4817-95-2

Usage

Uses

Used in Pharmaceutical Research and Development:
Z-VAL-PHE-OME is used as a research compound for exploring its therapeutic potential in various health conditions. Its unique combination of amino acids and the O-methyl ester suggests possible applications in the treatment of muscle-related disorders, tissue repair processes, and neurological conditions.
Used in Muscle Health Applications:
Z-VAL-PHE-OME is used as a muscle health supplement due to its valine content, which is essential for muscle metabolism and repair. Z-VAL-PHE-OME may support the development of treatments aimed at enhancing muscle function and recovery.
Used in Tissue Repair Applications:
The presence of valine in Z-VAL-PHE-OME makes it a candidate for use in tissue repair applications. It may be utilized in the development of therapies that promote healing and regeneration of damaged tissues.
Used in Neurological Disorder Treatment:
Z-VAL-PHE-OME is used as a component in the research of neurological disorder treatments, capitalizing on phenylalanine's role in neurotransmitter production. Z-VAL-PHE-OME may contribute to the development of drugs targeting brain health and the treatment of neurological conditions.
Used in Drug Delivery Systems:
Considering the potential impact of the O-methyl ester on bioavailability and pharmacokinetics, Z-VAL-PHE-OME may be employed in the design of drug delivery systems. These systems could improve the compound's effectiveness and targeting in therapeutic applications.

Upstream product

• 1149-26-4 (S)-N-(benzyloxycarbonyl)valine 
• 2577-90-4 methyl (2S)-2-amino-3-phenylpropanoate 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 69472-89-5 N-(Benzyloxycarbonyl)-L-valin-2-pyridylester 
• 63-91-2 L-phenylalanine 
• 1149-26-4 N-benzyloxycarbonylvaline 
• 541-41-3 chloroformic acid ethyl ester 
• 124-38-9 carbon dioxide 
• 803653-50-1 Valyl-phenylalanin-methylester 
• 100-39-0 benzyl bromide 
• 67-56-1 methanol 
• 96031-66-2 Cbz-Val-Phe-NH₂ 
• 33857-66-8 N-benzyloxycarbonyl-L-valine 2-pyridylthiol ester 
• 54647-77-7 N-[(benzyloxy)carbonyl]-L-valine, compound with dicyclohexylamine (1:1) 

Downstream Products

• 39614-17-0 L-valyl-L-phenylalanine methyl ester 
• 79259-44-2 N-cbz-L-Val-L-Phe-L-Leu-NH₂ 
• 25460-78-0 N-cbz-L-Val-L-Phe-OEt 
• 35590-86-4 (3S,6S)-3-(1-methylethyl)-6-(phenylmethyl)piperazine-2,5-dione 
• 55260-14-5 N-<(2-Hydroxy-1-naphthyl)methylene>-(S)-valyl-(S)-phenylalanine methyl ester 
• 143508-83-2 Dbs-S-Val-S-Phe-OMe 
• 131697-40-0 Boc-Asn-Arg(Mts)-Val-Arg-(Mts)-Val-Phe-OMe 
• 131697-37-5 Z-Arg(Mts)-Val-Phe-OMe 
• 131697-38-6 Z-Val-Arg(Mts)-Val-Phe-OMe 
• 131696-83-8 H-Asn-Arg-Val-Arg-Val-Phe-OMe*3AcOH 
• 131697-39-7 Z-Arg(Mts)-Val-Arg(Mts)-Val-Phe-OMe 
• 19542-51-9 N-benzyloxycarbonyl-L-valyl-L-phenylalanine 
• 879125-75-4 N-(N-benzyloxycarbonyl-valyl)-phenylalanine 

Relevant academic research and scientific papers

A Quick Route to Multiple Highly Potent SARS-CoV-2 Main Protease Inhibitors**

The COVID-19 pathogen, SARS-CoV-2, requires its main protease (SC2MPro) to digest two of its translated long polypeptides to form a number of mature proteins that are essential for viral replication and pathogenesis. Inhibition of this vital pr

Optimization and anti-cancer properties of fluoromethylketones as covalent inhibitors for ubiquitin C-terminal hydrolase L1

The deubiquitinating enzyme (DUB) UCHL1 is implicated in various disease states including neurodegenerative disease and cancer. However, there is a lack of quality probe molecules to gain a better understanding on UCHL1 biology. To this end a study was carried out to fully characterize and optimize the irreversible covalent UCHL1 inhibitor VAEFMK. Structure-activity relationship studies identified modifications to improve activity versus the target and a full cellular characterization was carried out for the first time with this scaffold. The studies produced a new inhibitor, 34, with an IC50 value of 7.7 μM against UCHL1 and no observable activity versus the closest related DUB UCHL3. The molecule was also capable of selectively inhibiting UCHL1 in cells and did not demonstrate any discernible off-target toxicity. Finally, the molecule was used for initial probe studies to assess the role of UCHL1 role in proliferation of myeloma cells and migration behavior in small cell lung cancer cells making 34 a new tool to be used in the biological evaluation of UCHL1.

