7625-57-2

Usage

Uses

Used in Peptide Synthesis:
BOC-PHE-GLY-OME is used as a building block in peptide synthesis for its ability to be easily incorporated into peptides. The BOC protecting group ensures that the compound can be added to the growing peptide chain without unwanted side reactions, and it can be removed under mild conditions once the desired peptide sequence is achieved.
Used in Drug Development:
BOC-PHE-GLY-OME is utilized as a potential candidate in drug development due to its unique structure and properties. Its role as a synthetic derivative of phenylalanine and glycine allows it to be explored for therapeutic applications, particularly in the design of novel peptide-based drugs.
Used in Biochemistry and Molecular Biology Research:
In the field of biochemistry and molecular biology, BOC-PHE-GLY-OME serves as a research tool for studying peptide synthesis mechanisms, protein structure, and function. Its ease of incorporation and removal from peptides makes it an ideal compound for investigating various biological processes and interactions.

Upstream product

• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 5680-79-5 glycine ethyl ester hydrochloride 
• 50903-54-3 N-[(1,1-dimethylethoxy)carbonyl]-L-phenylalanine pentafluorophenyl ester 
• 616-34-2 methoxycarbonylmethylamine 
• 543-27-1 isobutyl chloroformate 
• 24424-99-5 di-tert-butyl dicarbonate 
• 63-91-2 L-phenylalanine 
• 35909-82-1 2,3,4,6-tetra-O-benzyl-1-O-(N-tert-butoxycarbonyl-L-phenylalanyl)-β-D-glucopyranose 
• 74293-09-7 2-tert-Butoxycarbonylamino-3-phenyl-propionic acid (2S,3R,4S,5S,6R)-3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yl ester 
• 81000-39-7 (S)-2-((tert-butoxycarbonyl)amino)-3-phenylpropanethioic S-acid 
• 91127-04-7 Boc-Phe-O-CO-i-Bu 
• 67729-36-6 Boc-Phe-O-COO-isoBu 

Downstream Products

• 25616-33-5 2-((2S)-2-((tert-butoxycarbonyl)amino)-3-phenylpropanamido)acetic acid 
• 65559-51-5 L-Phenylalaninyl-glycine methyl ester 
• 66876-64-0 Boc-Phe-Phe-Gly-OMe 
• 73148-98-8 Boc-Phe-Gly-Leu-Met-NH₂ 
• 66489-65-4 Boc-Phe-Gly-NHNH₂ 
• 7625-59-4 L-phenylalanylglycine methyl ester hydrochloride 
• 87976-65-6 (S)-tert-butyl (1-((2-hydroxyethyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate 
• 105224-79-1 H-Phe-Gly-OMe*TFA 
• 76982-22-4 cyclo-N,N'-diacetyl- 
• 5037-75-2 cyclo(Gly-Phe) 
• 161323-92-8 (tert-butoxycarbonyl)-D-tyrosyl-L-phenylalanylglycine 
• 113807-28-6 N-Boc-D-alanyl-L-phenylalanyl-glycine methyl ester 

Relevant academic research and scientific papers

Pd-Catalysed oxidative carbonylation of α-amino amides to hydantoins under mild conditions

The first example of palladium-catalysed oxidative carbonylation of unprotected α-amino amides to hydantoins is described here. The selective synthesis of the target compounds was achieved under mild conditions (1 atm of CO), without ligands and bases. The catalytic system overrode the common reaction pathway that usually leads instead to the formation of symmetrical ureas.

Gram-Scale Synthesis of a Hexapeptide by Fragment Coupling in a Ball Mill

Synthesis of long peptides is generally considered as a challenge to peptide chemists, in addition to producing significant amounts of toxic waste, such as DMF. Here we show that using solvent-less methods, such as ball milling, enabled the production of

Synthesis, in vitro ADME profiling and in vivo pharmacological evaluation of novel glycogen phosphorylase inhibitors

A small set of indole-2-carboxamide derivatives identified from a high-throughput screening campaign has been described as a novel, potent, and glucose-sensitive inhibitors of glycogen phosphorylase a (GPa). Among this series of compounds, compound 2 exhibited moderate GP inhibitory activity (IC50 = 0.29 μM), good cellular efficacy (IC50 = 3.24 μM for HepG2 cells and IC50 = 7.15 μM for isolated rat hepatocytes), together with good absorption, distribution, metabolism, and elimination (ADME) profiles. The in vivo animal study revealed that compound 2 significantly inhibited an increase of fasting blood glucose level in adrenaline-induced diabetic mice.

