino-2-deoxy-β-D-glucopyranoside)-N'-carbonyl-L-phenyl-alanyl-glycine ethyl ester 
• 1446350-55-5 N-Boc-L-Phe-Gly-L-Phe-Gly-OEt 
• 74075-21-1 Ts-Phe-Gly-Pro-OBzl 
• 74075-22-2 Ts-Phe-Gly-Pro 
• 74075-20-0 Ts-Phe-Gly 
• 201293-51-8 (S)-4-[(S)-1-[(S)-1-(Ethoxycarbonylmethyl-carbamoyl)-2-phenyl-ethylcarbamoyl]-2-(4-hydroxy-phenyl)-ethyl]-2-(4-hydroxy-benzyl)-3-oxo-piperazine-1-carboxylic acid tert-butyl ester 
• 35646-66-3 Ts-Phe-Gly-OEt 

Relevant academic research and scientific papers

MgI2-Mediated Chemoselective Cleavage of Protecting Groups: An Alternative to Conventional Deprotection Methodologies

The scope of MgI2 as a valuable tool for quantitative and mild chemoselective cleavage of protecting groups is described here. This novel synthetic approach expands the use of protecting groups, widens the concept of orthogonality in synthetic processes, and offers a facile opportunity to release compounds from solid supports. Amazing MgI2: Protecting groups have had a tremendous positive impact on the art of biomolecule synthesis. In a context in which the use of attractive protecting groups is often limited by harsh deprotection conditions and low chemoselective flexibility, MgI2 offers, by the execution of a very simple protocol, a fresh vision with extensive perspectives.

HMDO-promoted peptide and protein synthesis in ionic liquids

Hexamethyldisiloxane (HMDO) has been developed to efficiently promote the metal-free direct coupling of an amino function of one cysteine-free peptide or protein and a C-terminal thioester of the second peptide in ionic liquids. The amide-coupling reaction proceeds smoothly under mild conditions to afford the corresponding products in good to excellent yields (63-94%). Peptide couplings were also achieved using in-situ-generated thioesters by the thioesterification of oxo esters.

Biomimetic peptide bond formation in water with aminoacyl phosphate esters

Aminoacyl phosphates, biomimetic analogues of aminoacyl adenylates, react efficiently with amino acid esters to form dipeptides with retention of stereochemical integrity. The reactions are selective and occur readily in the presence of nucleophiles other than amino groups on their side chains. Aminoacyl phosphate esters that lack an amino-protecting group are also suitable for peptide bond formation, leading to a simplified overall process.

Enhancement of the small intestinal uptake of phenylalanylglycine via a H+/oligopeptide transport system by chemical modification with fatty acids

The transport characteristics of chemically modified phenylalanylglycine (PheGly) with butyric acid (C4-Phe-Gly) and caproic acid (C6-Phe-Gly) were examined using rabbit intestinal brush-border membrane vesicles (BBMVs). In the prese

A Selective Electrocatalytic Cleavage of the Benzyloxycarbonyl Group from Peptides

An electrosynthetic procedure for the cleavage of the benzyloxycarbonyl group from protected amino acids and peptides is described.It is based on the use of a high surface area palladium cathode in methanol/acetic acid and gives an excellent selectivity under very mild conditions.

Synthesis and biological activity of a ketomethylene analogue of a tripeptide inhibitor of angiotensin converting enzyme

An analogue of a tripeptide inhibitor of angiotensin converting enzyme, Bz-Phe-Gly-Pro, has been synthesized in which the amide bond connecting phenylalanine and glycine has been replaced by a ketomethylene group. This nonpeptide analogue, 20, shows more potent converting enzyme inhibiting activity, I50=0.07 μM, than Bz-Phe-Gly-Pro, I50=9.4 μM, or than the orally active D-3-mercapto-2-methylpropanoyl-L-proline (captopril, 1)I50=0.30 μM. Compound 20 has a K(i)of 1.06 x 10-7 and either competitive or noncompetitive enzyme kinetics depending on what substrate is used in the converting enzyme assay. In tests for inhibition of angiotensin I induced contractions in the guinea pig ileum, 20 has one-tenth the activity of 1.