Chemoselective synthesis of carbamates using CO2 as carbon source

Synthesis of carbamates directly from amines using CO2 as the carbon source is a straightforward and sustainable approach. Herein, we describe a highly effective and chemoselective methodology for the synthesis of carbamates at room temperature and atmosp

Fully enzymatic N→C-directed peptide synthesis using C-terminal peptide α-carboxamide to ester interconversion

Chemoenzymatic peptide synthesis is potentially the most cost-efficient technology for the synthesis of short and medium-sized peptides with some important advantages. For instance, stoichiometric amounts of expensive coupling reagents are not required and racemisation does not occur rendering purification easier compared to chemical peptide synthesis. In this paper, a novel interconversion reaction of peptide C-terminal α-carboxamides into primary alkyl esters with alcalase was used to develop a fully enzymatic peptide synthesis strategy. For each elongation step a cost-efficient amino acid carboxamide building block was used followed by the interconversion of the elongated peptide carboxamide to the corresponding primary alkyl ester. These peptide esters are the starting materials for the next enzymatic peptide elongation step. Copyright

Expeditious amide-forming reactions using thiol esters

The reaction of a 2-pyridylthiol ester with a dimethylaluminum amide leads to the rapid formation of the corresponding amide. The tolylthiol esters can be activated with silver trifluoroacetate and coupled even with poorly reactive amino compounds. (C) 20

Peptide-titanium complex as catalyst for asymmetric addition of hydrogen cyanide to aldehyde

The complex of titanium ethoxide and an acyclic dipeptide ester whose terminal amino group is modified to a salicylal-type Schiff base catalyzes the asymmetric addition of hydrogen cyanide to aldehydes with high enantioselectivity. In the reaction of benzaldehyde and hydrogen cyanide, (R)-mandelonitrile is obtained with an enantiomeric excess of 90% when N-((2-hydroxy-1-naphthyl)methylene)-(S)-valyl-(S)-tryptophan methyl ester is employed. In place of the dipeptide, the amide derivatives of an amino acid modified by substituted salicylaldehyde, such as N-(3,5-dibromosalicylidene)-(S)-valine piperidide, exhibit an entirely opposite stereoselectivity to yield S-cyanohydrins with optical purities up to 97% ee. This novel peptide-titanium complex, therefore, enables us to afford optically active cyanohydrins of both absolute configurations by using natural S-amino acids as chiral auxiliaries.

KINETICS OF THE ALKALINE HYDROLYSIS OF SEVERAL N-BENZYLOXYCARBONYLDIPEPTIDE METHYL AND ETHYL ESTERS

The reaction rates of the alkaline hydrolysis of synthesized N-protected dipeptide methyl and ethyl esters were studied systematically.From the kinetic data the energies of activation, the pre-exponential factors and the reference values at 40 deg C were calculated.The rate of hydrolysis shows to be strongly dependent on the C-terminal amino acid in the sequence Gly >> Ala/Met/Phe > Leu >> Val/Pro.Surprisingly the N-terminal amino acid also exerts an effect, but in a different sequence.N-Terminal Phe in particular shows a relative accelerating effect.Remarkable is the significantly faster ester hydrolysis of glycine containing dipeptide ethyl esters in ethanol/water compared to the corresponding methyl esters in methanol/water.

2(1H)-Pyridone as Leaving Group in Acylation Reactions - Applications in Peptide Synthesis

Alkyl 2-pyridyl carbonates 3 or mixtures of 3 and the isomeric N-(alkoxycarbonyl)-2-pyridones 3' are useful for the introduction of urethane protective groups into amino acids.The N-protected amino acids 7 - 10 react with 2(1H)-pyridone (1a) using the carbodiimide method to yield 2-pyridyl active esters 11, which easily undergo coupling reactions with amino acid esters 12 with elimination of 1a to give peptides 13 in good yields as well as high optical purities.

Peptide Synthesis by Means of Immobilized Enzymes. I. Immobilized α-Chimotripsin

α-Chymotrypsin covalently bound to silica, enzacryl AA, and enzacryl AH catalyzes peptide bond formation between N-protected dipeptide methyl esters and H-Leu-NH2 with results similar to those with the free enzyme.The influence of water-miscible and water