Engineered Substrate for Cyclooxygenase-2: A Pentapeptide Isoconformational to Arachidonic Acid for Managing Inflammation

Beyond the conventional mode of working of anti-inflammatory agents through enzyme inhibition, herein, COX-2 was provided with an alternate substrate. A proline-centered pentapeptide isoconformational to arachidonic acid, which exhibited appreciable selectivity for COX-2, overcoming acetic acid- and formalin-induced pain in rats to almost 80%, was treated as a substrate by the enzyme. Remarkably, COX-2 metabolized the pentapeptide into small fragments consisting mainly of di- and tripeptides that ensured the safe breakdown of the peptide under in vivo conditions. The kinetic parameter Kcat/Km for COX-2-mediated metabolism of the peptide (6.3 × 105 M-1 s-1) was quite similar to 9.5 × 105 M-1 s-1 for arachidonic acid. Evidenced by the molecular dynamic studies and the use of Y385F COX-2, it was observed that the breakage of the pentapeptide has probably been taken place through H-bond activation of the peptide bond by the side chains of Y385 and S530.

Synthesis and Analysis of Natural-Product-Like Macrocycles by Tandem Oxidation/Oxa-Conjugate Addition Reactions

As traditional small-molecule drug discovery programs focus on a relatively narrow range of chemical space, most human proteins are viewed as unreachable targets. Consequently, there is a strong interest in expanding the chemical space in drug discovery b

Phosphorus pentoxide for amide and peptide bond formation with minimal by-products

Phosphorus pentoxide and DMAP are used for amide bond formation from carboxylic acids and amines. Dipeptides and amides have been synthesized using this reagent in 42–77% yields and >99% ees. The protocol is attractive as it occurs at ambient temperature, the formation of organic by-products is minimal and the reagent can be readily quenched using water. Furthermore, excellent enantioselectivities are observed without the use of harsh triazole based additives.

Diphenylsilane as a coupling reagent for amide bond formation

A simple procedure for amide bond formation using diphenylsilane as a coupling reagent is described. This methodology enables the direct coupling of carboxylic acids with primary and secondary amines, releasing only hydrogen and a siloxane as by-products. Only one equivalent of each partner is needed, providing a more sustainable amidation method producing minimal wastes. This methodology was also extended to the synthesis of peptides and lactams by addition of Hünig's base (DIPEA) and 4-dimethylaminopyridine (DMAP).

Aggregation propensity of amyloidogenic and elastomeric dipeptides constituents

This study demonstrates the self-assembly of N- and C-terminal protected dipeptides Phe–Gly and Pro–Gly which were derived from amyloidogenic and elastomeric peptide sequences. These constituents afforded nanostructured supramolecular ensembles through va

RIBOSOME-MEDIATED INCORPORATION OF PEPTIDES AND PEPTIDOMIMETICS

Modified ribosomes that were selected using a dipeptidyl-puromycin aminonucleoside are used to mediate site-specific incorporation of one or more peptides and peptidomimetics into protein in a cell free translation system. In addition, new fluorescent dipeptidomimetics have been synthesized and incorporated into proteins, as well as modified proteins containing one or more non-naturally occurring dipeptides.

Peptide Mechanosynthesis by Direct Coupling of N-Protected α-Amino Acids with Amino Esters

In view of developing alternatives to classical peptide synthesis strategies that suffer from low efficacy and negative environmental impact, the reactivity of N-protected α-amino acids, amino esters, and N-ethyl-N′-(3-dimethylaminopropyl)carbodiimide was